Author:
Creamer L. K.,Mills O. E.,Richards E. L.
Abstract
SummaryA study of the hydrolysis of β-casein-B by crystalline rennin or rennet extract at pH 6·5, using a disk electrophoresis technique, showed that 3 bonds in β-casein are appreciably more sensitive than the others to rennin proteolysis, and that these bonds are probably located near the C-terminus of the protein. The most susceptible bond is hydrolysed, at 10°C, about 200 times faster than any other bond, whilst at 37°C it is hydrolysed 60 times faster. A study of the hydrolysis of this bond showed that its rate of hydrolysis at 37°C and pH 6·5 is decreased by either increased ionic strength or increased calcium ion concentration at constant ionic strength. Conformational changes in the substrate are probably responsible for these effects.
Publisher
Cambridge University Press (CUP)
Subject
Animal Science and Zoology,General Medicine,Food Science
Cited by
46 articles.
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