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Journal of Dairy Science Vol. 59 No. 3 391-395
© 1976 by American Dairy Science Association ®
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Low Temperature Inactivation in Milk of Heat-Resistant Proteases from Psychrotrophic Bacteria1

J. T. Barach, D. M. Adams and M. L. Speck

Department of Food Science, North Carolina State University, Raleigh 27607

ABSTRACT

Development of bitter flavor or gelation in ultra-high temperature sterilized milk may be the result of bacterial proteases which survive the heat treatment. The heat-resistance of these proteases appear to preclude their destruction by heat during processing. These proteases, however, can be inactivated at pasteurization temperatures apparendy by some mechanism other dian or in addition to heat. The parameters for this low temperature inactivation of these proteases were investigated. Activity of buffer solutions of bacterial proteases was reduced by more than 90% during 10 min at 55 C. Inactivation of protease in raw or sterile milk was slower and less complete but approached 70% during 60 min at 55 C. Effectiveness of the low temperature inactivation treatment appeared to be independent of protease concentration. The treatment did not alter the flavor or casein composition of raw or ultra-high temperature sterilized milk containing protease much greater than would be expected to occur normally in milk.


FOOTNOTES

1 Paper Number 4742 of the Journal Series of the North Carolina Agricultural Experiment Station, Raleigh. The use of trade names in this publication does not imply endorsement by the North Carolina Agricultural Experiment Station of the products named, nor criticism of similar ones not mentioned.







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Copyright © 1976 by the American Dairy Science Association ®.