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Studies on Milk Proteins. I. Conditioning of Milk Proteins with Pancreatic Enzymes

Research Laboratory, Armour and, Company, Chicago, Illinois

ABSTRACT

When milk is treated with minute amounts of active pancreatic enzymes and pasteurized immediately, its proteins undergo modifications. This change is evidenced by the fact that hard, strong clots no longer can be formed through the use of acids or coagulating enzymes such as pepsin or rennin. Conquest et al. (1) have described this action in connection with milk of reduced curd tension. Casein primarily is affected according to the work of Turner (3), who has obtained a greater solubility in 70 per cent ethyl alcohol in this protein separated from pancreatic enzyme-treated milk than that found in a normal control.

The laboratories of Armour and Company have been interested in studying caseins precipitated from acidified, pancreatic enzyme-treated milks and have noted a change somewhat different from the above. These caseins appear to be affected by heat in a manner opposite to the untreated control. For example, temperatures in excess of 150° F.