Comparative catalytic activity of two plant proteinases upon caprine caseins in solution

• Type: Article in International Scientific Journal
• Date: 2000

Authors

Silva, SV (Author) Other; F. Xavier Malcata (Author) Other

Journal

Title: Food Chemistry

Vol. 71

Pages: 207-214

ISSN: 0308-8146

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 12 Citations

Scopus - 14 Citations

Other information

Authenticus ID: P-000-YJR

DOI: 10.1016/s0308-8146(00)00157-6

Abstract (EN): The proteolytic activities of cardosins A and B, two (plant) proteinases from Cynara cardunculus, toward caprine caseins, independently, or in the presence of each other as Na-caseinate, were studied in a comparative fashion using polyacrylamide gel electrophoresis and reversed phase high performance liquid chromatography. The electrophoretic degradation patterns of both alpha(s)- and beta-casein, brought about by the cardosins, were similar to one another. In what concerns the specificity of these two enzymes upon caseinate. the major cleavage sites were Leu127-Thr128 and Leu190-Tyr191, both in beta-casein. When caseins were tested independently, both cardosins cleaved Phe153-Tyr153 in alpha(s1)-casein, as well as Leu127-Thr128 and Leu190-Tyr191 in beta-casein.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 8