You are on page 1of 13

The first step in the digestion of milk is that of coagulating or curding.

Milk may be made to


curdle by adding an acid to it, such as lemon juice or some other acid fruit juice or by the
hydrochloric acid of the stomach. Normally, the coagulation of milk in the stomach of a young
mammal is done by an enzyme secreted by glands in the stomach and known as rennin. This
enzyme is especially abundant in the mucous lining of the stomach of young mammals and is
extracted to be used in the manufacture of cheese.
The fifth edition of Harpers Review of Physiological Chemistry (p. 177, 1955) says of rennin:
This enzyme causes coagulation of milk, and is important in the digestive processes of infants
because it prevents the rapid passage of milk from the stomach. In the presence of calcium
rennin changes irreversibly the casein of milk to a paracasein which is then acted upon by
pepsin. This enzyme is said to be absent from the stomach of adults.
Although, heretofore, it has been thought that the sole function of rennin is to coaugulate milk, it
seems from Harpers statement that it may be a true digestive enzyme. It changes casein to
paracasein so that pepsin can act upon it. Enzymes are specific in their action. Each enzyme acts
upon a particular type of food and certain of these can act upon a starch or a protein only after
other enzymes have first acted upon them and changed them from their original composition.
Harpers statement seems to imply that pepsin acts upon paracasein rather than upon casein.
If this is the true relation of pepsin to the digestion of casein it means that rennin is essential to
the efficient digestion of this protein. Rennin becomes of far greater importance in the digestion
of milk than has heretofore been thought.
Rennin has been the subject of much controversy among physiologists. There was, first, the
question: does rennin exist or does pepsin do the work ascribed to this enzyme? French and
German investigators finally succeeded in establishing, to the satisfaction of everyone
concerned, the existence of rennin as separate from pepsin. This did not end the controversy.
While investigators now admit that rennin does, indeed, exist, many of them assert that it never
exists in the human stomach, contending that it is found only in the fourth stomach of the calf.
In his Advances in Enzymology (London, 1954) Berridge defends the view that rennin is never
found in the human stomach. He says that Experiment tends to confirm the absence of rennin
from human gastric juice. On the other hand, Eusterman and Balfour, in The Stomach and the
Duodenum (1936) state that, according to a number of investigators, rennin tends to disappear
from the adult stomach. This statement implies that somebody, somewhere, found rennin in the
human stomach, while its disappearance from the adult stomach has led to the suggestion that
Berridge, who makes no distinction between infants and adults, made all of his experiments on
adults.

In the second edition of his Textbook of Medical Physiology 1961 Arthur C. Guyton, M.D.,
says rennin is found in the gastric juice of babies in large quantities, but it is present only to a
very slight extent if at all in the gastric juice of adults. Also casein seems to be digested by babies
much more easily than it is by adults, presumably because of rennin activity in the babys
stomach.
In the 1950 edition of The Physiological Basis of Medical Practice, Best and Taylor say that the
rennin content of adults is low and provide us with the following data: Rennin is especially
abundant in the gastric mucosa of young animals, while pepsin is present in minimal amounts
The optimum pH for the action of rennin is between 5 and 6.5, and it is quite inactive at the pH
of the gastric contents of the normal adult. In the infant, however, the pH of the gastric contents
(5-6.5) is around the optimum for the action of this enzyme.
This indicates that the digestive processes required for the digestion of milk are somewhat
different from those required for other foods and especially for other proteins. It is essential that
the milk be coagulated and that the casein be converted into paracasein. I have seen two patients
on a milk diet in which the milk did not coagulate, but was rushed along the digestive track into
the colon and expelled in an unchanged fluid state. A glass of milk would be taken and in less
than five minutes it would pass from the colon. Perhaps, in the absence of coagulation, milk
would never be digested, but would pass through the digestive track too rapidly for the digestive
enzymes to do their work.
In large numbers of other cases I have seen very large stools pass that were composed of large,
hard milk curds that were white, apparently having undergone no digestion. Coagulation alone is
not sufficient to assure the digestion of milk. In a few of these cases, the curds have been so large
and there have been so many of them that bowel impaction resulted. We frequently see white
curds in
the stools of infants, indicating that, although the milk coagulated, apparently in a normal
manner, the curds were not digested. We assume in these cases that milk has been taken in excess
of enzymic capacity.
As rennin is active in low acid medium and is inactivated by the normal gastric juice of the adult,
and as it is concerned solely with the digestion of milk, it should come as no surprise to us to
learn that it is not secreted by the adult stomach. In this connection it should be stressed that the
acidity of the juice poured into the stomach is determined by the food eaten. Milk taken alone
will occasion the flow of gastric juice that is low in acidity. Even in early childhood, when there
is still a supply of rennin in the stomach, taking flesh, eggs or other protein at the same meal with
milk will tend to result in the secretion of a highly acid gastric juice that will destroy or
inactivate the rennin and interfere with or retard milk digestion, hence the wisdom of our rule:
take milk alone or let it alone.

Rennin is apparently involved exclusively in the digestion of milk and tends to disappear from
the gastric juice (is no longer secreted by the stomach) when the normal time to wean the child
approaches. Some physiologists say that the concentration of rennin in the adult gastric juice is
low; others say it isnt detectable. A two year old baby normally has a mouth full of teeth and can
begin eating solid foods. At this age, also, the salivary glands begin the secretion of the enzyme
ptyalin, which is necessary to starch digestion! Intestinal enzymes essential to starch digestion
begin to be secreted at this time, also.
Thus, both the presence of adequate chewing apparatus and the secretion of digestive enzymes
indicate that now is the time to begin the feeding of solid foods. In an article by a dentist, which
appeared a few years ago, the author makes the statement that the baby should be weaned when
the first two teeth are cut, as this signifies that solid foods are now to be taken. Of all persons a
dentist should know that two teeth do not enable a baby to chew foods adequately. As these first
two teeth are in the front (are biters and not chewers), the baby is certainly not physiologically or
anatomically equipped for such chewing.
When the first teeth are through and the starch-splitting enzymes are being secreted, there starts a
decline in the production of rennin; this is to say, its secretion begins to decline at the age of two.
It continues to be secreted in decreasing amounts during the next three to four years, that is,
during what I have called the transition period (see Hygienic Care of Children), in which the
child is normally making the transition from the exclusive milk diet of infancy to the solid food
diet of later life. During this transition period milk is normally taken. Should it surprise us to
learn that when the child reaches the age at which it should normally be fully weaned its
digestive glands cease to secrete the enzymes that are specially related to milk digestion?
One question comes to mind that I can find no data for an answer. It is this: Does the individual
who continues to take milk regularly, from infancy into adulthood, continue to secrete rennin for
a longer period of time than does the individual who is weaned at the normal weaning time of
three to five years? This is to ask: Does the stomach continue to secrete rennin for an abnormally
long period of time if the infant diet is persisted into late childhood and thereafter? Does the
persistence of the need for rennin cause the body to continue to secrete it? If it does continue to
secrete this digestive enzyme longer than normal, at what time of life does it disappear from the
digestive juice of the stomach? If it continues to secrete rennin but in much decreased amounts,
in those who continue to take milk, does this account for the fact that some physiologists find no
trace of rennin in the subjects they use in their tests?
While the answer to this question (I have cut it up into several subordinate questions) may prove
to be of no great practical value, it would prove interesting as well as instructive concerning the
power of the body to adjust itself to varying circumstances of life, especially its power of the
body to adapt its digestive juices and enzymes to the food eaten. Every such advance in

knowledge of the chemistry of digestion provides us with added data to assist us in determining,
not only the normal diet of man, but, also, and of equal importance, the normal mode of feeding.
Todays nutritionists wholly neglect all natural indications of the normal feeding of man. One
food is as good as another and any food is equally as good at any time of life as at another,
providing the commercial manipulators of our foodstuffs can prepare it in a manner that it is
acceptable to all ages. For example, although we know that during the first period of life after
birth, even the lion cub does not eat flesh, our nutritionists do not hesitate to advocate flesh food
for the human infant at a period of its development when the young carnivores of all kinds are
still drawing their nutriment from the maternal font. Arrogance and egotism cause them to
assume that they can improve the normal order of feeding. The results of their efforts are not
encouraging.
While considerable confusion exists about rennin, there is one thing about which there is general
agreement: namely, the adult human stomach has no rennin. Berg and others have shown that the
adult organism does not use milk as efficiently as the rapidly growing organism and that, milk is
base-forming in the infant and acid-forming in the adult. Berg attributed this to the more rapidly
growing organism. May it not be, in light of the foregoing that the greater efficiency of the young
animal in assimilating milk rests upon the fact that the infant and young child digest milk better?
This suggestion derives support from the fact noted by Berg and others, that, adult organisms
handle sour milk more efficiently, the characteristics of the milk having been greatly altered by
the ferment action of bacteria.
Every indication of nature is contrary to the present dogma of the dairy industry and the medical
profession that we must take our quart of milk every day so long as we live; that, even at the age
of a hundred, we are not to be weaned. Nature indicates that we are to be weaned at an early
age. In medical circles the tendency of the pendulum, just at present, is to swing violently and far
in the opposite direction. In increasing numbers, medical men are blaming milk for a growing
number of illnesses in children and adults. From being the all-good milk is rapidly becoming the
all-bad. Certainly the assumption that invalids and convalescents, who have weak digestive
powers, should be fed milk like an infant, because in their enfeebled condition they can handle
milk better than other foods, is no longer tenable.
The Hygienist will see in all these facts a justification of Grahams condemnation of the use of
milk and milk products by the adult and his observation that the use of milk by the adult makes
him logy and lazy. Trall also pointed out that milk is not a normal part of the adult diet. Those of
us who have had an extensive experience with the milk diet, formerly so strenuously advocated
as a near-panacea, will discover in the foregoing facts at least partial explanation of the many
troubles that the milk diet produced. Polyuria, constipation, diarrhea, bowel impaction, nausea,
much gas and discomfort, increased blood pressure, a water-logged state of the tissues (edema),

catarrh, indigestion and other troubles arising out of the harmless practice of overfeeding on
milk, necessitated all manners of manipulations to make it acceptable to patients.

Both the evaporation of water and the coagulation of the proteins work together to form a skin on
the surface of cooked milk dishes like creamy soups, puddings, and even a mug of hot chocolate.
The thickness and chewiness of the skin is affected by how hot the milk is heated (resulting in
more evaporation and coagulation) and the fat content in the milk (which encourages
coagulation). The skin starts forming on the stovetop and continues forming as the dish cools.
The easiest way to prevent a skin from forming is to stir the milk as it heats and then to continue
stirring occasionally as it cools. This breaks up the protein clumps and makes sure the
temperature of the milk stays even throughout. Pressing plastic wrap or wax paper against the
surface of a cooling dish also discourages a skin from forming. This prevents evaporation and
keeps the surface moist.

The term denaturation is used more frequently than coagulation by scientific investigators at the
present time to denote certain changes in proteins. Definite characteristics of the proteins are
changed when they are coagulated, among which is loss of solubility in water and dilute salt
solutions. In some instances and under certain conditions the coagulation process may be
reversible.
Manner in which denaturation may be brought about. Coagulation of proteins may be brought
about by a variety of processes. In cookery one of the principal means of coagulation is heat. But
in addition to heat the action of acids, alkalies, salts, alcohol, mechanical agitation, radiation, and
ultra-sonic vibrations may denature the protein and convert it from a soluble into an insoluble
form.
Some changes in the proteins during denaturation. All investigators agree that denaturation is
brought about in two steps. The first step is a preliminary alteration of the protein or
denaturation. The second is a physical change which leads to coagulation or aggregation. Clayton
in discussing "Foods as Colloid Systems" reviews some of the theories of protein denaturation.
"Hydrolysis has been frequently reported as the cause of denaturation, but present views incline
to the idea of some structural rearrangement within the molecule. Thus, the refractive index
increases during heat denaturation, whilst X-ray diffraction patterns lead to the view that
coagulation is accompanied by the elimination of water between NH1 and COOH groups. . . .
Cubin holds that denaturation is the distortion or opening up of the protein unit, whilst
flocculation is the process following this and rendered possible by it. Interaction of NH1 and
COOH groups situated on contiguous colloid units leads to aggregation and, hence, coagulation."
No matter how denaturation is brought about, the denatured product has sulfur atoms, the
combination of which differs from those in the native protein. Mirsky and Anson have shown
that in native egg albumin no sulfhydryl (SH) and disulfide (S-S) groups are detectable by
certain methods. But in completely coagulated protein the number of SH and S-S groups
detectable is the same as in hydrolyzed protein. These workers have also shown that in partially
coagulated protein when the soluble and insoluble fractions are separated the soluble portion
contains no detectable SH or S-S groups, but the insoluble fraction has the number of reactive
SH and S-S groups characteristic of the completely denatured protein. In the interfacial
coagulation of a protein, i.e., when a film of insoluble protein forms at the surface of a protein
solution, SH and S-S groups appear, the number being the same as that found in the hydrolyzed
protein. Also when the proteins are denatured by ultra-violet light, by acids, or by other means
the SH and S-S groups appear. From these results they conclude that the formation of insoluble
proteins and increase in detectable SH and S-S groups are closely linked phenomena; that
denaturation is a definite chemical reaction; and that a given protein molecule is either
completely native or completely denaturated.
In a later paper Mirsky and Anson report that the number of detectable SH and S-S groups in
different proteins varies with the pH and the temperature. To illustrate, native hemoglobin had no
detectable SH groups at pH 6.8. But with increase of pH the SH groups become detectable in
increasing numbers up to pH 9.6. But native egg albumin showed no detectable group at pH 6.8
or pH 9.6. However, denatured hemoglobin had detectable groups at pH 6.8 and still more at pH

9.6. They found that intact, unhydrolyzed proteins possess in addition to SH groups other
reducing groups which can be oxidized by ferricyanide. The number and activity of these groups
vary from protein to protein. They are probably contained in the tyrosine and tryptophane
component of proteins. "It can now be seen that the activation of SH and S-S groups in protein
denatura-tion is part of a more general process."
Heat coagulation. As has been indicated heat coagulation of proteins is used in preparation of
food products, and, fortunately for the mental equilibrium of the cook, heat coagulation of
proteins is ordinarily not reversible. Otherwise, many cooked dishes would, with certain
treatment, revert to their original uncooked consistency.
Some of the changes occurring during heat coagulation of the proteins have been indicated. But
these are not the only factors playing a role in the process. Electrolytes have some role in heat
coagulation of proteins. This is shown in the work with distilled water egg custards. It has been
shown that, if the mineral content of egg white is lowered through dialysis, coagulation does not
occur on heating. The effect of electrolytes in heat coagulation may be brought about either by
chemical reaction or by adsorption. If the effect of salts is brought about by adsorption, the salts
must be very strongly adsorbed and almost impossible to remove from the aggregated protein by
washing the protein, for the process is usually irreversible. Any theory of heat coagulation of the
proteins must not only explain how the proteins are rendered insoluble by heat but the effect of
other factors. That the heat coagulation of proteins is influenced by electrolytes, sugar,
temperature, time, the reaction of the solution, and the presence of water and other factors is
evident when the cooking of eggs, custards, salad dressings, cheese and egg dishes, baked
products, and meat is observed. The effect of some of these factors can be determined in the
laboratory; but the understanding of the manner of their action is lacking in many instances and
awaits explanation by the colloid chemist or biochemist.
Bancroft and Rutzler have reported that heat-coagulated egg white may be peptized by dextrose
and certain salts. They showed that the coagulated and repeptized egg-white sols are identical
with the original solution by immuno-biological tests for species specificity and isoelectric point
measurements. Because of the similarity of the reversed protein to the original protein they
believe that coagulation is a colloidal reaction which is due to a physical rather than a chemical
change.
Interfacial denaturation. Proteins are also denatured at interfaces, typical examples being the
insoluble portion of beaten egg white, and froth or foam on milk. When egg white or milk foams
are allowed to remain undisturbed, they gradually collapse and the wrinkled membranes, skin, or
films may be observed through the microscope. Mention has already been made that protein can
be recovered from a solution by removing the foam. Denaturation of protein solution occurs by
shaking and in some instances spontaneously, an example being the membrane formed at the
interface of an air/protein solution when no agitation has occurred.
Neurath and Bull state that both heat and surface denaturation processes involve an unfolding of
the peptide chains which in the natural state are curled up in the interior of the molecule and
become stretched out when the molecule comes in contact with the surface of the bulk of the
solution. The polar groups of the protein molecule, the amino, carboxyl, the OH groups of the

hydroxy acids, the sulfur-containing groups, and the peptide linkages, have an affinity for water;
whereas the non-polar or lyophobic groups, the hydrocarbon residues, tend to be repelled by
water. Thinking that an interaction between the amino and carboxyl groups during heat
denaturation might diminish the lyophobic or polar properties of natural protein, whereas an
unfolding of the peptide chains by surface denaturation might expose lyophobic groups to the
surface, which in the native state are buried in the interior, Neurath and Bull measured the
volume contraction of native, heat-denatured, and surface-denatured proteins. They found that
the native protein had the lowest density, heat-denatured ones were intermediate, and the surfacedenatured protein had the highest density.
This membrane-forming property of protein through denaturation is important in food
preparation, in all products in which beaten egg white is used, in emulsions, and wherever
interfacial reactions occur.
Membranes form readily on the surface of protoplasm and play important parts in cell functions.
The presence of calcium has been shown to stiffen the surface membranes in some instances,
whereas sodium and potassium in the absence of calcium tend to soften and dissolve the
membrane.
This suggests that salts may also have some influence in surface denatura-tion and that the salts
of flour, egg, and milk used in cooked products may modify the denaturation at surfaces.
Clayton states that high concentrations of sugar in egg white will prevent surface denaturation,
which of course has application in making angel cakes, meringues, and sweetened souffle
Read more: http://chestofbooks.com/food/science/Experimental-Cookery/Coagulation-OfProteins.html#ixzz45kLcrSDH

Raw food is wonderful because it is rich in the vitamins and minerals which the healthy or sick
body always needs for its immediate well-being and for bodily storage (Sherman). The human
digestive tract is not always, or not in every individual, capable of handling an exclusive raw
dietary, because it is just not as strong as the larger stomach of a cow or a horse.
The human digestive system resembles that of the ape. The diet of the ape is closer to the ideal
than the diet of modern man. Dr. Kellog, in his excellent and scholarly work, The New Dietetics,
discusses this important issue as follows: Man, like the chimpanzee or the orang-outang, has a
simple digestive machinery adapted to the digestion of fruits, nuts, grains, eggs, and milk. It is a
feeble stomach, like the stomach of primates, the aristocrats of the animal kingdom, adapted to
the digestion of the choicest of natures tidbits.
Dr. Kellogg further makes the point that man does gastronomic stunts from which the hardiest
beast of the forest would recoil. The modern home or public eating place concocts the most
unwholesome food mixtures. The basic food values of these food mixtures are destroyed in their
process of preparation. The vitamins and minerals are destroyed by cooking. Foods are made
indigestible by adding fat to boil, fry or roast, and made further indigestible and otherwise
injurious by the addition of salt, pepper, and other spices and condiments.
Modern dinnerplates are heaped with devitalizing, health-destroying eatables. Ordinary cookery
furnishes gas-forming soups, acid-forming entrees, ulcer-forming sugar-sweetened desserts.
A health-building dietary must exclude ordinary table sugar (sucrose) or even brown sugar,
because it has been demonstrated that sugar produces inflammation of the mucous membranes of
the stomach, intestines, nose and throat, and of the deeper structures-the joints, the nerves, the
heart, the arteries. When sugar is used in excess-or when sugar is used in such per-capita
proportions as the American people use it (two pounds per person per week)-it must be a
contributing basic cause of the acute and chronic diseases that are characterized by inflammation.
Here is an important tip to doctors as well as laymen: Stop buying sugar as food. Let the
industrial chemists make use of this product, as they are already doing, for the manufacture of
wonderful synthetic products such as the clothes we wear, the toothbrushes we use, etc.
To come back to the important subject under discussionthat of raw food versus cooked foodStarchy foods are easier to digest when cooked or baked or toasted- The chemical term
hydrolysis means the addition of water to the starch, a kind of predigestion of starch. In other
words, by cooking cereals, such as Wheatena, rice, oatmeal or any other grain food, in water, the
heat and the water soften the starch granules, thereby making them more easily available to the
digestive machinery of the human economy.

Starch, like any other food, should be cooked without salt or butter. The salt would harden the
cellular structure of the grain and would therefore make it difficult to digest. This is one
objection to adding salt during the cooking of any foods. Another objection to salt is that the
body treats it as an unwanted product- The kidneys must excrete it. If a person suffers from
kidney deficiency, salt remains with-in the blood and tissues and tends to contribute to sclerosis
or hardening of the arteries, etc.
A baked potato is easier to digest than a raw potato, or even than a boiled potato, because the
potato contains more water than do the grain foods. It therefore becomes ideally cooked by the
higher temperature of baking. The heat of the baking temperature converts the raw potato starch
plus its water content (about 80 per cent) into an easily digestible food.
Those people who choose to live on a raw food diet should include baked potato and some form
of cooked grain such as brown rice, buck-wheat, millet, wholewheat or oatmeal, in order not to
starve their bodies of the B vitamins. The B vitamins are found in these grain foods. These are
the vitamins that are not destroyed by cooking, aging or staleness. Vitamins A, C and D, and
minerals besides, are found in the raw fruits and raw vegetables. It is for this reason that raw
foods should be consumed in high daily rations.
A phenomenon recognized as hidden hunger is sometimes mentioned by nutrition authoritiesThose individuals who suffer from hidden hunger crave sweets and stimulants. What they
really lack are the foods that are rich in vitamins and minerals.
Modern men and women do not know as much about their food needs as they know about other
personal needs. To form scientifically correct habits in the modern adult requires a kind of reeducation from wrong to right. It is necessary to remove him for a time from the temptation to
want coffee, tea, cake, or injurious entrees that make it impossible to attain good health.
Raw vegetable salads and fresh raw fruits are considered as extras which unenlightened
(though educated) people of our time omit from their daily food intake. (Frozen fruits, frozen
fruit juices, and frozen vegetables are not as heathful as the fresh market raw fruits and
vegetables.) I believe that the adult person requires between 60 to 75 per cent of raw food in the
daily bill of fare.
Breakfast may be composed entirely of raw fruits. An energetic, healthy person will not feel
weak on arising in the morning, requiring bread, eggs and other conventional breakfast foods.
The noon meal may be composed of one raw food and one cooked dish (see menus for breakfast
and luncheon combinations). Dinners can be banquet meals every day of the week without
requiring much processing or preparation.

The modern housewife, restaurant cook, institutional cook or caterer put together the most
unwholesome mixtures. In the future, food preparation will be based on the New Knowledge of
Nutrition. Foods will be selected and served in attractive and wholesome dishes that will really
enhance the health and well-being of the race. Eating properly prepared and combined foods will
eliminate one of the causes of widely prevalent diseases of the stomach and intestines.
I believe that it is good for the body to use a certain percentage of cooked foods. The legumes
(the beans, peas, and lentils) are excel-lent sources of protein, starch, minerals and vitamins that
are avail-able for human nutrition only after they are properly cooked or baked. The human
stomach and intestines cannot digest these products in their raw state as can quadruped animals,
such as the horse and the cow.
The healthy human stomach can digest one variety of legume in the raw statepeanuts. Peanuts
are easier to digest raw than roasted because in the process of roasting the fat content is
decomposed, making this excellent food difficult to digest. For the same reason, other kinds of
nuts should be eaten in their fresh raw state, rather than roasted or salted.
Nuts combine ideally with raw fruit and raw salads. The digestion of nuts require a good, healthy
stomach and an abundance of nerve energy. Those who are rather delicate physically, or even
emotionally, must limit their food intake to the lighter varieties.
The foods that are most easily digested are cooked cereals, baked potatoes and fresh raw honeyall for the bodys immediate energy needs. Fats, such as butter, cream, and oil, are also
comparatively easy to digest when used uncooked and unfried, in small amounts, as seasoning
only.
People who are very sturdy may live on a raw diet, even excluding animal products such as
butterfat, eggs and milk. A choice of ideal raw foods to make up a health-promoting dietary
would have to include the aligator pear or avocado as a source of fat and protein; nuts can be
used for the same bodily needs. Fresh raw fruits and vegetables taken in juice form, and some in
salad form, will avoid a bulging abdomen. The human digestive tract cannot handle as much
roughage as some people consume in large platefuls of raw salad courses.
In summary, a raw food diet can be followed by those who are strong physically and have a
robust nervous system. Such people can nourish their bodies to great advantage without any
cooked and baked foods. The majority, however, must use a certain amount of cooked food. One
meal a day, or even two, should contain one or two adequately chosen and prepared cooked food
cours