Professional Documents
Culture Documents
99:18
http://dx.doi.org/10.3168/jds.2015-10794
American Dairy Science Association, 2016.
*Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering,
China Agricultural University, Beijing 100083, China
Key Laboratory of Functional Dairy, Ministry of Education, College of Food Science and Nutritional Engineering, China Agricultural University,
Beijing 100083, China
ABSTRACT
Therefore, improving the structure and flavor deficiencies of low-fat yogurt deserved close attention.
Several methods have been used to improve the
properties of low-fat yogurt, including addition of whey
protein, use of suitable starter cultures, enhanced total solids content, use of thickeners, and modification
of processing parameters (Sodini et al., 2004). The
viscoelasticity or apparent viscosity of yogurt can be
increased 2 to 3 times by adjusting the total solids and
protein contents or by adding thickeners or enzymes to
the milk base. Addition of thickeners (polysaccharides
or gelatin) or enzymes (lactoperoxidase, protease, and
transglutaminase) allows for new cross-links in the network and enhances the rigidity of the gel and its waterholding capacity. Processing parameters, including
heat treatment, shearing, homogenization, and storage
period, affect texture and thickness-in-mouth of yogurt.
Starter cultures help to improve the smoothness and
water-holding capacity of yogurt, because they can produce exopolysaccharides (EPS) during fermentation
and gel formation. The addition of increasing levels of
-LG causes marked increases in storage modulus (G)
compared with -LA, and some differences in behavior
exist among the different -LG variants (GravelandBikker and Anema, 2003).
Heat treatment, one of the predominant processes of
dairy product manufacturing, leads to denaturation of
milk proteins and interaction among denatured milk
proteins, which may dramatically affect the texture and
consistency of yogurt (Mulvihill and Grufferty, 1995).
Whey proteins are much more heat-sensitive than casein. The denatured whey proteins interact with each
other to form soluble whey protein aggregates or interact with casein micelles to form whey protein-coated
casein micelles (Krzeminski et al., 2011). Most whey
proteins are denatured during normal heat treatment
of yogurt manufacture, during which the formation of
disulfide bonds and occurrence of hydrophobic interactions within denatured whey proteins and between
denatured whey proteins and -CN on the surface of
Low-fat yogurt has been attracting increasing attention from health-conscious consumers because of
its nutritional values and health-promoting properties
(Kckcetin, 2008). However, milk fat has important
roles in emulsification and in flavor and texture development in the formed gels. A reduced fat content may
reduce viscosity and increase whey syneresis, which can
affect the appearance, texture, and mouthfeel of lowfat yogurt (Lee and Lucey, 2004; Houz et al., 2005).
ZHAO ET AL.
4:1
3:1
2:1
1:1
12.94
0
4.0
12.94
12.13
0.33
4.0
12.46
10.78
0.87
4.0
11.65
8.08
1.96
4.0
10.04
ZHAO ET AL.
Table 2. Rheological properties (means SD) of low-fat yogurts fortified with different casein to whey protein ratios
Casein to whey protein ratio
Item
Fermentation time (min)
Gelation time (min)
pH at gelation
G (storage modulus) at pH 4.6 (Pa)
ad
4:1 (Control)
270.12
96.56
5.71
40.76
2.31
4.62a
0.01d
5.23d
3:1
262.22
88.42
5.78
51.12
Means within a row with different letters are significantly different (P < 0.05).
2:1
b
4.43
3.21b
0.02c
4.21c
251.23
81.22
5.82
118.82
1:1
c
5.82
3.11c
0.01b
13.23b
240.15
76.12
5.88
206.35
3.54d
1.24d
0.01a
23.45a
ZHAO ET AL.
Figure 3. Electron micrographs of low-fat yogurts produced with casein to whey protein (CN:WP) ratios of 4:1 (Control, A), 3:1 (B), 2:1
(C), and 1:1 (D). As the CN:WP ratio decreased, the crosslinked network became denser and finer, and the pores became smaller, as shown in
panels B, C, and D. The yogurt with a CN:WP of 1:1 (panel D) appeared the most homogeneous, with the smallest and most evenly distributed
pores. Color version available online.
Table 3. Disulfide bond content (mol/g of protein; means SD) of unheated and heated milk protein
samples with different casein to whey protein ratios
Casein to whey protein ratio
Treatment
Unheated (25C)
Heated (95C)
4:1 (Control)
d,B
0.20 0.01
14.28 1.47d,A
ad
3:1
2:1
c,B
0.23 0.01
20.07 1.51c,A
1:1
b,B
0.27 0.02
25.25 1.07b,A
Means within a row with different letters are significantly different (P < 0.05).
Means within a column with different letters are significantly different (P < 0.05).
A,B
0.33 0.03a,B
27.78 1.24a,A
Table 4. Surface hydrophobicity (S0, unitless; means SD) changes of unheated and heated milk protein samples with different casein to whey
protein ratios
Casein to whey protein ratio
Treatment
Unheated (25C)
Heated (95C)
4:1 (Control)
3:1
a,B
1,731.72 17.54
2,178.01 28.31d,A
2:1
b,B
1,567.23 18.38
2,565.02 14.27c,A
1:1
c,B
1,416.24 19.70
2,720.05 12.08b,A
1,351.32 17.64d,B
2,898.25 20.07a,A
ad
Means within a row with different letters are significantly different (P < 0.05).
Means within a column with different letters are significantly different (P < 0.05).
A,B
ZHAO ET AL.
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