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Authors
Advisor(s)
Abstract(s)
The breakdown of as -caseins and ~-caseins (in the form of as -caseins, the form of
~-caseins, and the form of a mixture of as- and ~-caseins in Na-caseinate) by cardosin A, one of
the major two proteinases present in the flowers of Cynara cardunculus L., was experimentally studied
via urea polyacrylamide gel electrophoresis. In Na-caseinate, as- and ~-caseins were degraded
up to 46 and 76 %, respectively, by 10 h of hydrolysis. In separated form, as-caseins reached a
leveI of degradationup to 67 %while ~-caseins were quickly and extensively degraded up to 76 %.
Ingeneral, ~-caseins seemed to be more susceptible to proteolysis than as-caseins.
Description
Keywords
Milk protein Enzyme Plant rennet Electrophoresis
Pedagogical Context
Citation
SILVA, Sofia V; MALCATA, F. Xavier - Proteolysis of ovine caseins by cardosin A, an aspartic acid proteinase from Cynara cardunculus L. . Lait. ISSN 0023-7302. Vol. 78 (1998), p. 513-519
Publisher
INRA/Elsevier
