Proposed Mechanism for the Antioxygenic Action of Trypsin in Milk
Open Access
- 1 June 1972
- journal article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 55 (6) , 753-758
- https://doi.org/10.3168/jds.s0022-0302(72)85568-1
Abstract
The treatment of milk with trypsin (3.4.4.4) increases the resistance of milk lipids to oxidation as demonstrated by flavor scores and thiobarbiturie acid. Evidence from milk points to the conclu- sion that ~he antioxygenic effect of the enzyme is due to its ability to increase the copper binding capacity of milk and is a function of the degree of proteolysis. Electrophoretic analysis of major milk proteins revealed that trypsin hydrolyzes casein but not the fl-lactog)obulins.Keywords
This publication has 8 references indexed in Scilit:
- Rapid Methods for Determining Copper Content of MilkJournal of Dairy Science, 1967
- Genetic Polymorphism in Caseins of Cows’ Milk. II. Confirmation of the Genetic Control of β-Casein VariationJournal of Dairy Science, 1964
- Protein phenotyping by direct polyacrylamide-gel electrophoresis of whole milkBiochimica et Biophysica Acta (BBA) - General Subjects, 1964
- Oxidation of Milk Fat Globule Membrane Material. I. Thiobarbituric Acid Reaction as a Measure of Oxidized Flavor in Milk and Model SystemsJournal of Dairy Science, 1962
- Influence of Protein Hydrolysis on the Susceptibility of Milk to Oxidized Flavor DevelopmentJournal of Dairy Science, 1953
- The Thermodynamics of Metallo—Protein Combinations. Comparison of Copper Complexes with Natural ProteinsJournal of the American Chemical Society, 1952
- The Spectra of Copper Complexes with Some Proteins, Amino Acids, and Related Substances.The Journal of Physical Chemistry, 1950
- Oxidized Flavor in Milk. XIV. A Possible Mode of Action of Inhibitors in Preventing the Development of Oxidized Flavor in MilkJournal of Dairy Science, 1944