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}\viewkind1\viewscale100\margl0\margr0\margt0\margb0\deftab80\dntblnsbdb\expshrt
n\paperw9840\paperh13340\pard\sb0\sl-240{\bkmkstart Pg1}{\bkmkend Pg1}\par\pard\
ql \li1231\sb0\sl-207\slmult0 \par\pard\ql\li1231\sb0\sl-207\slmult0 \par\pard\q
l\li1231\sb95\sl-207\slmult0 \up0 \expndtw-3\charscalex100 \ul0\nosupersub\cf1\f
2\fs18 J. Basic Microbiol. \ul0\nosupersub\cf2\f3\fs18 40\ul0\nosupersub\cf1\f2\
fs18 (2000) 2, 83 - 92 \par\pard\qj \li1231\sb0\sl-200\slmult0 \par\pard\qj\li1
231\sb0\sl-200\slmult0 \par\pard\qj\li1231\sb0\sl-200\slmult0 \par\pard\qj\li123
1\ri1037\sb99\sl-200\slmult0 \up0 \expndtw0\charscalex103 (Departamento de Biolo
gia - Faculdade de Filosofia Cincias e Letras de Ribeiro Preto - Uni\up0 \expndt
w0\charscalex105 versidade de So Paulo; \ul0\super\cf3\f4\fs18 1\ul0\nosupersub\
cf1\f2\fs18 Centro de Qumica de Protenas and Departamento de Ginecologia e \up0 \e
xpndtw-2\charscalex100 Obstetrcia - Faculdade de Medicina de Ribeiro Preto - Unive
rsidade de So Paulo) \par\pard\ql \li1231\sb241\sl-345\slmult0 \up0 \expndtw0\cha
rscalex97 \ul0\nosupersub\cf4\f5\fs30 Glucoamylase activity from the thermophili
c fungus \par\pard\ql \li1231\sb15\sl-345\slmult0 \up0 \expndtw0\charscalex97 \u
l0\nosupersub\cf5\f6\fs30 Scytalidium thermophilum. \par\pard\ql \li1231\sb0\sl340\slmult0 \up0 \expndtw0\charscalex97 \ul0\nosupersub\cf4\f5\fs30 Biochemical
and regulatory properties \par\pard\qj \li1231\ri1046\sb180\sl-220\slmult0 \up0
\expndtw-2\charscalex100 \ul0\nosupersub\cf6\f7\fs20 M\ul0\nosupersub\cf7\f8\fs1
6 ARIANA \ul0\nosupersub\cf6\f7\fs20 C\ul0\nosupersub\cf7\f8\fs16 EREIA\ul0\nosu
persub\cf6\f7\fs20 , H\ul0\nosupersub\cf7\f8\fs16 CTOR \ul0\nosupersub\cf6\f7\fs2
0 F. T\ul0\nosupersub\cf7\f8\fs16 ERENZI\ul0\nosupersub\cf6\f7\fs20 , J\ul0\nosu
persub\cf7\f8\fs16 OO \ul0\nosupersub\cf6\f7\fs20 A. J\ul0\nosupersub\cf7\f8\fs16
ORGE\ul0\nosupersub\cf6\f7\fs20 , L\ul0\nosupersub\cf7\f8\fs16 EWIS \ul0\nosupe
rsub\cf6\f7\fs20 J. G\ul0\nosupersub\cf7\f8\fs16 REENE\ul0\super\cf3\f4\fs18 1\u

l0\nosupersub\cf6\f7\fs20 , J\ul0\nosupersub\cf7\f8\fs16 OSE \ul0\nosupersub\cf6

\f7\fs20 C. R\ul0\nosupersub\cf7\f8\fs16 OSA\ul0\super\cf3\f4\fs18 1 \up0 \expnd
tw-3\charscalex100 \ul0\nosupersub\cf6\f7\fs20 and\ul0\nosupersub\cf7\f8\fs16 \
ul0\nosupersub\cf6\f7\fs20 M\ul0\nosupersub\cf7\f8\fs16 ARIA \ul0\nosupersub\cf6
\f7\fs20 D\ul0\nosupersub\cf7\f8\fs16 E \ul0\nosupersub\cf6\f7\fs20 L\ul0\nosupe
rsub\cf7\f8\fs16 OURDES \ul0\nosupersub\cf6\f7\fs20 T. M. P\ul0\nosupersub\cf7\f
8\fs16 OLIZELI \par\pard\ql \li1231\sb0\sl-207\slmult0 \par\pard\ql\li1231\sb164
\sl-207\slmult0 \up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf8\f9\fs18 (Recei
ved 01 September 1999/Accepted 08 November 1999) \par\pard\ql \li1231\sb173\sl-2
07\slmult0 \up0 \expndtw-3\charscalex100 \ul0\nosupersub\cf1\f2\fs18 A glucoamyl
ase activity produced by the thermophilic fungus \ul0\nosupersub\cf8\f9\fs18 Scy
talidium thermophilum \ul0\nosupersub\cf1\f2\fs18 was purified \par\pard\qj \li1
231\ri1025\sb0\sl-193\slmult0 \up0 \expndtw-1\charscalex100 6.8-fold by ion exch
ange chromatography. The protein exhibited a molecular mass of about 86 kDa \lin
e \up0 \expndtw-1\charscalex100 (7% PAGE and SDS-PAGE), or 68.5 kDa (Bio Sil SEC
-400 FPLC). The pI of the enzyme was 8.4. \line \up0 \expndtw0\charscalex100 Opt
ima of pH and temperature, with starch or maltose as substrates were, 6.5/60 C
and 5.0/55 C, \line \up0 \expndtw-1\charscalex100 respectively. The enzyme had
a half-life of 22 min at 55 C with starch as substrate, and it was fully \line
\up0 \expndtw0\charscalex100 stable with maltose. Maltase activity was activated
by 10 m\ul0\nosupersub\cf9\f10\fs14 M\ul0\nosupersub\cf1\f2\fs18 Ba\ul0\super\
cf3\f4\fs18 ++\ul0\nosupersub\cf1\f2\fs18 (7.8%); Mn\ul0\super\cf3\f4\fs18 ++\u
l0\nosupersub\cf1\f2\fs18 (12.4%) or Mg\ul0\super\cf3\f4\fs18 ++ \line \up0 \ex
pndtw-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18 (28%). The enzyme contained ap
proximately 25.5% carbohydrate. \ul0\nosupersub\cf8\f9\fs18 K\ul0\sub\cf3\f4\fs1
8 m\ul0\nosupersub\cf1\f2\fs18 and \ul0\nosupersub\cf8\f9\fs18 V\ul0\sub\cf3\f4
\fs18 max\ul0\nosupersub\cf1\f2\fs18 values for starch and \line \up0 \expndtw1\charscalex100 maltose were 0.28 mg/ml, 67.2 U/mg protein and 1.40 mg/ml, 5.61
U/mg protein, respectively. The \line \up0 \expndtw0\charscalex100 products of h
ydrolysis of starch, detected by thin layer chromatography, showed only glucose
after \line \up0 \expndtw0\charscalex103 30 min, indicating a glucoamylase activ
ity. The amino terminal sequence of the purified protein \line \up0 \expndtw-1\c
harscalex100 showed 93% homology with a glucoamylase activity purified from \ul0
\nosupersub\cf8\f9\fs18 Humicola grisea\ul0\nosupersub\cf1\f2\fs18 var. \ul0\no
supersub\cf8\f9\fs18 thermoidea\ul0\nosupersub\cf1\f2\fs18 . \par\pard\qj \li123
1\sb0\sl-213\slmult0 \par\pard\qj\li1231\ri1023\sb3\sl-213\slmult0 \up0 \expndtw
0\charscalex103 \ul0\nosupersub\cf6\f7\fs20 Biotechnological industries show inc
reasing interest in the use of microbial sources of \line \up0 \expndtw-2\charsc
alex100 amylolytic activity (V\ul0\nosupersub\cf7\f8\fs16 IHINEN\ul0\nosupersub\
cf6\f7\fs20 and M\ul0\nosupersub\cf7\f8\fs16 NTSL\ul0\nosupersub\cf6\f7\fs20 1989
, G\ul0\nosupersub\cf7\f8\fs16 UZMN\ul0\nosupersub\cf6\f7\fs20 -M\ul0\nosupersub\
cf7\f8\fs16 ALDONADO\ul0\nosupersub\cf6\f7\fs20 and P\ul0\nosupersub\cf7\f8\fs1
6 AREDEZ\ul0\nosupersub\cf6\f7\fs20 -\line \up0 \expndtw0\charscalex100 L\ul0\no
supersub\cf7\f8\fs16 PEZ\ul0\nosupersub\cf6\f7\fs20 1995, C\ul0\nosupersub\cf7\f
8\fs16 RABB \ul0\nosupersub\cf6\f7\fs20 and M\ul0\nosupersub\cf7\f8\fs16 ITCHINS
ON\ul0\nosupersub\cf6\f7\fs20 1997, J\ul0\nosupersub\cf7\f8\fs16 AMES\ul0\nosup
ersub\cf6\f7\fs20 and L\ul0\nosupersub\cf7\f8\fs16 EE\ul0\nosupersub\cf6\f7\fs2
0 1997). For instance, glucoa-\line \up0 \expndtw-1\charscalex100 mylase [ \up0
\expndtw-1\charscalex100 (1,4)-\ul0\nosupersub\cf7\f8\fs16 D\ul0\nosupersub\cf6
\f7\fs20 -glucan glucohydrolase, EC 3.2.1.3] activity, which attacks \up0 \expn
dtw-1\charscalex100 -1,4 link-\par\pard\ql \li1231\sb1\sl-197\slmult0\tx7235 \up
0 \expndtw0\charscalex102 ages from the nonreducing end of starch, releasing \ul
0\nosupersub\cf7\f8\fs16 D\ul0\nosupersub\cf6\f7\fs20 -glucose in the \tab \up0
\expndtw-2\charscalex100 -configuration, is \par\pard\qj \li1231\ri1023\sb4\sl-2
20\slmult0 \up0 \expndtw-3\charscalex100 widely used for the production of highglucose (96 to 98% glucose) and high-fructose (55% \up0 \expndtw-4\charscalex100
fructose) syrups. \par\pard\qj \li1231\ri1022\sb0\sl-215\slmult0\fi193 \up0 \ex
pndtw-1\charscalex100 Thermophilic microorganisms are regarded as an attractive
source of thermostable amy-\line \up0 \expndtw-2\charscalex100 lolytic enzymes,
for industrial use (T\ul0\nosupersub\cf7\f8\fs16 OSI \ul0\nosupersub\cf10\f11\fs

20 et al.\ul0\nosupersub\cf6\f7\fs20 1993, A\ul0\nosupersub\cf7\f8\fs16 LMEIDA

\ul0\nosupersub\cf10\f11\fs20 et al. \ul0\nosupersub\cf6\f7\fs20 1995, K\ul0\nos
upersub\cf7\f8\fs16 ADOWAKI \ul0\nosupersub\cf10\f11\fs20 et al. \line \up0 \exp
ndtw-2\charscalex100 \ul0\nosupersub\cf6\f7\fs20 1996, M\ul0\nosupersub\cf7\f8\f
s16 ISHRA \ul0\nosupersub\cf6\f7\fs20 and M\ul0\nosupersub\cf7\f8\fs16 AHESHWARI
\ul0\nosupersub\cf6\f7\fs20 1996, P\ul0\nosupersub\cf7\f8\fs16 OLIZELI \ul0\nos
upersub\cf10\f11\fs20 et al\ul0\nosupersub\cf6\f7\fs20 . 1996, B\ul0\nosupersub\
cf7\f8\fs16 USCH \ul0\nosupersub\cf10\f11\fs20 et al.\ul0\nosupersub\cf6\f7\fs20
1997, B\ul0\nosupersub\cf7\f8\fs16 UAINAIN \line \up0 \expndtw0\charscalex100
\ul0\nosupersub\cf10\f11\fs20 et al. \ul0\nosupersub\cf6\f7\fs20 1998, V\ul0\nos
upersub\cf7\f8\fs16 AN \ul0\nosupersub\cf6\f7\fs20 D\ul0\nosupersub\cf7\f8\fs16
EN \ul0\nosupersub\cf6\f7\fs20 B\ul0\nosupersub\cf7\f8\fs16 URG \ul0\nosupersub\
cf10\f11\fs20 et al. \ul0\nosupersub\cf6\f7\fs20 1998). In the present study we
describe an extracellular \line \up0 \expndtw-3\charscalex100 glucoamylase activ
ity produced by \ul0\nosupersub\cf10\f11\fs20 Scytalidium\ul0\nosupersub\cf11\f1
2\fs20 \ul0\nosupersub\cf10\f11\fs20 thermophilum\ul0\nosupersub\cf6\f7\fs20 ,
a fungus isolated from phase \line \up0 \expndtw-1\charscalex100 II of mushroom
compost soil (S\ul0\nosupersub\cf7\f8\fs16 TRAATSMA \ul0\nosupersub\cf6\f7\fs20
and S\ul0\nosupersub\cf7\f8\fs16 AMSON \ul0\nosupersub\cf6\f7\fs20 1993). We des
cribe an optimised \line \up0 \expndtw0\charscalex100 medium for the enzyme prod
uction, and some of its biochemical properties. This enzyme \line \up0 \expndtw2\charscalex100 was partially sequenced at the amino terminus, which showed homo
logy with a glucoamy-\line \up0 \expndtw-3\charscalex100 lase produced by the th
ermophilic fungus \ul0\nosupersub\cf10\f11\fs20 Humicola grisea\ul0\nosupersub\c
f6\f7\fs20 var. \ul0\nosupersub\cf10\f11\fs20 thermoidea\ul0\nosupersub\cf6\f7\
fs20 . \par\pard\ql \li1231\sb0\sl-230\slmult0 \par\pard\ql\li1231\sb148\sl-230\
slmult0 \up0 \expndtw-4\charscalex100 \ul0\nosupersub\cf12\f13\fs20 Materials an
d methods \par\pard\qj \li1231\ri1031\sb155\sl-200\slmult0\fi0 \up0 \expndtw-1\c
harscalex100 \ul0\nosupersub\cf2\f3\fs18 Organism and growth conditions:\ul0\nos
upersub\cf8\f9\fs18 Scytalidium thermophilum\ul0\nosupersub\cf13\f14\fs18 \ul0
\nosupersub\cf1\f2\fs18 (15.8) [= CBS 671.88 = ATCC 66938] \line \up0 \expndtw0\
charscalex100 was maintained at 45 C, in slants of solid 4% oatmeal baby food (
Q\ul0\nosupersub\cf9\f10\fs14 UAKER\ul0\nosupersub\cf1\f2\fs18 ) medium. Conidia
from \line \up0 \expndtw-3\charscalex100 10-day-old cultures were inoculated in
to 125 ml E\ul0\nosupersub\cf9\f10\fs14 RLENMEYER\ul0\nosupersub\cf1\f2\fs18 fl
asks containing 25 ml liquid medium: \par\pard\ql \li1231\sb1\sl-175\slmult0 \up
0 \expndtw-2\charscalex100 0.1% calcium carbonate; 0.6% yeast extract; 0.1% pept
one; 1.0% sodium chloride; 0.6% ammonium
{\shp {\*\shpinst\shpleft20\shptop0\shpright9839\shpbottom13340\shpfhdr0\shpbxpa
ge\shpbypage\shpwr3\shpwrk0\shpfblwtxt1\shpz5\shplid0
{\sp{\sn shapeType}{\sv 0}}{\sp{\sn fFlipH}{\sv 0}}{\sp{\sn fFlipV}{\sv 0}}{\sp{
\sn geoRight}{\sv 9819}}{\sp{\sn geoBottom}{\sv 13340}}
{\sp{\sn pVerticies}{\sv 8;5;(0,0);(0,0);(9819,0);(9819,13340);(0,13340)}}
{\sp{\sn pSegmentInfo}{\sv 2;12;16384;45824;1;45824;1;45824;1;45824;1;45824;2457
7;32768}}
{\sp{\sn fFillOK}{\sv 1}}{\sp{\sn fFilled}{\sv 1}}{\sp{\sn fillColor}{\sv 167772
15}}{\sp{\sn fLine}{\sv 0}}{\sp{\sn lineType}{\sv 0}}{\sp{\sn fArrowheadsOK}{\sv
1}}{\sp{\sn fBehindDocument}{\sv 1}}{\sp{\sn lineColor}{\sv 0}}
}}\par\pard\sect\sectd\fs24\paperw9840\paperh13340\pard\sb0\sl-240{\bkmkstart Pg
2}{\bkmkend Pg2}\par\pard\li1231\sb0\sl-230\slmult0\par\pard\li1231\sb0\sl-230\s
lmult0\par\pard\li1231\sb20\sl-230\slmult0\fi0\tx7874 \up0 \expndtw-2\charscalex
100 \ul0\nosupersub\cf6\f7\fs20 84\tab \up0 \expndtw-2\charscalex100 \ul0\nosupe
rsub\cf1\f2\fs18 M. C\ul0\nosupersub\cf9\f10\fs14 EREIA\par\pard\qj \li1231\sb0\
sl-192\slmult0 \par\pard\qj\li1231\ri1036\sb20\sl-192\slmult0\fi0 \up0 \expndtw0
\charscalex100 \ul0\nosupersub\cf1\f2\fs18 acetate and 1.0% cassava flour, pH 6.
0. The cultures were incubated at 45 C without agitation. After \up0 \expndtw0\
charscalex100 seven days of incubation, when glucoamylase activity reache
d a maximum, the cultures were \up0 \expndtw0\charscalex104 harvested by fi
ltration and the filtrate was saved as a source of crude extracellular glucoamyl

ase. \up0 \expndtw-1\charscalex100 Mycelial pads were ground with sea sand, at 0
C with ten vol. of cold 100 m\ul0\nosupersub\cf9\f10\fs14 M\ul0\nosupersub\cf1
\f2\fs18 sodium acetate buffer, \up0 \expndtw0\charscalex103 pH 5.5 (buffer A).
After centrifugation (20,000
g,\ul0\nosupersub\cf14\f15\fs18 \ul0\nosupersu
b\cf1\f2\fs18 20 min, 4 C) the supernatant fraction was the \up0 \expndtw-2\cha
rscalex100 source of intracellular enzyme. \par\pard\qj \li1231\sb0\sl-191\slmu
lt0 \par\pard\qj\li1231\ri1034\sb18\sl-191\slmult0\fi0 \up0 \expndtw0\charscalex
100 \ul0\nosupersub\cf2\f3\fs18 Enzymatic assays, determination of protein and n
eutral carbohydrate:\ul0\nosupersub\cf8\f9\fs18 \ul0\nosupersub\cf1\f2\fs18 Glu
coamylase activity \up0 \expndtw-1\charscalex100 was assayed at 60 C, in a reac
tion mixture containing 0.2 ml of diluted enzyme and 0.2 ml of 1.0% \up0 \expndt
w-3\charscalex100 starch in 100 m\ul0\nosupersub\cf9\f10\fs14 M\ul0\nosupersub\c
f1\f2\fs18 sodium acetate buffer, pH 5.5. The amount of glucose released was es
timated by the \up0 \expndtw-2\charscalex100 glucose oxidase procedure (B\ul0\no
supersub\cf9\f10\fs14 ERGMEYER\ul0\nosupersub\cf1\f2\fs18 and B\ul0\nosupersub\
cf9\f10\fs14 ERNT\ul0\nosupersub\cf1\f2\fs18 1974). Maltase activity was assaye
d as described \up0 \expndtw-1\charscalex100 above, except that 1.7% maltose was
used as substrate. An enzyme unit is the amount that produces \up0 \expndtw0\ch
arscalex100 1 mol of glucose per minute. Protein was determined by the method o
f L\ul0\nosupersub\cf9\f10\fs14 OWRY\ul0\nosupersub\cf1\f2\fs18 \ul0\nosupersub
\cf8\f9\fs18 et al.\ul0\nosupersub\cf1\f2\fs18 (1951). Total \up0 \expndtw0\cha
rscalex100 neutral carbohydrate was quantified by the phenol sulphuric acid meth
od of D\ul0\nosupersub\cf9\f10\fs14 UBOIS\ul0\nosupersub\cf1\f2\fs18 \ul0\nosup
ersub\cf8\f9\fs18 et al.\ul0\nosupersub\cf1\f2\fs18 (1956), \up0 \expndtw-2\cha
rscalex100 using \ul0\nosupersub\cf9\f10\fs14 D\ul0\nosupersub\cf1\f2\fs18 -mann
ose as standard. \par\pard\qj \li1231\sb0\sl-180\slmult0 \par\pard\qj\li1231\ri1
032\sb39\sl-180\slmult0 \up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf2\f3\fs1
8 Gel filtration\ul0\nosupersub\cf1\f2\fs18 : The molecular weight of the purifi
ed enzyme was estimated by FPLC using a Bio Sil-\line \up0 \expndtw-3\charscalex
100 SEC-400 filtration column (0.78 \up0 \expndtw-3\charscalex100 30.0 cm) equil
ibrated and eluted with 50 m\ul0\nosupersub\cf9\f10\fs14 M\ul0\nosupersub\cf1\f2
\fs18 Tris-HCl, pH 7.5 plus \par\pard\qj \li1231\ri1037\sb4\sl-200\slmult0\fi0
\up0 \expndtw0\charscalex102 100 m\ul0\nosupersub\cf9\f10\fs14 M\ul0\nosupersub\
cf1\f2\fs18 KCl. The flow rate was 1 ml/min and 1.0 ml fractions were collected
and assayed. Void \line \up0 \expndtw-3\charscalex100 volume \ul0\nosupersub\cf
8\f9\fs18 (Vo)\ul0\nosupersub\cf1\f2\fs18 was determined with Blue Dextran, usi
ng as MW markers \up0 \expndtw-3\charscalex100 -amylase (200 kDa); alcohol \par\
pard\ql \li1231\sb1\sl-175\slmult0 \up0 \expndtw-1\charscalex100 dehydrogenase (
150 kDa); bovine serum albumin (66 kDa) and ovalbumin (45 kDa). \par\pard\qj \li
1231\ri1038\sb185\sl-200\slmult0 \up0 \expndtw-1\charscalex100 \ul0\nosupersub\c
f2\f3\fs18 Electrophoresis and amino acid sequencing\ul0\nosupersub\cf1\f2\fs18
: Non-denaturating PAGE (7.0%) electrophoresis was \line \up0 \expndtw-1\charsca
lex100 carried out by the method of R\ul0\nosupersub\cf9\f10\fs14 EISFIELD\ul0\n
osupersub\cf1\f2\fs18 \ul0\nosupersub\cf8\f9\fs18 et al.\ul0\nosupersub\cf1\f2\
fs18 (1962) and SDS-PAGE (7.0%) according to L\ul0\nosupersub\cf9\f10\fs14 AEMM
LI \line \up0 \expndtw-1\charscalex100 \ul0\nosupersub\cf1\f2\fs18 (1970). MW m
arkers were: \up0 \expndtw-2\charscalex100 -galactosidase \up0 \expndtw-1\charsc
alex100 (116 kDa); phosphorylase-b (97 kDa); bovine serum \par\pard\qj \li1231\
ri1027\sb0\sl-194\slmult0\fi0 \up0 \expndtw0\charscalex100 albumin (66 kDa); ova
lbumin (45 kDa), and carbonic anydrase (29 kDa). Protein was stained with \line
\up0 \expndtw-2\charscalex100 silver (B\ul0\nosupersub\cf9\f10\fs14 LUM\ul0\nosu
persub\cf1\f2\fs18 \ul0\nosupersub\cf8\f9\fs18 et al.\ul0\nosupersub\cf1\f2\fs1
8 1987). Glucoamylase activity was visualised on polyacrylamide gels as describ
ed \line \up0 \expndtw0\charscalex100 by B\ul0\nosupersub\cf9\f10\fs14 ASAVESWAR
A\ul0\nosupersub\cf1\f2\fs18 R\ul0\nosupersub\cf9\f10\fs14 AO\ul0\nosupersub\cf
1\f2\fs18 \ul0\nosupersub\cf8\f9\fs18 et al.\ul0\nosupersub\cf1\f2\fs18 (1981)
. Isoelectric focusing was carried out according to O\u8217?F\ul0\nosupersub\cf9
\f10\fs14 ARRELL \line \up0 \expndtw-3\charscalex100 \ul0\nosupersub\cf8\f9\fs18
et al.\ul0\nosupersub\cf1\f2\fs18 (1977) using Pharmalite pH 8.0 - 10.5. For a
mino acid sequencing the protein was electroblotted \line \up0 \expndtw0\charsca

lex103 onto a PVDF membrane after SDS PAGE. The blotted protein band was submitt
ed to automatic \line \up0 \expndtw0\charscalex104 E\ul0\nosupersub\cf9\f10\fs14
DMAN\ul0\nosupersub\cf1\f2\fs18 degradation. The sequencing was carried out in
a Procise model 491 protein sequencer \line \up0 \expndtw0\charscalex100 (PE-A
pplied Biosystem, Foster city) using gas-phase chemistry with on-line i
dentification of \line \up0 \expndtw-1\charscalex100 phenylthiohydantoin deriva
tive. A 10 picomol standard was used to quantify PTH-amino acids. \par\pard\qj \
li1231\ri1013\sb172\sl-193\slmult0\fi0 \up0 \expndtw0\charscalex102 \ul0\nosuper
sub\cf2\f3\fs18 Chromatography of hydrolysis products:\ul0\nosupersub\cf1\f2\fs1
8 The hydrolysis products of glucoamylase activity on \up0 \expndtw0\charscalex
103 soluble starch or maltose as substrates were analysed by thin-layer chromato
graphy on silica gel \up0 \expndtw-2\charscalex100 (DC-Alufolien Kieselgel 60, M
\ul0\nosupersub\cf9\f10\fs14 ERCK\ul0\nosupersub\cf1\f2\fs18 ). The mobile phase
was: butanol/ethanol/water (5 : 3 : 2, by vol.). \up0 \expndtw-2\charscalex100
Sugars were detected with orcinol (F\ul0\nosupersub\cf9\f10\fs14 ONTANA\ul0\nosu
persub\cf1\f2\fs18 \ul0\nosupersub\cf8\f9\fs18 et al\ul0\nosupersub\cf1\f2\fs18
. 1988). \par\pard\qj \li1231\sb0\sl-190\slmult0 \par\pard\qj\li1231\ri1029\sb2
0\sl-190\slmult0 \up0 \expndtw0\charscalex100 \ul0\nosupersub\cf2\f3\fs18 Chemic
als:\ul0\nosupersub\cf1\f2\fs18 DEAE-cellulose, CM-cellulose, acrylamide an
d molecular weight standards were \line \up0 \expndtw0\charscalex104 purchas
ed from S\ul0\nosupersub\cf9\f10\fs14 IGMA\ul0\nosupersub\cf1\f2\fs18 Chemicals
Co. Maltose was purchased from M\ul0\nosupersub\cf9\f10\fs14 ERCK\ul0\nosupersu
b\cf1\f2\fs18 . Cassava flour was \line \up0 \expndtw-1\charscalex100 manufactur
ed in Maceio, State of Alagoas, Brazil. All other reagents were of analytical g
rade. \par\pard\ql \li1231\sb0\sl-230\slmult0 \par\pard\ql\li1231\sb187\sl-230\s
lmult0 \up0 \expndtw-4\charscalex100 \ul0\nosupersub\cf12\f13\fs20 Results \par\
pard\qj \li1231\ri1022\sb205\sl-213\slmult0 \up0 \expndtw-2\charscalex100 \ul0\n
osupersub\cf6\f7\fs20 The composition of the culture medium (M-5; T\ul0\nosupers
ub\cf7\f8\fs16 OSI \ul0\nosupersub\cf10\f11\fs20 et al.\ul0\nosupersub\cf6\f7\fs
20 1993) was optimised for maximal \up0 \expndtw-2\charscalex100 production and
secretion of glucoamylase activity, by modifying the original concentration, \u
p0 \expndtw-1\charscalex100 or substituting some of its constituents. The enzyme
levels were not significantly affected \up0 \expndtw0\charscalex100 by altering
the concentrations of calcium carbonate, peptone or yeast extract (not shown).
\up0 \expndtw-3\charscalex100 However, glucoamylase production, and principally
its secretion, were markedly stimulated \up0 \expndtw-2\charscalex100 by increas
ing the concentration of sodium chloride above 0.4% (Table 1). In the absence of
\up0 \expndtw0\charscalex102 this salt, the amount of glucoamylase released int
o the medium was approximately one\up0 \expndtw-1\charscalex100 fourth of total
activity, in contrast with cultures grown with 1% of sodium chloride, which \up0
\expndtw0\charscalex100 secreted about 80% of the enzyme. Higher concentrations
of sodium chloride diminished \up0 \expndtw-4\charscalex100 growth and did not
improve further the enzyme production.
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}}\par\pard\sect\sectd\fs24\paperw9840\paperh13340\pard\sb0\sl-240{\bkmkstart Pg
3}{\bkmkend Pg3}\par\pard\li1231\sb0\sl-230\slmult0\par\pard\li1231\sb0\sl-230\s
lmult0\par\pard\li1231\sb65\sl-230\slmult0\fi0\tx8459 \up0 \expndtw-2\charscalex
100 \ul0\nosupersub\cf1\f2\fs18 Glucoamylase from a thermophilic fungus\tab \up0
\expndtw-2\charscalex100 \ul0\nosupersub\cf6\f7\fs20 85\par\pard\li1231\sb166\s
l-207\slmult0\fi0 \up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18 Tabl

e 1\par\pard\li1231\sb1\sl-191\slmult0\fi0 \up0 \expndtw-1\charscalex100 Effect

of NaCl on the production of glucoamylase activity and on the growth of \ul0\nos
upersub\cf8\f9\fs18 Scytalidium thermo-\par\pard\li1231\sb1\sl-192\slmult0\fi0 \
up0 \expndtw-2\charscalex100 philum\par\pard\li1231\sb161\sl-207\slmult0\fi6\tx2
948\tx4944\tx6654 \up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18 NaCl
*\tab \up0 \expndtw-2\charscalex100 Extra\tab \up0 \expndtw-2\charscalex100 Intr
a\tab \up0 \expndtw-2\charscalex100 Protein\par\pard\li1231\sb1\sl-190\slmult0\f
i6\tx2948\tx4944\tx6654 \up0 \expndtw-2\charscalex100 %\tab \up0 \expndtw-2\char
scalex100 (Total U)\tab \up0 \expndtw-2\charscalex100 (Total U)\tab \up0 \expndt
w-2\charscalex100 (Total mg)\par\pard\li1231\sb125\sl-207\slmult0\fi6\tx3039\tx4
944\tx6745 \up0 \expndtw-2\charscalex100 0.0\tab \up0 \expndtw-2\charscalex100 1
.78\tab \up0 \expndtw-2\charscalex100 5.42\tab \up0 \expndtw-2\charscalex100 7.7
5\par\pard\li1231\sb1\sl-190\slmult0\fi6\tx3039\tx4944\tx6654 \up0 \expndtw-2\ch
arscalex100 0.2\tab \up0 \expndtw-2\charscalex100 2.66\tab \up0 \expndtw-2\chars
calex100 6.76\tab \up0 \expndtw-2\charscalex100 11.47\par\pard\li1231\sb1\sl-193
\slmult0\fi6\tx3039\tx4944\tx6654 \up0 \expndtw-2\charscalex100 0.4\tab \up0 \ex
pndtw-2\charscalex100 3.39\tab \up0 \expndtw-2\charscalex100 6.34\tab \up0 \expn
dtw-2\charscalex100 11.32\par\pard\li1231\sb0\sl-193\slmult0\fi6\tx3039\tx4944\t
x6654 \up0 \expndtw-2\charscalex100 0.5\tab \up0 \expndtw-2\charscalex100 6.51\t
ab \up0 \expndtw-2\charscalex100 5.74\tab \up0 \expndtw-2\charscalex100 10.98\pa
r\pard\li1231\sb0\sl-193\slmult0\fi6\tx2948\tx4944\tx6654 \up0 \expndtw-2\charsc
alex100 0.8\tab \up0 \expndtw-2\charscalex100 10.25\tab \up0 \expndtw-2\charscal
ex100 2.71\tab \up0 \expndtw-2\charscalex100 10.05\par\pard\li1231\sb1\sl-194\sl
mult0\fi6\tx2948\tx4944\tx6654 \up0 \expndtw-2\charscalex100 1.0\tab \up0 \expnd
tw-2\charscalex100 10.88\tab \up0 \expndtw-2\charscalex100 2.40\tab \up0 \expndt
w-2\charscalex100 10.01\par\pard\qj \li1231\ri1031\sb151\sl-200\slmult0\tx1431 \
up0 \expndtw0\charscalex102 * NaCl was added to 25 ml of M-5 medium containing
0.1% CaCO\ul0\sub\cf3\f4\fs18 3\ul0\nosupersub\cf1\f2\fs18 ; 0.1% peptone; 0.6%
yeast \line\tab \up0 \expndtw-2\charscalex100 extract; 0.2% gelatine and 1.0% st
arch. The pH was adjusted to 6.0. \par\pard\qj \li1231\sb0\sl-212\slmult0 \par\p
ard\qj\li1231\sb0\sl-212\slmult0 \par\pard\qj\li1231\ri1022\sb7\sl-212\slmult0\f
i193 \up0 \expndtw0\charscalex100 \ul0\nosupersub\cf6\f7\fs20 Other nitrogen-con
taining compounds were tested as substitutes for gelatine (Table 2). \up0 \expnd
tw0\charscalex100 Ammonium acetate, ammonium sulphate and ammonium nitrate incre
ased glucoamylase \up0 \expndtw-2\charscalex100 secretion from about 87% to 93%
- 96%. A very high stimulus of glucoamylase production \up0 \expndtw-2\charscale
x100 was elicited by ammonium acetate, which increased five-fold specific activi
ty. When other \up0 \expndtw-1\charscalex100 carbohydrate sources were used as s
ubstitutes for starch, the best result was obtained with \up0 \expndtw-2\charsca
lex100 cassava flour, which doubled the specific enzyme production. Altogether,
the modifications \up0 \expndtw-1\charscalex100 introduced in the composition of
the M-5 medium increased by 36-fold (from about 1.8 to \up0 \expndtw0\charscale
x100 65 U/mg cell protein) the specific activity of amylase, and the enzyme was
almost totally \up0 \expndtw-4\charscalex100 (96%) released into the culture med
ium. \par\pard\qj \li1231\ri1023\sb18\sl-200\slmult0\fi193 \up0 \expndtw-3\chars
calex100 In order to purify the extracellular glucoamylase, a dialysed crude f
iltrate was applied to \line \up0 \expndtw-4\charscalex100 a DEAE-cellulose colu
mn (1.9 \up0 \expndtw-4\charscalex100 20.0 cm) equilibrated and eluted with 10 m
\ul0\nosupersub\cf7\f8\fs16 M\ul0\nosupersub\cf6\f7\fs20 Tris-HCl \par\pard\qj
\li1231\ri1021\sb11\sl-212\slmult0 \up0 \expndtw-2\charscalex100 pH 7.5, at the
flow rate of 28 ml/h. Ten ml fractions were collected and assayed for enzyme \li
ne \up0 \expndtw-2\charscalex100 activity. Glucoamylase activity was eluted into
two fractions. Form I (76% of total activity) \line \up0 \expndtw-2\charscalex1
00 did not bind to the resin and eluted with a bulk of protein in the void volum
e, whereas form \line \up0 \expndtw-4\charscalex100 II \up0 \expndtw0\charscalex
106 (24% of total activity) was retained and eluted at 52 m\ul0\nosupersub\cf7\
f8\fs16 M\ul0\nosupersub\cf6\f7\fs20 concentration of a linear \line \up0 \expn
dtw-2\charscalex100 (0 - 500 m\ul0\nosupersub\cf7\f8\fs16 M\ul0\nosupersub\cf6\f
7\fs20 ) NaCl gradient, prepared in the same buffer (Fig. 1). We concentrated in
puri-\line \up0 \expndtw-3\charscalex100 fying and characterising glucoamylase

form I only, considering that it represented the larger \line \up0 \expndtw0\cha
rscalex100 enzymatic component, in comparison with form II. Nevertheless, prelim
inary results (not \line \up0 \expndtw-2\charscalex100 shown) had revealed that
glucoamylase form I and form II exhibited quite similar enzyma-\line \up0 \expnd
tw-4\charscalex100 tic properties. \par\pard\ql \li1231\sb0\sl-207\slmult0 \par\
pard\ql\li1231\sb206\sl-207\slmult0 \up0 \expndtw-4\charscalex100 \ul0\nosupersu
b\cf1\f2\fs18 Table 2 \par\pard\ql \li1231\sb1\sl-198\slmult0 \up0 \expndtw-2\ch
arscalex100 Effect of nitrogen sources on glucoamylase production \par\pard\li12
38\sb169\sl-207\slmult0\fi0\tx3518\tx5228\tx6939 \up0 \expndtw-2\charscalex100 C
ompounds\tab \up0 \expndtw-2\charscalex100 Extracellular\tab \up0 \expndtw-2\cha
rscalex100 Intracellular\tab \up0 \expndtw-2\charscalex100 Protein\par\pard\li12
38\sb1\sl-190\slmult0\fi0\tx3518\tx5228\tx6939 \up0 \expndtw-2\charscalex100 add
ed *\tab \up0 \expndtw-2\charscalex100 (total U)\tab \up0 \expndtw-2\charscalex1
00 (total U)\tab \up0 \expndtw-2\charscalex100 (total U)\par\pard\li1238\sb126\s
l-207\slmult0\fi0\tx3609\tx5228\tx6939 \up0 \expndtw-2\charscalex100 none\tab \u
p0 \expndtw-2\charscalex100 2.66\tab \up0 \expndtw-2\charscalex100 0.50\tab \up0
\expndtw-2\charscalex100 1.71\par\pard\li1238\sb1\sl-188\slmult0\fi0\tx3610\tx5
229\tx6940 \up0 \expndtw-2\charscalex100 gelatine\tab \up0 \expndtw-2\charscalex
100 9.19\tab \up0 \expndtw-2\charscalex100 1.33\tab \up0 \expndtw-2\charscalex10
0 2.71\par\pard\li1238\sb2\sl-194\slmult0\fi0\tx3518\tx5228\tx6939 \up0 \expndtw
-2\charscalex100 CH\ul0\sub\cf3\f4\fs18 3\ul0\nosupersub\cf1\f2\fs18 COONH\ul0\s
ub\cf3\f4\fs18 4\tab \up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18 8
3.88\tab \up0 \expndtw-2\charscalex100 3.05\tab \up0 \expndtw-2\charscalex100 4.
13\par\pard\li1238\sb0\sl-193\slmult0\fi0\tx3609\tx5228\tx6939 \up0 \expndtw-2\c
harscalex100 (NH\ul0\sub\cf3\f4\fs18 4\ul0\nosupersub\cf1\f2\fs18 )H\ul0\sub\cf3
\f4\fs18 2\ul0\nosupersub\cf1\f2\fs18 PO\ul0\sub\cf3\f4\fs18 3\tab \up0 \expndtw
-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18 1.85\tab \up0 \expndtw-2\charscalex
100 1.27\tab \up0 \expndtw-2\charscalex100 2.49\par\pard\li1238\sb0\sl-192\slmul
t0\fi0\tx3609\tx5228\tx6939 \up0 \expndtw-2\charscalex100 NH\ul0\sub\cf3\f4\fs18
4\ul0\nosupersub\cf1\f2\fs18 NO\ul0\sub\cf3\f4\fs18 3\tab \up0 \expndtw-2\chars
calex100 \ul0\nosupersub\cf1\f2\fs18 9.67\tab \up0 \expndtw-2\charscalex100 0.30
\tab \up0 \expndtw-2\charscalex100 1.56\par\pard\li1238\sb1\sl-194\slmult0\fi0\t
x3518\tx5228\tx6939 \up0 \expndtw-2\charscalex100 (NH\ul0\sub\cf3\f4\fs18 4\ul0\
nosupersub\cf1\f2\fs18 )\ul0\sub\cf3\f4\fs18 2\ul0\nosupersub\cf1\f2\fs18 SO\ul0
\sub\cf3\f4\fs18 4\tab \up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18
19.80\tab \up0 \expndtw-2\charscalex100 1.53\tab \up0 \expndtw-2\charscalex100
3.35\par\pard\li1238\sb0\sl-193\slmult0\fi0\tx3610\tx5229\tx6940 \up0 \expndtw-2
\charscalex100 Urea\tab \up0 \expndtw-2\charscalex100 8.59\tab \up0 \expndtw-2\c
harscalex100 1.57\tab \up0 \expndtw-2\charscalex100 3.16\par\pard\qj \li1231\sb0
\sl-180\slmult0 \par\pard\qj\li1231\ri1029\sb3\sl-180\slmult0\tx1431 \up0 \expnd
tw-2\charscalex100 * The compounds were added (1% w/v) to 25 ml of M-5 medium c
ontaining by 0.1% CaCO\ul0\sub\cf3\f4\fs18 3\ul0\nosupersub\cf1\f2\fs18 ; 0.1%
\line\tab \up0 \expndtw-2\charscalex100 peptone; 0.5% NaCl; 0.6% yeast extract
and 1.0% starch. The pH was adjusted to 6.0.
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2af88be2ef843f133c3b61e23b6b4b083c4ba2693f10bc07e26b3f0ff8923d3f4e5f10e85169dacf
f67581be3670fcc7aafec35fb5858fc51f0d7ed15f0c3f6cbf855f0e3f683bbfd9cf4efd983e30cf
1fec7975affecfbe3af00780be267c45f88df0475df027c1393f697d2bc55f0afc73f0affe16978c
bc3eb7d3fc6bf1f784bc5561ad5e49a8782ac962d26d749fae3f635fd96fc23fb177ecd5f0c3f66c
f057883c43e2fd27e1eda788eef52f1978b1accf893c6de35f1ef8cbc45f127e23f8df5a8b4e82d7
4eb4bff197c43f17f8a3c4d369da7dbc561a61d5469d64bf66b588900fa76bf2efe07ffc1466f7c6
ff00177f6cad1bf681f837a87ec77f063f65bf80ff00b367c7bd3bc61f1ebc59e12d2bc6baaf807e
35ea9fb4d586bde33f899e1ed0b5dd7344f84ba6e8e7e0085d1bc23ae6bb73e348ed6e67d4bc5369
a2deeab65e1bd2bf512bf3b7e34ffc136fe0c7ed27f10ff6b4d6be3eddea3e3df857fb59fc25fd8c
fe19789be15e9973e25f015f787af3f632f8bdf1b3e35f83fc5563f123c1be2fd2fc4b3dc6b5e34f
8ada0de7f6769f6fa07f64ff00c206b15d6a1e20b1f12ddd869a01f27fecf5ff00058f1f1860ff00
829dfc51f187ecf5e37f855f003f60bf811f0dff0068ff00879378b20b8d27e33fc6ff00837e2cf8
59f1abe2acdf10b52f87fa9adb9f87b63e33d03e1445a8fc30f0af885ed7c60fa06af65aaf8d74ef
0fdfea71e87a6fa07c15fdb43f6d1d33e317ec61e16fdad3e137eceba3f80bfe0a05a5f8d3fe1529
f811e31f1d6afe31f80fe3bf0afc11f147ed1965f0efe2cdcf8d2ca1d0fe2a59eb3f0bfc1be29b49
be247802cfc1561a4f8df424d2bfe110d4b45d7b4dd7a1adf0f3fe08c1f02fc17f13ff006edf18eb
9f187f68df88be0bfdbabe037873f678f17f817c7ff1cfe32f8e751f0e781e1f875e3cf871e389b5
1f1afc43f895e36bbf893acf88f4af1bc93783b52f1b68d7775f09059dee9fe099a1d3fc45acc13f
63f05ffe09ebf1cbc3ff00157f649f1dfed1ff00b6447f1ffc2ffb0cf873c65a6fecf7e11f0d7c02
d3be0ceb1ab78abc5df0b353f814bf11fe3e78bd7e28fc4783e2678b744f843e20f15787b4f87c13
e15f83de1a9b5ef15eb5e29bed02e251a569ba6007ead57cb9fb477ec5bfb32fed673f83affe3dfc
2eb4f186bdf0f8eb49e08f18693e26f1afc3cf1f7856d3c4b6f6f6be25d2744f885f0d3c49e0ff00
1bd8681e2386d2c47883c3b06beba16b6fa7e9d36a9a75d4da7d94907d47450078f7c2bf803f07be
08783f4af873f097c09a5780be1b683e06d03e1c683f0cfc3f36a56bf0d342f097872efc4d7d6b67
a2fc3c6bd93c19a4ea7aa5d78bf5c97c5fe26d3f43b6f13f8f776951f8df59f10c5e1df0ea695e07
f02ffe09bffb11fecd5f116dbe2b7c12fd9fbc2de08f1ce93a4f88340f096a49ab78bfc41a6fc36d
03c577515df89b41f841e17f15788f5cf0a7c1ad13c40f05bc1ac691f0af44f07e9da8e9f6b69a5d
d5b4ba6dadbda47f6ed1400514514005145140051451400514514005145140051451400514514005
14514005145140051451400514514005145140051451400514514005145140051451400514514005
14514005145140051451400514514005145140051451400514514005145140051451400514514005
145140051451400514514005145140051451400514514005145140057e6ef893fe0ae5ff0004fcf0
a78bbc6fe06d53e396af73e24f873e38f187c36f1a5b7877e077ed0be30d3f44f1d7803c45a8f84b
c67e1a935ff08fc29d73c3f79a87873c49a4ea5a36a634ed52f2186faca7884cdb327f48abf1bff6
0ffd9aff00693d1fc33fb406a1ac7ed03f1efe04e95acffc143ffe0a1fe3ad03e13cdf0afe0647a3
5f7813c65fb6e7c6df18f853c4ba4ea1f11be0cebfe3cbef0bfc4cf0deb163e30d1f5b8fc4b25a6a
5a4f8860d47c337306973e9eea01fb07a6ea169abe9d61aad848d3586a7656ba8594cf0cf6cf2da5
ec11dcdb48f6f751c373033c32a3343710c53c44949638e4565176bf1f7c17fb3ef8d3fe1acffe0a
81fb4f78a3e147c4ff00893f11fc1fe33d034cfd88f4ff00107c52f1cf827c35ac782ef7fe09f7fb
3c697e2df087c11bcd4f5f4f87ff000fec7c7df1b61f1d7867c59e3bd27448bec9e38b6b9d5b58bb
9751f0c432da7e08fc0efd953fe0a017bf183f667f895fb3dfc1ef1a7ecd7f14a7f853fb5b7823e2
feb8ff00b31fc77f82d69e06f8c3e3bfd87bf6848fe0abfed17fb46fed17fb52fc6df1ff00edaf67
e14fda1dbe18436ff1267f86f77f0f17c6da1e9fe27d33c436373af68ba16a001fd96fc4df8b1f0e
7e0d787b4ff15fc50f17693e0cf0feade30f03fc3fd2f52d5e49963d4bc6bf12bc59a47817c07e18
b086de1b8b9bbd5fc53e2ed7b48d0b4ab482191e6bdbe8b76c89649537741f17f87fc4baa78d345d
1aeee2e751f87be26b5f0878b219b4bd5b4f8ec3c417be0ef09f8fadad2d2ef51b1b4b3d72ddfc2d
e38f0d5f36a9a0dc6a7a4c3777b75a2cd7d1ebba3eb5a6e9ff00c4afed17fb17783be277ecfdfb22
68de15ff00824ffede5a8fc72f83fe3ffd957c6bfb7cf8dbc5f6bf124278a20f873f157e12c7f1e7
56d4f4f7f881a9afeddbf14bc5da6cff001417c15e2ef8627c65aaf87fc17ab78df58d1fc4fe1cb5
d76cf46bff00d71fda7fe1bfed63e32f839fb58697f0dfc1dfb4b6bdf02f4bff0082927ec77e28d5
be07786755f1cf81fe2cfc56ff00826ee83fb0efec2b69f1dfe0ff00ecf327887c47e0bd7f4eb4bd
f88d1fc4a7f17784bc27e2ff0008ea3e28f14e81f1b3c10da8bf8fbc41e21d3b5200fe87e8afe4b2
fbf668f88fe30f8e9f0c349fd93ff662fdb6ff00665ff827df8a3f6d9fd85e2f16fc2cbdd4fe2f7c
09b1bdd3742f831ff051d87f6b8f881a77c29b2f1e5a7c40f837f037c4cde34fd917c15e3c1a9e93
f0f3c3df103c77e194d72c744d4ee648bc51abe3fed45fb097893e1ff8dfc67e0af047c27fda3e1f
d9cfe1b7ed89f18b53f819e03befd9b7e277fc141bf6551e05f887fb167fc139f59bab5f157ecfd6
1f1cfc0df1b20d12f3e3d681fb41c5f077e26fc2fd5f54f0b7c16f1927c77d0e7d3342d4fc65e1d9
9403faebae1be287c4af03fc18f869f113e30fc4dd7a1f0afc36f851e05f16fc4af883e28b9b4d42
fedfc37e07f02e81a878a3c59af4f63a45a6a1aade43a3e83a55fea32da699617ba85c25bb436569
7372f142ff001e7fc13074bf8cda07ec43f057c37f1dfe16df7c1ef1cf866cbc49a05af83b56f1d7
c47f881ad3f82b4cf16eb907807c49ad6a3f17bc5df103e27787f52f15f844691e2097c01e39f1d7

8afc49f0f62bf87c1ba9ea715c68cda6d87e35fec9ff00f04e8f116aff00b3d7fc1237c43f1ffe13
fed0baf7c69f8ada4fc57f81bff052693e2a7c4df8efacebfe24fd9ffe23fec15fb66786f5bf87df
1ff47d73c733d95af82e5f8a92fc1dd23c336fa8d8d9c9e14f165ef86d3c353e93ad6ad34d7601fd
057c08fdaa7e07fed257ff0012b45f84fe25f105e78a3e0debfa07863e2a781fc75f0d3e28fc1df8
89e01d63c57e14d2fc73e1587c4ff0e7e31f833c05e39d2ecfc4fe11d6b4dd7fc3bab5c787d748d7
34f9de5d2efae8daddac1f4357cfff0002ff0065ef825fb37cff0010b50f84de16d5f4df107c59d7
f43f13fc4df19f8c3c7ff11be2bfc42f1eeb3e18f09e8de04f0c5c78afe22fc59f16f8dfc75ad5b7
867c1de1fd23c39e1cd32fbc433697a0e9769f66d26cecd67ba337d0140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451401ffd9}}}}}\pard\sb0\sl-240{\bkmkstart
Pg4}{\bkmkend Pg4}\par\pard\li1231\sb0\sl-230\slmult0\par\pard\li1231\sb0\sl-23
0\slmult0\par\pard\li1231\sb20\sl-230\slmult0\fi0\tx7874 \up0 \expndtw-2\charsca
lex100 \ul0\nosupersub\cf6\f7\fs20 86\tab \up0 \expndtw-2\charscalex100 \ul0\nos
upersub\cf1\f2\fs18 M. C\ul0\nosupersub\cf9\f10\fs14 EREIA\par\pard\ql \li6530\s
b0\sl-207\slmult0 \par\pard\ql\li6530\sb0\sl-207\slmult0 \par\pard\ql\li6530\sb0
\sl-207\slmult0 \par\pard\ql\li6530\sb0\sl-207\slmult0 \par\pard\ql\li6530\sb0\s
l-207\slmult0 \par\pard\ql\li6530\sb144\sl-207\slmult0 \up0 \expndtw-2\charscale
x100 \ul0\nosupersub\cf1\f2\fs18 Fig. 1 \par\pard\qj \li6530\ri1061\sb0\sl-193\s
lmult0 \up0 \expndtw0\charscalex102 Separation of extracellular \line \up0 \ex
pndtw0\charscalex102 glucoamylase activities by \line \up0 \expndtw-1\charscal
ex100 DEAE-cellulose chromato-\line \up0 \expndtw-1\charscalex100 graphy. The
column (1.9 \par\pard\qj \li6530\ri1060\sb0\sl-191\slmult0 \up0 \expndtw0\cha
rscalex104 20.0 cm) was equilibrated \line \up0 \expndtw-2\charscalex100 with
10 m\ul0\nosupersub\cf9\f10\fs14 M\ul0\nosupersub\cf1\f2\fs18 Tris-HCl pH 7.5 \
line \up0 \expndtw0\charscalex109 and eluted with a linear \line \up0 \expnd
tw0\charscalex104 (0 - 500 m\ul0\nosupersub\cf9\f10\fs14 M\ul0\nosupersub\cf1\f2
\fs18 ) gradient of \line \up0 \expndtw0\charscalex102 NaCl, in the same buf
fer, at \line \up0 \expndtw-1\charscalex100 a flow rate of 28.0 ml/h. Ten \line
\up0 \expndtw0\charscalex100 millilitre fractions were col-\line \up0 \expndtw0\
charscalex100 lected and assayed. Sym-\par\pard\li6530\sb1\sl-207\slmult0\fi0
\tx6991\tx7141 \up0 \expndtw-1\charscalex100 bols:\tab \up0 \expndtw-4\charscale

x100 (\tab \up0 \expndtw-1\charscalex100 ) glucoamylase ac-\par\pard\li6530\sb

1\sl-188\slmult0\fi0 \up0 \expndtw-1\charscalex100 tivities, Form I and Form II;
\par\pard\li6530\sb2\sl-194\slmult0\fi0\tx6681\tx6981\tx8037 \up0 \expndtw-4\cha
rscalex100 (\tab \up0 \expndtw-1\charscalex100 )\tab \up0 \expndtw-1\charscalex1
00 absorbance\tab \up0 \expndtw-1\charscalex100 280 nm;\par\pard\li6530\sb0\sl-1
93\slmult0\fi0\tx6772 \up0 \expndtw-1\charscalex100 (\tab \up0 \expndtw-1\charsc
alex100 ) NaCl gradient\par\pard\qj \li1231\sb0\sl-200\slmult0 \par\pard\qj\li12
31\sb0\sl-200\slmult0 \par\pard\qj\li1231\sb0\sl-200\slmult0 \par\pard\qj\li1231
\ri1022\sb112\sl-200\slmult0\fi193 \up0 \expndtw0\charscalex100 \ul0\nosupersub\
cf6\f7\fs20 In order to purify Form I, fractions with this activity were pooled,
dialysed, and applied \line \up0 \expndtw0\charscalex100 to a CM-cellulose (2.0
\up0 \expndtw0\charscalex100 6.0 cm) column equilibrated with 10 m\ul0\nosupers
ub\cf7\f8\fs16 M\ul0\nosupersub\cf6\f7\fs20 sodium acetate buffer, \par\pard\qj
\li1231\ri1023\sb10\sl-213\slmult0\fi0 \up0 \expndtw0\charscalex100 pH 5.5, and
eluted with a linear gradient of NaCl (0 - 500 m\ul0\nosupersub\cf7\f8\fs16 M\u
l0\nosupersub\cf6\f7\fs20 ) in the same buffer. Five ml \up0 \expndtw0\charscale
x103 fractions were collected at a flow rate of 24.4 ml/h (Fig. 2). All steps we
re carried out at \up0 \expndtw0\charscalex100 4 C. Glucoamylase activity was e
luted as a single peak with 125 m\ul0\nosupersub\cf7\f8\fs16 M\ul0\nosupersub\cf
6\f7\fs20 of salt with a recove\up0 \expndtw-2\charscalex100 ry of 41.6% and pu
rification of 6.8-fold (Table 3). \par\pard\ql \li6544\sb0\sl-207\slmult0 \par\p
ard\ql\li6544\sb0\sl-207\slmult0 \par\pard\ql\li6544\sb0\sl-207\slmult0 \par\par
d\ql\li6544\sb0\sl-207\slmult0 \par\pard\ql\li6544\sb44\sl-207\slmult0 \up0 \exp
ndtw-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18 Fig. 2 \par\pard\qj \li6544\ri1
048\sb5\sl-193\slmult0 \up0 \expndtw0\charscalex101 Separation of extracellula
r \line \up0 \expndtw-2\charscalex100 glucoamylase \up0 \expndtw0\charscalex106
(form I) by \line \up0 \expndtw0\charscalex100 CM-cellulose chromatogra-\line
\up0 \expndtw0\charscalex100 phy. The column \up0 \expndtw-2\charscalex100
(2.0 \par\pard\qj \li6544\ri1049\sb8\sl-192\slmult0\fi0 \up0 \expndtw0\charscale
x106 6.0 cm) was equilibrated \line \up0 \expndtw0\charscalex103 with 10 m\ul
0\nosupersub\cf9\f10\fs14 M\ul0\nosupersub\cf1\f2\fs18 sodium acetate \line \up
0 \expndtw0\charscalex100 buffer, pH \up0 \expndtw0\charscalex101 5.5 and elu
ted \line \up0 \expndtw0\charscalex106 with a linear gradient of \line \up0
\expndtw-2\charscalex100 NaCl \up0 \expndtw0\charscalex103 (0 - 500 m\ul0\nosupe
rsub\cf9\f10\fs14 M\ul0\nosupersub\cf1\f2\fs18 ) in the \line \up0 \expndtw0\c
harscalex100 same buffer at a flow rate of \par\pard\qj \li6544\ri1047\sb13\sl-1
86\slmult0 \up0 \expndtw0\charscalex106 24.4 ml/h. Five millilitre \line \up0
\expndtw0\charscalex100 fractions were collected and \line \up0 \expndtw-2\char
scalex100 assayed. Symbols: ( ) gluco-\line \up0 \expndtw-2\charscalex100 amyla
se activities; ( ) absor-\par\pard\li6544\sb9\sl-207\slmult0\fi0\tx7076\tx8094
\up0 \expndtw-2\charscalex100 bance\tab \up0 \expndtw0\charscalex101 280 nm; (
\tab \up0 \expndtw0\charscalex101 ) NaCl\par\pard\qj \li6544\ri1048\sb4\sl-180\
slmult0 \up0 \expndtw0\charscalex105 gradient. Other details as \up0 \expndtw
-2\charscalex100 described in the text \par\pard\sect\sectd\fs24\paperw9840\pape
rh13340\pard\sb0\sl-240{\bkmkstart Pg5}{\bkmkend Pg5}\par\pard\li1231\sb0\sl-230
\slmult0\par\pard\li1231\sb0\sl-230\slmult0\par\pard\li1231\sb65\sl-230\slmult0\
fi0\tx8459 \up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18 Glucoamylas
e from a thermophilic fungus\tab \up0 \expndtw-2\charscalex100 \ul0\nosupersub\c
f6\f7\fs20 87\par\pard\li1231\sb166\sl-207\slmult0\fi0 \up0 \expndtw-2\charscale
x100 \ul0\nosupersub\cf1\f2\fs18 Table 3\par\pard\li1231\sb1\sl-188\slmult0\fi0
\up0 \expndtw-2\charscalex100 Summary of the purification steps of extracellular
glucoamylase form I\par\pard\li1231\sb163\sl-207\slmult0\fi6\tx3518\tx4374\tx52
29\tx6085\tx6940\tx7797 \up0 \expndtw-2\charscalex100 Step\tab \up0 \expndtw-2\c
harscalex100 Total\tab \up0 \expndtw-2\charscalex100 Total\tab \up0 \expndtw-2\c
harscalex100 Total\tab \up0 \expndtw-2\charscalex100 Specific\tab \up0 \expndtw2\charscalex100 Yield\tab \up0 \expndtw-2\charscalex100 Purifi-\par\pard\li1238\
sb1\sl-190\slmult0\fi2279\tx4374\tx5229\tx6085\tx6940\tx7797 \up0 \expndtw-2\cha
rscalex100 volume\tab \up0 \expndtw-2\charscalex100 protein\tab \up0 \expndtw-2\
charscalex100 activity\tab \up0 \expndtw-2\charscalex100 activity\tab \up0 \expn
dtw-2\charscalex100 (%)\tab \up0 \expndtw-2\charscalex100 cation\par\pard\li1238

\sb1\sl-193\slmult0\fi2279\tx4374\tx6085\tx7797 \up0 \expndtw-2\charscalex100 (m

l)\tab \up0 \expndtw-2\charscalex100 (mg)\tab \up0 \expndtw-2\charscalex100 (U/m
g)\tab \up0 \expndtw-2\charscalex100 (-fold)\par\pard\li1238\sb125\sl-207\slmult
0\fi0\tx3517\tx4374\tx5228\tx6176\tx6939\tx7797 \up0 \expndtw-2\charscalex100 Fi
ltrate\tab \up0 \expndtw-2\charscalex100 780\tab \up0 \expndtw-2\charscalex100 3
03.4\tab \up0 \expndtw-2\charscalex100 2828\tab \up0 \expndtw-2\charscalex100 9.
3\tab \up0 \expndtw-2\charscalex100 100\tab \up0 \expndtw-2\charscalex100 -\par\
pard\li1238\sb1\sl-190\slmult0\fi0 \up0 \expndtw-2\charscalex100 DEAE-cellulose\
par\pard\li1238\sb1\sl-193\slmult0\fi181\tx3518\tx4465\tx5229\tx6085\tx7032\tx77
97 \up0 \expndtw-2\charscalex100 Form I\tab \up0 \expndtw-2\charscalex100 710\ta
b \up0 \expndtw-2\charscalex100 50.4\tab \up0 \expndtw-2\charscalex100 2146\tab
\up0 \expndtw-2\charscalex100 42.6\tab \up0 \expndtw-2\charscalex100 75.9\tab \u
p0 \expndtw-2\charscalex100 4.6\par\pard\li1238\sb0\sl-193\slmult0\fi181\tx3518\
tx4465\tx5320\tx6085\tx7032\tx7797 \up0 \expndtw-2\charscalex100 Form II\tab \up
0 \expndtw-2\charscalex100 164\tab \up0 \expndtw-2\charscalex100 56.6\tab \up0 \
expndtw-2\charscalex100 682\tab \up0 \expndtw-2\charscalex100 12.1\tab \up0 \exp
ndtw-2\charscalex100 24.1\tab \up0 \expndtw-2\charscalex100 1.3\par\pard\li1238\
sb0\sl-193\slmult0\fi0\tx3520\tx4467\tx5230\tx6086\tx7032\tx7797 \up0 \expndtw-2
\charscalex100 CM-cellulose\tab \up0 \expndtw-2\charscalex100 175\tab \up0 \expn
dtw-2\charscalex100 18.7\tab \up0 \expndtw-2\charscalex100 1176\tab \up0 \expndt
w-2\charscalex100 62.9\tab \up0 \expndtw-2\charscalex100 41.6\tab \up0 \expndtw2\charscalex100 6.8\par\pard\qj \li1231\sb0\sl-220\slmult0 \par\pard\qj\li1231\r
i1022\sb68\sl-220\slmult0\fi193 \up0 \expndtw0\charscalex100 \ul0\nosupersub\cf6
\f7\fs20 The purified enzyme showed a single protein band in PAGE (Fig. 3A) and
SDS-PAGE \line \up0 \expndtw0\charscalex100 (Fig. 3B) coincident with glucoam
ylase activity against starch \up0 \expndtw0\charscalex100 (Fig. 3C) or mal
tose \par\pard\qj \li1231\ri1022\sb8\sl-211\slmult0\fi0 \up0 \expndtw0\charscale
x102 (Fig. 3D), as substrates. The molecular mass of the enzyme was estimated to
be 86.0 kDa \up0 \expndtw0\charscalex100 (SDS-PAGE), or 68.5 kDa (Bio Sil-SEC-4
00 filtration). This difference in apparent mole\up0 \expndtw-1\charscalex100 cu
lar mass could be due to the fact that the enzyme was a glycoprotein (25.5% carb
ohydrate \up0 \expndtw0\charscalex100 content). According to H\ul0\nosupersub\cf
7\f8\fs16 AMES \ul0\nosupersub\cf6\f7\fs20 and R\ul0\nosupersub\cf7\f8\fs16 ICKW
OOD \ul0\nosupersub\cf6\f7\fs20 (1985) many glycoproteins migrate anoma\up0 \exp
ndtw0\charscalex100 lously, even in the presence of excess SDS and thiol reagent
s, probably because they bind \up0 \expndtw0\charscalex100 SDS only to the prote
in part of the molecule. The reduced net charge resulting from reduc\up0 \expndt
w0\charscalex100 ed SDS binding lowers the polypeptide mobility during electroph
oresis, yielding artifactu\up0 \expndtw-2\charscalex100 ally high molecular weig
ht estimates. \par\pard\qj \li1231\ri1022\sb10\sl-210\slmult0\fi193 \up0 \expndt
w0\charscalex103 Thin layer chromatography (TLC) of the products of hydrolysis o
f starch (Fig. 4A) or \line \up0 \expndtw0\charscalex100 maltose (Fig. 4B) revea
led only glucose as the hydrolysis product, after 30 min of reaction, \line \up0
\expndtw-1\charscalex100 indicating that the purified enzyme was a glucoamylase
[ \up0 \expndtw-1\charscalex100 (1,4)-\ul0\nosupersub\cf7\f8\fs16 D\ul0\nosuper
sub\cf6\f7\fs20 -glucan glucohydrolase, \par\pard\ql \li1231\sb6\sl-216\slmult0
\up0 \expndtw-2\charscalex100 EC 3.2.1.3]. \par\pard\qj \li1231\ri1022\sb0\sl-21
3\slmult0\fi193 \up0 \expndtw0\charscalex100 Table 4 summarises some biochemical
properties of \ul0\nosupersub\cf10\f11\fs20 S. thermophilum\ul0\nosupersub\cf6\
f7\fs20 glucoamylase acti-\line \up0 \expndtw0\charscalex100 vity using either
starch or maltose as substrates. Activation energy values (Ea) for the hy-\line
\up0 \expndtw0\charscalex100 drolysis of starch and maltose, calculated from A\u
l0\nosupersub\cf7\f8\fs16 RRHENIUS \ul0\nosupersub\cf6\f7\fs20 plots were, 2.64
and 1.97 Kcal \line \up0 \expndtw0\charscalex105 mol\ul0\super\cf3\f4\fs19\ul0\s
uper\cf3\f4\fs18 -1\ul0\nosupersub\cf6\f7\fs20 respectively. The isoelectric po
int was 8.4. Optima of pH and temperature, using \line \up0 \expndtw0\charscalex
102 starch or maltose as substrates, were 6.5/60 C and 5.0/55 C, respectively.
Glucoamylase \line \up0 \expndtw0\charscalex100 had a half-life of 22 minutes a
t 55 C using starch as substrate, and it was completely stable \line \up0 \expn
dtw0\charscalex104 with maltose. The thermostability of the enzyme was improved

(100% after 60 min at \line \up0 \expndtw0\charscalex104 60 C) when it was in

cubated at 60 C in the presence of either 1% (w/v) starch, or 10% \line \up0 \e
xpndtw0\charscalex100 sorbitol, and then assayed for glucoamylase activity using
starch or maltose as substrates. \line \up0 \expndtw-1\charscalex100 Similar re
sults were reported by others (T\ul0\nosupersub\cf7\f8\fs16 OSI \ul0\nosupersub\
cf10\f11\fs20 et al.\ul0\nosupersub\cf6\f7\fs20 1993, S\ul0\nosupersub\cf7\f8\
fs16 ILVA \ul0\nosupersub\cf6\f7\fs20 and P\ul0\nosupersub\cf7\f8\fs16 ERALTA \u
l0\nosupersub\cf6\f7\fs20 1998). \par\pard\qj \li1231\ri1021\sb0\sl-215\slmult0\
fi193 \up0 \expndtw-1\charscalex100 The preferred substrates for \ul0\nosupersub
\cf10\f11\fs20 S. thermophilum\ul0\nosupersub\cf6\f7\fs20 glucoamylase activity
were starch, maltose, \line \up0 \expndtw-1\charscalex100 glycogen, amylopectin
, amylose, and isomaltose, in that order (data not shown). These data \line \up0
\expndtw0\charscalex100 are compatible with the values of \ul0\nosupersub\cf10\
f11\fs20 K\ul0\sub\cf3\f4\fs18 m\ul0\nosupersub\cf6\f7\fs20 and \ul0\nosupersub
\cf10\f11\fs20 V\ul0\sub\cf3\f4\fs18 max\ul0\nosupersub\cf6\f7\fs20 calculated
from H\ul0\nosupersub\cf7\f8\fs16 ANES \ul0\nosupersub\cf6\f7\fs20 plots (H\ul0\
nosupersub\cf7\f8\fs16 ANES \ul0\nosupersub\cf6\f7\fs20 1932), \line \up0 \expnd
tw0\charscalex105 determined at the optimum temperature for glucoamylase and mal
tase activities, using \line \up0 \expndtw-1\charscalex100 starch or maltose
as substrates at concentrations from \up0 \expndtw-1\charscalex100 0.05 to
\up0 \expndtw-1\charscalex100 4.5 mg/ml and 0.2 to \par\pard\qj \li1231\ri102
2\sb0\sl-215\slmult0\fi0 \up0 \expndtw0\charscalex100 10.0 mg/ml, respectively (
Table 4). Glucoamylase activity was inhibited by several metal \line \up0 \expnd
tw0\charscalex100 ions used at 1 m\ul0\nosupersub\cf7\f8\fs16 M\ul0\nosupersub\c
f6\f7\fs20 concentration, such as Ba\ul0\super\cf3\f4\fs19\ul0\super\cf3\f4\fs1
8 ++\ul0\nosupersub\cf15\f16\fs10 \ul0\nosupersub\cf6\f7\fs20 (20%), Ca\ul0\su
per\cf3\f4\fs19\ul0\super\cf3\f4\fs18 ++\ul0\nosupersub\cf15\f16\fs10 \ul0\nosu
persub\cf6\f7\fs20 (22.7%), Cu\ul0\super\cf3\f4\fs19\ul0\super\cf3\f4\fs18 ++\u
l0\nosupersub\cf6\f7\fs20 (17.2%), EDTA \line \up0 \expndtw-1\charscalex100 (23
%), Hg\ul0\super\cf3\f4\fs19\ul0\super\cf3\f4\fs18 +\ul0\nosupersub\cf6\f7\fs20
(24.4%), Mg\ul0\super\cf3\f4\fs19\ul0\super\cf3\f4\fs18 ++\ul0\nosupersub\cf
15\f16\fs10 \ul0\nosupersub\cf6\f7\fs20 (20.8%), Mn\ul0\super\cf3\f4\fs19\ul0
\super\cf3\f4\fs18 ++\ul0\nosupersub\cf6\f7\fs20 (21.1%), Na\ul0\super\cf3\f4
\fs19\ul0\super\cf3\f4\fs18 +\ul0\nosupersub\cf6\f7\fs20 (22.8%), NH\ul0\sub\
cf3\f4\fs18 4+\ul0\nosupersub\cf6\f7\fs20 (13.7%), Zn\ul0\super\cf3\f4\fs19\u
l0\super\cf3\f4\fs18 ++ \line \up0 \expndtw0\charscalex100 \ul0\nosupersub\cf6\f
7\fs20 (24.1%). On the other hand, maltase activity was activated by 10 m\ul0\no
supersub\cf7\f8\fs16 M\ul0\nosupersub\cf6\f7\fs20 Ba\ul0\super\cf3\f4\fs19\ul0\
super\cf3\f4\fs18 ++\ul0\nosupersub\cf6\f7\fs20 (7.8%), 10 m\ul0\nosupersub\cf7
\f8\fs16 M \line \up0 \expndtw0\charscalex100 \ul0\nosupersub\cf6\f7\fs20 Mn\ul0
\super\cf3\f4\fs19\ul0\super\cf3\f4\fs18 ++\ul0\nosupersub\cf6\f7\fs20 (12.4%),
and 10 m\ul0\nosupersub\cf7\f8\fs16 M\ul0\nosupersub\cf6\f7\fs20 Mg\ul0\super\
cf3\f4\fs19\ul0\super\cf3\f4\fs18 ++\ul0\nosupersub\cf6\f7\fs20 (28%). Other re
agents inhibited 20 to 87% the enzyme. \par\pard\ql \li1231\ri1022\sb0\sl-212\sl
mult0\fi110 \up0 \expndtw-1\charscalex100 -mercaptoethanol completely inhibited
the hydrolysis of both substrates. This result might \line \up0 \expndtw-1\chars
calex100 suggest the participation of protein disulphide bonds in the catalytic
activity. \line \up0 \expndtw0\charscalex100 Sequence data of the first fif
teen amino terminal residues of
the purified protein \line \up0 \expndt
w0\charscalex103 (Table 5) revealed that \ul0\nosupersub\cf10\f11\fs20 S. therm
ophilum \ul0\nosupersub\cf6\f7\fs20 glucoamylase shared 93% homology with that
\line \up0 \expndtw0\charscalex100 of the thermophilic fungus \ul0\nosupersub
\cf10\f11\fs20 Humicola grisea\ul0\nosupersub\cf6\f7\fs20 var. \ul0\nosupers
ub\cf10\f11\fs20 thermoidea.\ul0\nosupersub\cf6\f7\fs20 No signal peptide
was \line \up0 \expndtw-2\charscalex100 found.
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28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a
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28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a28a0028a
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28a0028a28a0028a28a0028a28a00fffd9}}}}}\pard\sb0\sl-240{\bkmkstart Pg6}{\bkmkend
Pg6}\par\pard\li1231\sb0\sl-230\slmult0\par\pard\li1231\sb0\sl-230\slmult0\par\
pard\li1231\sb20\sl-230\slmult0\fi0\tx7874 \up0 \expndtw-2\charscalex100 \ul0\no
supersub\cf6\f7\fs20 88\tab \up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf1\f2
\fs18 M. C\ul0\nosupersub\cf9\f10\fs14 EREIA\par\pard\ql \li6098\sb0\sl-207\slmu
lt0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult
0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0
\par\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \p
ar\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par
\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par\p
ard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par\par
d\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\
ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql
\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\l
i6098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li6
098\sb0\sl-207\slmult0 \par\pard\ql\li6098\sb0\sl-207\slmult0 \par\pard\ql\li609
8\sb118\sl-207\slmult0 \up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18
Fig. 3 \par\pard\qj \li6098\ri1044\sb8\sl-190\slmult0 \up0 \expndtw0\charscalex
105 Gel electrophoresis of purified \line \up0 \expndtw0\charscalex100 glucoa
mylase activity. (A) silver-\line \up0 \expndtw0\charscalex100 stained 7% PAGE.
Lanes 1 and 2, \par\pard\ql \li6098\sb5\sl-197\slmult0 \up0 \expndtw0\charscale
x103 0.62 g and 1.0 g, respectively; \par\pard\qj \li6098\ri1041\sb0\sl-196
\slmult0 \up0 \expndtw0\charscalex100 (B) 7% SDS-PAGE. Lane 3, puri-\line \up0 \
expndtw0\charscalex103 fied glucoamylase (2.5 g). MM, \line \up0 \expndtw0\cha
rscalex102 molecular mass markers. (C) glu-\line \up0 \expndtw-1\charscalex100 c
oamylase activity gels of samples \line \up0 \expndtw0\charscalex105 from the pu
rification steps using \line \up0 \expndtw-2\charscalex100 starch and (D) maltos
e as substrate \par\pard\ql \li1231\sb0\sl-230\slmult0 \par\pard\ql\li1231\sb0\s
l-230\slmult0 \par\pard\ql\li1231\sb160\sl-230\slmult0 \up0 \expndtw-4\charscale
x100 \ul0\nosupersub\cf12\f13\fs20 Discussion \par\pard\qj \li1231\ri1021\sb205\
sl-212\slmult0 \up0 \expndtw0\charscalex100 \ul0\nosupersub\cf6\f7\fs20 The prod
uction of glucoamylase by \ul0\nosupersub\cf10\f11\fs20 S. thermophilum\ul0\nosu
persub\cf6\f7\fs20 was largely increased by replacing \line \up0 \expndtw-1\cha
rscalex100 starch by cassava flour, and gelatine by ammonium acetate, in the ori
ginal M5 culture me-\line \up0 \expndtw-2\charscalex100 dium. Production of m
icrobial glucoamylase in cassava flour was reported by others \line \up0
\expndtw-3\charscalex100 (K\ul0\nosupersub\cf7\f8\fs16 ILIKIAN \ul0\nosupersub\
cf6\f7\fs20 1996, R\ul0\nosupersub\cf7\f8\fs16 EDDY \ul0\nosupersub\cf6\f7\fs20
and B\ul0\nosupersub\cf7\f8\fs16 ASAPPA \ul0\nosupersub\cf6\f7\fs20 1996). Gluco
amylase activity from \ul0\nosupersub\cf10\f11\fs20 Aspergillus flavus \line \up

0 \expndtw0\charscalex103 \ul0\nosupersub\cf6\f7\fs20 cultivated on cassava peel

was 170-times higher than that obtained with soluble starch \line \up0 \expndt
w-4\charscalex100 (S\ul0\nosupersub\cf7\f8\fs16 ANI \ul0\nosupersub\cf10\f11\fs2
0 et al.\ul0\nosupersub\cf6\f7\fs20 1992). \par\pard\qj \li1231\ri1022\sb10\sl210\slmult0\fi193 \up0 \expndtw-2\charscalex100 An interesting result was observ
ed when \ul0\nosupersub\cf10\f11\fs20 S. thermophilum \ul0\nosupersub\cf6\f7\fs2
0 was cultivated in the presence \line \up0 \expndtw0\charscalex100 of different
concentrations of sodium chloride (Table 1). This salt increased the secretion
\line \up0 \expndtw0\charscalex100 glucoamylase activity. The influence of osmot
ic potential on enzyme levels has been stu-\line \up0 \expndtw0\charscalex102 di
ed in only a few microbial systems, and different effects have been reported. Os
motic \line \up0 \expndtw-3\charscalex100 stress favours the production and secr
etion of a periplasmic \up0 \expndtw-3\charscalex100 -galactosidase from \ul0\no
supersub\cf10\f11\fs20 Penicilli-\par\pard\qj \li1231\ri1022\sb8\sl-213\slmult0\
fi0 \up0 \expndtw0\charscalex100 um notatum\ul0\nosupersub\cf6\f7\fs20 (F\ul0\n
osupersub\cf7\f8\fs16 IEDUREK \ul0\nosupersub\cf6\f7\fs20 1998). Similar results
were obtained for cellulase activity in \ul0\nosupersub\cf10\f11\fs20 Tri\up0 \
expndtw-2\charscalex100 choderma reesei\ul0\nosupersub\cf6\f7\fs20 and \ul0\nos
upersub\cf10\f11\fs20 Sporotrichum\ul0\nosupersub\cf6\f7\fs20 \ul0\nosupersub\c
f10\f11\fs20 cellulophilum\ul0\nosupersub\cf6\f7\fs20 growing on wheat bran (K\
ul0\nosupersub\cf7\f8\fs16 IM \ul0\nosupersub\cf10\f11\fs20 et al.\ul0\nosupersu
b\cf6\f7\fs20 1985). \up0 \expndtw0\charscalex100 However, the possibility that
the increased glucoamylase secretion in \ul0\nosupersub\cf10\f11\fs20 S. thermo
philum\ul0\nosupersub\cf6\f7\fs20 is \up0 \expndtw-4\charscalex100 due to chang
es in external osmolarity, is still a speculation. \par\pard\sect\sectd\fs24\pap
erw9840\paperh13340{\shp
{\*\shpinst\shpleft0\shptop0\shpright9840\shpbottom13340\shpwr3\shpfblwtxt0\shpz
-10000\shplid6
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14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451400514514005145
14005145140051451400514514005145140051451400514514005145140051451401ffd9}}}}}\pa
rd\sb0\sl-240{\bkmkstart Pg7}{\bkmkend Pg7}\par\pard\li1231\sb0\sl-230\slmult0\p
ar\pard\li1231\sb0\sl-230\slmult0\par\pard\li1231\sb65\sl-230\slmult0\fi0\tx8459
\up0 \expndtw-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18 Glucoamylase from a t
hermophilic fungus\tab \up0 \expndtw-3\charscalex100 \ul0\nosupersub\cf6\f7\fs20
89\par\pard\ql \li5746\sb0\sl-207\slmult0 \par\pard\ql\li5746\sb0\sl-207\slmult
0 \par\pard\ql\li5746\sb0\sl-207\slmult0 \par\pard\ql\li5746\sb0\sl-207\slmult0
\par\pard\ql\li5746\sb0\sl-207\slmult0 \par\pard\ql\li5746\sb0\sl-207\slmult0 \p
ar\pard\ql\li5746\sb0\sl-207\slmult0 \par\pard\ql\li5746\sb0\sl-207\slmult0 \par
\pard\ql\li5746\sb0\sl-207\slmult0 \par\pard\ql\li5746\sb0\sl-207\slmult0 \par\p
ard\ql\li5746\sb0\sl-207\slmult0 \par\pard\ql\li5746\sb0\sl-207\slmult0 \par\par
d\ql\li5746\sb0\sl-207\slmult0 \par\pard\ql\li5746\sb0\sl-207\slmult0 \par\pard\
ql\li5746\sb0\sl-207\slmult0 \par\pard\ql\li5746\sb0\sl-207\slmult0 \par\pard\ql
\li5746\sb0\sl-207\slmult0 \par\pard\ql\li5746\sb135\sl-207\slmult0 \up0 \expndt
w-2\charscalex100 \ul0\nosupersub\cf1\f2\fs18 Fig. 4 \par\pard\qj \li5746\ri1050
\sb6\sl-192\slmult0\fi0 \up0 \expndtw0\charscalex102 Analysis of the hydrolys
is products \line \up0 \expndtw0\charscalex103 released by the purified \ul0\no
supersub\cf8\f9\fs18 S. thermophi-\line \up0 \expndtw0\charscalex100 lum\ul0\nos
upersub\cf1\f2\fs18 glucoamylase acting on starch (A) \line \up0 \expndtw-2\cha
rscalex100 or maltose (B). Glucoamylase (3.6 mU) \line \up0 \expndtw0\charscalex
108 was incubated with the substrates \line \up0 \expndtw0\charscalex102 (10
mg/ml) in 100 m\ul0\nosupersub\cf9\f10\fs14 M\ul0\nosupersub\cf1\f2\fs18 sodiu
m acetate \line \up0 \expndtw0\charscalex104 buffer, pH 5.5, at 60 C, for diff
erent \line \up0 \expndtw0\charscalex105 times (0; 0.5; 1; 2; 24 hours). Abbre-\
line \up0 \expndtw-2\charscalex100 viations: G, glucose; M, maltose \par\pard\ql
\li1231\sb0\sl-207\slmult0 \par\pard\ql\li1231\sb129\sl-207\slmult0 \up0 \expnd
tw-2\charscalex100 Table 4 \par\pard\qj \li1231\ri1036\sb0\sl-200\slmult0 \up0 \
expndtw0\charscalex100 Kinetic constants and some intrinsic properties of \ul0\
nosupersub\cf8\f9\fs18 S. thermophilum\ul0\nosupersub\cf1\f2\fs18
glucoamyla
se activities using \up0 \expndtw-2\charscalex100 starch and maltose as substrat
e \par\pard\li1238\sb161\sl-207\slmult0\fi0\tx5228\tx7508 \up0 \expndtw-2\charsc
alex100 Parameters\tab \up0 \expndtw-2\charscalex100 Starch\tab \up0 \expndtw-2\
charscalex100 Maltose\par\pard\li1238\sb122\sl-207\slmult0\fi0\tx5319\tx7600 \up
0 \expndtw-2\charscalex100 Activation energy (Ea Kcal mol\ul0\super\cf3\f4\fs18
-1\ul0\nosupersub\cf1\f2\fs18 )\tab \up0 \expndtw-2\charscalex100 2.64\tab \up0
\expndtw-2\charscalex100 1.97\par\pard\li1238\sb1\sl-190\slmult0\fi0\tx6369 \up0
\expndtw-2\charscalex100 Carbohydrate content (%)\tab \up0 \expndtw-2\charscale
x100 25.50\par\pard\li1238\sb1\sl-193\slmult0\fi0\tx6460 \up0 \expndtw-2\charsca
lex100 Isoelectric point (pI)\tab \up0 \expndtw-2\charscalex100 8.40\par\pard\li
1238\sb1\sl-194\slmult0\fi0\tx6371 \up0 \expndtw-2\charscalex100 Molecular mass
(Filtration Gel, kDa)\tab \up0 \expndtw-2\charscalex100 68.50\par\pard\li1238\sb

0\sl-192\slmult0\fi0\tx6370 \up0 \expndtw-2\charscalex100 Molecular mass (SDS-PA

GE, kDa)\tab \up0 \expndtw-2\charscalex100 86.00\par\pard\li1238\sb1\sl-193\slmu
lt0\fi0\tx5320\tx7601 \up0 \expndtw-2\charscalex100 Optimum pH\tab \up0 \expndtw
-2\charscalex100 6.50\tab \up0 \expndtw-2\charscalex100 5.00\par\pard\li1238\sb1
\sl-194\slmult0\fi0\tx5229\tx7509 \up0 \expndtw-2\charscalex100 Optimum temperat
ure ( C)\tab \up0 \expndtw-2\charscalex100 60.00\tab \up0 \expndtw-2\charscalex1
00 55.00\par\pard\li1238\sb0\sl-193\slmult0\fi0\tx5228\tx7509 \up0 \expndtw-2\ch
arscalex100 Stability 55 C (T\ul0\sub\cf3\f4\fs18 50\ul0\nosupersub\cf1\f2\fs18
- min)\tab \up0 \expndtw-2\charscalex100 22.00\tab \up0 \expndtw-2\charscalex1
00 60.00\par\pard\li1238\sb40\sl-193\slmult0\fi0\tx5319\tx7600 \dn3 \expndtw-2\c
harscalex100 \ul0\nosupersub\cf8\f9\fs18 K\ul0\nosupersub\cf3\f4\fs12 m\ul0\supe
r\cf1\f2\fs27 (mg ml\ul0\super\cf3\f4\fs18 -1\ul0\nosupersub\cf1\f2\fs18 )\tab
\up0 \expndtw-2\charscalex100 0.28\tab \up0 \expndtw-2\charscalex100 1.40\par\pa
rd\li1238\sb25\sl-162\slmult0\fi0\tx5228\tx7601 \dn3 \expndtw-2\charscalex100 \u
l0\nosupersub\cf8\f9\fs18 V\ul0\nosupersub\cf3\f4\fs12 max \ul0\super\cf1\f2\fs2
7 (U mg\ul0\super\cf3\f4\fs18 -1\ul0\nosupersub\cf16\f17\fs9 \ul0\super\cf1\f2\
fs27 protein)\tab \up0 \expndtw-2\charscalex100 67.20\tab \up0 \expndtw-2\charsc
alex100 5.61\par\pard\qj \li1231\sb0\sl-212\slmult0 \par\pard\qj\li1231\ri1021\s
b112\sl-212\slmult0\fi193 \up0 \expndtw0\charscalex104 \ul0\nosupersub\cf10\f11\
fs20 S.\ul0\nosupersub\cf6\f7\fs20 \ul0\nosupersub\cf10\f11\fs20 thermophilum\u
l0\nosupersub\cf6\f7\fs20 glucoamylase activity was resolved into two component
s by ion ex-\line \up0 \expndtw-1\charscalex100 change chromatography. Form I (7
6% of total activity) was purified 6.8-fold. Some proper-\line \up0 \expndtw-1\c
harscalex100 ties of this glucoamylase, such as glycoproteic nature, molecular m
ass, specific activity and \line \up0 \expndtw0\charscalex104 ability to hydroly
se starch and maltose, resembled those of other fungal glucoamylases \line \up0
\expndtw0\charscalex100 (reviewed by V\ul0\nosupersub\cf7\f8\fs16 IHINEN \ul0\no
supersub\cf6\f7\fs20 and M\ul0\nosupersub\cf7\f8\fs16 NTSL \ul0\nosupersub\cf6\f7\f
s20 1989, G\ul0\nosupersub\cf7\f8\fs16 UZMN\ul0\nosupersub\cf6\f7\fs20 -M\ul0\nos
upersub\cf7\f8\fs16 ALDONADO \ul0\nosupersub\cf6\f7\fs20 and P\ul0\nosupersub\cf
7\f8\fs16 AREDEZ\ul0\nosupersub\cf6\f7\fs20 -L\ul0\nosupersub\cf7\f8\fs16 PEZ \li
ne \up0 \expndtw-1\charscalex100 \ul0\nosupersub\cf6\f7\fs20 1995, J\ul0\nosuper
sub\cf7\f8\fs16 AMES \ul0\nosupersub\cf6\f7\fs20 and L\ul0\nosupersub\cf7\f8\fs1
6 EE \ul0\nosupersub\cf6\f7\fs20 1997). This enzyme hydrolysed preferentially st
arch, but also exhibit-\line \up0 \expndtw-1\charscalex100 ed a significant malt
ase activity. Maltase and glucoamylase activities co-migrated in PAGE \line \up0
\expndtw0\charscalex100 (Fig. 3\ul0\super\cf15\f16\fs16\ul0\super\cf15\f16\fs15
\ul0\nosupersub\cf6\f7\fs20 A-D). These activities differed in optimum pH, eff
ect of temperature and also acti-\line \up0 \expndtw-1\charscalex100 vation ener
gy. Apparently, the activity against starch was protected at higher pH and tempe
-\par\pard\sect\sectd\fs24\paperw9840\paperh13340\pard\sb0\sl-240{\bkmkstart Pg8
}{\bkmkend Pg8}\par\pard\li1231\sb0\sl-230\slmult0\par\pard\li1231\sb0\sl-230\sl
mult0\par\pard\li1231\sb20\sl-230\slmult0\fi0\tx7874 \up0 \expndtw-1\charscalex1
00 \ul0\nosupersub\cf6\f7\fs20 90\tab \up0 \expndtw0\charscalex100 \ul0\nosupers
ub\cf1\f2\fs18 M. C\ul0\nosupersub\cf9\f10\fs14 EREIA\par\pard\li1231\sb0\sl-207
\slmult0\par\pard\li1231\sb3\sl-207\slmult0\fi0 \up0 \expndtw-1\charscalex100 \u
l0\nosupersub\cf1\f2\fs18 Table 5\par\pard\li1231\sb1\sl-192\slmult0\fi0 \up0 \e
xpndtw0\charscalex100 N-terminal amino acid sequence of the protein produced by
the thermophilic fungi \ul0\nosupersub\cf8\f9\fs18 Scytalidium\par\pard\li1231\s
b1\sl-192\slmult0\fi0 \up0 \expndtw-1\charscalex100 thermophilum\par\pard\li1231
\sb161\sl-207\slmult0\fi6\tx3234\tx5230\tx6940 \up0 \expndtw-1\charscalex100 \ul
0\nosupersub\cf1\f2\fs18 Edman cycle\tab \up0 \expndtw-1\charscalex100 Amino aci
d\tab \up0 \expndtw-1\charscalex100 pmol\tab \up0 \expndtw-1\charscalex100 \ul0\
nosupersub\cf8\f9\fs18 H. grisea\par\pard\li1231\sb121\sl-207\slmult0\fi6\tx3234
\tx5229\tx6940 \up0 \expndtw-1\charscalex100 \ul0\nosupersub\cf1\f2\fs18 01\tab
\up0 \expndtw-1\charscalex100 Ile\tab \up0 \expndtw-1\charscalex100 2.27\tab \up
0 \expndtw-1\charscalex100 Ile\par\pard\li1231\sb1\sl-191\slmult0\fi6\tx3234\tx5
229\tx6940 \up0 \expndtw-1\charscalex100 02\tab \up0 \expndtw-1\charscalex100 As
n\tab \up0 \expndtw-1\charscalex100 1.81\tab \up0 \expndtw-1\charscalex100 Asn\p
ar\pard\li1231\sb1\sl-192\slmult0\fi6\tx3234\tx5230\tx6941 \up0 \expndtw-1\chars

calex100 03\tab \up0 \expndtw-1\charscalex100 Thr\tab \up0 \expndtw-1\charscalex

100 1.28\tab \up0 \expndtw-1\charscalex100 Thr\par\pard\li1231\sb1\sl-194\slmult
0\fi6\tx3234\tx5229\tx6940 \up0 \expndtw-1\charscalex100 04\tab \up0 \expndtw-1\
charscalex100 Glu\tab \up0 \expndtw-1\charscalex100 1.58\tab \up0 \expndtw-1\cha
rscalex100 Glu\par\pard\li1231\sb0\sl-193\slmult0\fi6\tx3234\tx5230\tx6941 \up0
\expndtw-1\charscalex100 05\tab \up0 \expndtw-1\charscalex100 Lys\tab \up0 \expn
dtw-1\charscalex100 1.10\tab \up0 \expndtw-1\charscalex100 Lys\par\pard\li1231\s
b0\sl-193\slmult0\fi6\tx3234\tx5229\tx6940 \up0 \expndtw-1\charscalex100 06\tab
\up0 \expndtw-1\charscalex100 Ser\tab \up0 \expndtw-1\charscalex100 0.11\tab \up
0 \expndtw-1\charscalex100 Pro\par\pard\li1231\sb0\sl-193\slmult0\fi6\tx3234\tx5
229\tx6940 \up0 \expndtw-1\charscalex100 07\tab \up0 \expndtw-1\charscalex100 Il
e\tab \up0 \expndtw-1\charscalex100 0.98\tab \up0 \expndtw-1\charscalex100 Ile\p
ar\pard\li1231\sb0\sl-193\slmult0\fi6\tx3234\tx5229\tx6940 \up0 \expndtw-1\chars
calex100 08\tab \up0 \expndtw-1\charscalex100 Ala\tab \up0 \expndtw-1\charscalex
100 1.09\tab \up0 \expndtw-1\charscalex100 Ala\par\pard\li1231\sb0\sl-193\slmult
0\fi6\tx3234\tx5229\tx6941 \up0 \expndtw-1\charscalex100 09\tab \up0 \expndtw-1\
charscalex100 Trp\tab \up0 \expndtw-1\charscalex100 0.45\tab \up0 \expndtw-1\cha
rscalex100 Trp\par\pard\li1231\sb0\sl-193\slmult0\fi6\tx3234\tx5229\tx6940 \up0
\expndtw-1\charscalex100 10\tab \up0 \expndtw-1\charscalex100 Asn\tab \up0 \expn
dtw-1\charscalex100 0.78\tab \up0 \expndtw-1\charscalex100 Asn\par\pard\li1231\s
b0\sl-193\slmult0\fi6\tx3234\tx5230\tx6941 \up0 \expndtw-1\charscalex100 11\tab
\up0 \expndtw-1\charscalex100 Lys\tab \up0 \expndtw-1\charscalex100 0.53\tab \up
0 \expndtw-1\charscalex100 Lys\par\pard\li1231\sb0\sl-193\slmult0\fi6\tx3234\tx5
230\tx6941 \up0 \expndtw-1\charscalex100 12\tab \up0 \expndtw-1\charscalex100 Le
u\tab \up0 \expndtw-1\charscalex100 0.81\tab \up0 \expndtw-1\charscalex100 Leu\p
ar\pard\li1231\sb1\sl-194\slmult0\fi6\tx3234\tx5230\tx6941 \up0 \expndtw-1\chars
calex100 13\tab \up0 \expndtw-1\charscalex100 Leu\tab \up0 \expndtw-1\charscalex
100 0.99\tab \up0 \expndtw-1\charscalex100 Leu\par\pard\li1231\sb0\sl-192\slmult
0\fi6\tx3234\tx5229\tx6940 \up0 \expndtw-1\charscalex100 14\tab \up0 \expndtw-1\
charscalex100 Ala\tab \up0 \expndtw-1\charscalex100 1.03\tab \up0 \expndtw-1\cha
rscalex100 Ala\par\pard\li1231\sb1\sl-193\slmult0\fi6\tx3234\tx5229\tx6940 \up0
\expndtw-1\charscalex100 15\tab \up0 \expndtw-1\charscalex100 Asn\tab \up0 \expn
dtw-1\charscalex100 0.72\tab \up0 \expndtw-1\charscalex100 Asn\par\pard\qj \li12
31\ri1030\sb176\sl-190\slmult0 \up0 \expndtw0\charscalex103 Sequence data of \ul
0\nosupersub\cf8\f9\fs18 Humicola grisea\ul0\nosupersub\cf1\f2\fs18 var. \ul0\n
osupersub\cf8\f9\fs18 thermoidea\ul0\nosupersub\cf1\f2\fs18 homologous enzyme w
as take from Gen Bank \up0 \expndtw0\charscalex105 database, (accession number M
89475). The recovery of PTH - amino acids is given in picomol, \up0 \expndtw-1\c
harscalex100 which corresponds 80% of the product and is reported without any co
rrections \par\pard\qj \li1231\sb0\sl-210\slmult0 \par\pard\qj\li1231\ri1023\sb4
\sl-210\slmult0 \up0 \expndtw0\charscalex103 \ul0\nosupersub\cf6\f7\fs20 ratures
. This observation agrees with \ul0\nosupersub\cf10\f11\fs20 H. grisea\ul0\nosup
ersub\cf6\f7\fs20 glucoamylase (T\ul0\nosupersub\cf7\f8\fs16 OSI \ul0\nosupersu
b\cf10\f11\fs20 et al.\ul0\nosupersub\cf6\f7\fs20 1993) and sug-\line \up0 \exp
ndtw0\charscalex102 gested a common catalytic site for starch and maltose hydrol
ysis, but specialised subsites \line \up0 \expndtw-1\charscalex100 for each of t
hese substrates (S\ul0\nosupersub\cf7\f8\fs16 IVAKAMI \ul0\nosupersub\cf6\f7\fs2
0 and R\ul0\nosupersub\cf7\f8\fs16 ADHAKRISHNAN \ul0\nosupersub\cf6\f7\fs20 1976
, K\ul0\nosupersub\cf7\f8\fs16 ISS \ul0\nosupersub\cf10\f11\fs20 et al.\ul0\nosu
persub\cf6\f7\fs20 1981). \par\pard\qj \li1231\ri1022\sb8\sl-213\slmult0\fi193
\up0 \expndtw0\charscalex100 The purified glucoamylase presented 93% homology wi
th 15 amino terminal residues of \up0 \expndtw0\charscalex100 the same enzyme fr
om the thermophilic fungus \ul0\nosupersub\cf10\f11\fs20 Humicola grisea\ul0\nos
upersub\cf6\f7\fs20 var. \ul0\nosupersub\cf10\f11\fs20 thermoidea. \ul0\nosuper
sub\cf6\f7\fs20 Glucoa\up0 \expndtw0\charscalex105 mylase structural, functional
, and evolutionary relationships had been revised recently \up0 \expndtw-2\chars
calex100 (C\ul0\nosupersub\cf7\f8\fs16 OUTINHO \ul0\nosupersub\cf6\f7\fs20 and R
\ul0\nosupersub\cf7\f8\fs16 EILLY \ul0\nosupersub\cf6\f7\fs20 1997). \par\pard\q
j \li1231\ri1022\sb0\sl-220\slmult0\fi193 \up0 \expndtw0\charscalex103 The prese
nt study may contribute to the knowledge of the evolutionary tree of glucoa\up0

\expndtw0\charscalex108 mylase sequences, and to the basic knowledge of a glucoa

mylase that could be used \up0 \expndtw-2\charscalex100 industrially. \par\pard\
ql \li1231\sb0\sl-230\slmult0 \par\pard\ql\li1231\sb164\sl-230\slmult0 \up0 \exp
ndtw-4\charscalex100 \ul0\nosupersub\cf12\f13\fs20 Acknowledgements \par\pard\qj
\li1231\ri1038\sb195\sl-200\slmult0\fi0 \up0 \expndtw0\charscalex100 \ul0\nosup
ersub\cf1\f2\fs18 This work was supported by grants from Fundao de Amparo Pesquisa
do Estado de So Paulo \line \up0 \expndtw0\charscalex100 (FAPESP) and Conselho d
e Desenvolvimento Cientfico e Tecnolgico (CNPq). H. F. T.; J. A. J.; \par\pard\q
j \li1231\ri1038\sb6\sl-193\slmult0 \up0 \expndtw-2\charscalex100 L. J. G.; J.
C. R. and M. L. T. M. P. are Research Fellows of CNPq. M. C. is a recipient of
FAPESP \line \up0 \expndtw-2\charscalex100 Fellowship. This work is part of a Ma
ster Dissertation submitted to the Departamento de Biologia da \line \up0 \expnd
tw-1\charscalex100 Faculdade de Filosofia, Cincias e Letras de Ribeiro Preto - Uni
versidade de So Paulo. We thank \line \up0 \expndtw-3\charscalex100 A\ul0\nosuper
sub\cf9\f10\fs14 MAURI\ul0\nosupersub\cf1\f2\fs18 P\ul0\nosupersub\cf9\f10\fs14
INHAL\ul0\nosupersub\cf1\f2\fs18 , M\ul0\nosupersub\cf9\f10\fs14 AURICIO\ul0\no
supersub\cf1\f2\fs18 \ul0\nosupersub\cf9\f10\fs14 DE\ul0\nosupersub\cf1\f2\fs18
O\ul0\nosupersub\cf9\f10\fs14 LIVEIRA\ul0\nosupersub\cf1\f2\fs18 and R\ul0\no
supersub\cf9\f10\fs14 ICARDO\ul0\nosupersub\cf1\f2\fs18 F. A\ul0\nosupersub\cf9
\f10\fs14 LARCON\ul0\nosupersub\cf1\f2\fs18 for technical assistance. \par\pard
\ql \li1231\sb0\sl-230\slmult0 \par\pard\ql\li1231\sb167\sl-230\slmult0 \up0 \ex
pndtw-4\charscalex100 \ul0\nosupersub\cf12\f13\fs20 References \par\pard\qj \li1
231\sb0\sl-180\slmult0 \par\pard\qj\li1231\ri1028\sb52\sl-180\slmult0\tx1425 \up
0 \expndtw-1\charscalex100 \ul0\nosupersub\cf1\f2\fs18 A\ul0\nosupersub\cf9\f10\
fs14 LMEIDA\ul0\nosupersub\cf1\f2\fs18 , E. M., P\ul0\nosupersub\cf9\f10\fs14 OL
IZELI\ul0\nosupersub\cf1\f2\fs18 , M. L. T. M., T\ul0\nosupersub\cf9\f10\fs14 ER
ENZI\ul0\nosupersub\cf1\f2\fs18 , H. F. and J\ul0\nosupersub\cf9\f10\fs14 ORGE\u
l0\nosupersub\cf1\f2\fs18 , J. A., 1995. Purification and bio-\line\tab \up0 \ex
pndtw-2\charscalex100 chemical characterisation of \up0 \expndtw-2\charscalex100
-xylosidase from \ul0\nosupersub\cf8\f9\fs18 Humicola grisea\ul0\nosupersub\cf1
\f2\fs18 var. \ul0\nosupersub\cf8\f9\fs18 thermoidea\ul0\nosupersub\cf1\f2\fs18
. FEMS Microbiol. \par\pard\ql \li1425\sb8\sl-195\slmult0 \up0 \expndtw-3\chars
calex100 Lett., \ul0\nosupersub\cf2\f3\fs18 130\ul0\nosupersub\cf1\f2\fs18 , 171
- 176. \par\pard\qj \li1231\ri977\sb10\sl-190\slmult0\tx1425\tx1425 \up0 \expnd
tw-1\charscalex100 B\ul0\nosupersub\cf9\f10\fs14 ASAVEWARA\ul0\nosupersub\cf1\f2
\fs18 R\ul0\nosupersub\cf9\f10\fs14 AO\ul0\nosupersub\cf1\f2\fs18 , V., S\ul0\n
osupersub\cf9\f10\fs14 ASTRI\ul0\nosupersub\cf1\f2\fs18 , N. V. S. and S\ul0\nos
upersub\cf9\f10\fs14 UBBA\ul0\nosupersub\cf1\f2\fs18 R\ul0\nosupersub\cf9\f10\f
s14 AO\ul0\nosupersub\cf1\f2\fs18 , P. V., 1981. Purification and characteriza-\
line\tab \up0 \expndtw-2\charscalex100 tion of a thermostable glucoamylase from
the thermophilic fungus\ul0\nosupersub\cf8\f9\fs18 Thermomyces lanuginosus.\ul0
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\f3\fs18 \ul0\nosupersub\cf1\f2\fs18 379 - 387.
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}}\par\pard\sect\sectd\fs24\paperw9840\paperh13340\pard\sb0\sl-240{\bkmkstart Pg
9}{\bkmkend Pg9}\par\pard\li1231\sb0\sl-230\slmult0\par\pard\li1231\sb0\sl-230\s
lmult0\par\pard\li1231\sb65\sl-230\slmult0\fi0\tx8459 \up0 \expndtw-2\charscalex
100 \ul0\nosupersub\cf1\f2\fs18 Glucoamylase from a thermophilic fungus\tab \up0
\expndtw-3\charscalex100 \ul0\nosupersub\cf6\f7\fs20 91\par\pard\ql \li1231\ri9
65\sb166\sl-193\slmult0\fi0\tx1425\tx1425 \up0 \expndtw0\charscalex100 \ul0\nosu
persub\cf1\f2\fs18 B\ul0\nosupersub\cf9\f10\fs14 ERGMEYER\ul0\nosupersub\cf1\f2\
fs18 , H. V. and B\ul0\nosupersub\cf9\f10\fs14 ERNT\ul0\nosupersub\cf1\f2\fs18 ,
E., 1974. In: Methods of Enzymatic Analysis. Vol. 3. H. U. B\ul0\nosupersub\cf9
\f10\fs14 ERG\ul0\nosupersub\cf1\f2\fs18 -\line\tab \up0 \expndtw-2\charscalex10
0 \ul0\nosupersub\cf9\f10\fs14 MEYER\ul0\nosupersub\cf1\f2\fs18 (Editors). pp.
1205 - 1215. Verlag-Chimie Academic Press, New York. \line \up0 \expndtw0\charsc
alex102 B\ul0\nosupersub\cf9\f10\fs14 LUM\ul0\nosupersub\cf1\f2\fs18 , H., B\ul0
\nosupersub\cf9\f10\fs14 EIER\ul0\nosupersub\cf1\f2\fs18 , H. and G\ul0\nosupers
ub\cf9\f10\fs14 ROSS\ul0\nosupersub\cf1\f2\fs18 , H. J., 1987. Improved silver s
taining of plant protein, RNA and \line\tab \up0 \expndtw-3\charscalex100 DNA in
polyacrylamide gels. Electrophoresis, \ul0\nosupersub\cf2\f3\fs18 81\ul0\nosupe
rsub\cf1\f2\fs18 ,\ul0\nosupersub\cf2\f3\fs18 \ul0\nosupersub\cf1\f2\fs18 93
- 99. \par\pard\qj \li1231\ri1020\sb10\sl-190\slmult0\tx1425\tx1425 \up0 \expndt
w0\charscalex100 B\ul0\nosupersub\cf9\f10\fs14 UAINAIN\ul0\nosupersub\cf1\f2\fs1
8 , L. B., K\ul0\nosupersub\cf9\f10\fs14 ADOWAKI\ul0\nosupersub\cf1\f2\fs18 , M.
K., P\ul0\nosupersub\cf9\f10\fs14 OLIZELI\ul0\nosupersub\cf1\f2\fs18 , M. L. T.
M., T\ul0\nosupersub\cf9\f10\fs14 ERENZI\ul0\nosupersub\cf1\f2\fs18 , H. F. and
J\ul0\nosupersub\cf9\f10\fs14 ORGE\ul0\nosupersub\cf1\f2\fs18 , J. A., 1998. \l
ine\tab \up0 \expndtw-2\charscalex100 Characterization of a conidial alkaline ph
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s14 TRAATSMA\ul0\nosupersub\cf1\f2\fs18 , G. and S\ul0\nosupersub\cf9\f10\fs14 A
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9\fs18 Scytalidium thermophilum\ul0\nosupersub\cf1\f2\fs18 , an important \line\
tab \up0 \expndtw-3\charscalex100 fungus in mushroom compost. Mycol. Res., \ul0\
nosupersub\cf2\f3\fs18 97\ul0\nosupersub\cf1\f2\fs18 ,\ul0\nosupersub\cf2\f3\fs1
8 \ul0\nosupersub\cf1\f2\fs18 32kkk 328. \par\pard\qj \li1231\ri1016\sb10\sl190\slmult0\tx1425\tx1425 \up0 \expndtw0\charscalex100 T\ul0\nosupersub\cf9\f10\
fs14 OSI\ul0\nosupersub\cf1\f2\fs18 , L. R. O., T\ul0\nosupersub\cf9\f10\fs14 ER
ENZI\ul0\nosupersub\cf1\f2\fs18 , H. F. and J\ul0\nosupersub\cf9\f10\fs14 ORGE\u
l0\nosupersub\cf1\f2\fs18 , J. A., 1993. Purification and characterization of an
extra-\line\tab \up0 \expndtw0\charscalex100 cellular glucoamylase from the the
rmophilic fungus \ul0\nosupersub\cf8\f9\fs18 Humicola grisea \ul0\nosupersub\cf1
\f2\fs18 var.\ul0\nosupersub\cf8\f9\fs18 thermoidea.\ul0\nosupersub\cf1\f2\fs18

Can. J. Mi-\line \tab \up0 \expndtw-3\charscalex100 crobiol. \ul0\nosupersub\c

f2\f3\fs18 39\ul0\nosupersub\cf1\f2\fs18 ,\ul0\nosupersub\cf2\f3\fs18 \ul0\nosu
persub\cf1\f2\fs18 846 - 852. \par\pard\qj \li1231\ri1013\sb2\sl-200\slmult0\tx1
425 \up0 \expndtw0\charscalex100 V\ul0\nosupersub\cf9\f10\fs14 AN DER \ul0\nosup
ersub\cf1\f2\fs18 B\ul0\nosupersub\cf9\f10\fs14 URG\ul0\nosupersub\cf1\f2\fs18 ,
B., V\ul0\nosupersub\cf9\f10\fs14 RIEND\ul0\nosupersub\cf1\f2\fs18 , G., V\ul0\
nosupersub\cf9\f10\fs14 ELTMAN\ul0\nosupersub\cf1\f2\fs18 , O. R., G\ul0\nosuper
sub\cf9\f10\fs14 ERARD\ul0\nosupersub\cf1\f2\fs18 , V. and E\ul0\nosupersub\cf9\
f10\fs14 IJSINK\ul0\nosupersub\cf1\f2\fs18 , V. G. H., 1998. Enginee-\line\tab \
up0 \expndtw-3\charscalex100 ring an enzyme to resist boiling. Biochem., \ul0\no
supersub\cf2\f3\fs18 95\ul0\nosupersub\cf1\f2\fs18 ,\ul0\nosupersub\cf2\f3\fs18
\ul0\nosupersub\cf1\f2\fs18 2056 - 2060. \par\pard\qj \li1231\ri1017\sb0\sl-200
\slmult0\tx1425 \up0 \expndtw0\charscalex100 V\ul0\nosupersub\cf9\f10\fs14 IHINE
N\ul0\nosupersub\cf1\f2\fs18 , M. and M\ul0\nosupersub\cf9\f10\fs14 NTSL\ul0\nosupe
rsub\cf1\f2\fs18 , P., 1989. Microbial amylolitic enzymes (Review). Crit. Rev. B
iochem. \line\tab \up0 \expndtw-3\charscalex100 Mol. Biol., \ul0\nosupersub\cf2\
f3\fs18 24\ul0\nosupersub\cf1\f2\fs18 , 329 - 418. \par\pard\qj \li1231\ri1045\s
b162\sl-200\slmult0 \up0 \expndtw0\charscalex102 Mailing address: M\ul0\nosupers
ub\cf9\f10\fs14 ARIA \ul0\nosupersub\cf1\f2\fs18 D\ul0\nosupersub\cf9\f10\fs14 E
\ul0\nosupersub\cf1\f2\fs18 L\ul0\nosupersub\cf9\f10\fs14 OURDES \ul0\nosupersu
b\cf1\f2\fs18 T\ul0\nosupersub\cf9\f10\fs14 EIXERA \ul0\nosupersub\cf1\f2\fs18 D
\ul0\nosupersub\cf9\f10\fs14 E \ul0\nosupersub\cf1\f2\fs18 M\ul0\nosupersub\cf9\
f10\fs14 ORAES \ul0\nosupersub\cf1\f2\fs18 P\ul0\nosupersub\cf9\f10\fs14 OLIZELI
\ul0\nosupersub\cf1\f2\fs18 , Departamento de Biologia, \up0 \expndtw-1\charscal
ex100 Faculdade de Filosofia, Cincias e Letras de Ribeiro Preto, Universi
dade de So Paulo, Av. \up0 \expndtw-2\charscalex100 Bandeirantes, 3900, 14.04
0-901 - Ribeiro Preto - SP, Brazil \par\pard\ql \li1231\sb1\sl-175\slmult0 \up0 \
expndtw-2\charscalex100 e-mail: polizeli@ffclrp.usp.br
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