On the activity and specificity of cardosin B, a plant proteinase, on ovine caseins

• Tipo: Artigo em Revista Científica Internacional
• Data: 1999

Autores

Silva, SV (Autor) Outra; F. Xavier Malcata (Autor) Outra

Revista

Título: Food Chemistry

Vol. 67

Páginas: 373-378

ISSN: 0308-8146

Editora: Elsevier

Indexação

ISI Web of Knowledge - 25 Citações

Scopus - 32 Citações

Outras Informações

ID Authenticus: P-001-2N5

DOI: 10.1016/s0308-8146(99)00126-0

Abstract (EN): The proteolytic activity of cardosin B, an aspartic proteinase from the thistle, Cynara cardunculus, on ovine alpha(s)-caseins and beta-caseins (independently or present together in sodium caseinate) was followed by urea polyacrylamide gel electrophoresis and reversed phase high performance liquid chromatography. This enzyme degraded both types of caseins, but not to the same degree. In sodium-caseinate, by 10 h at 30 degrees C, alpha(s)-caseins were more susceptible to proteolysis by cardosin B than beta-casein whereas, in isolated form, the reverse was observed. Sequencing of the peptides produced by hydrolysis of Na-caseinate showed that the major cleavage sites in alpha 1-casein were Leu156-Asp157 and Trp164-Tyr165 whereas, in beta-casein, they were Leu127-Thr128, Leu165-Ser166 and Leu90-Tyr191. The bonds Trp164-Tyr165 and Leu165-Ser166 were the most susceptible to cardosin B when this enzyme acted upon isolated alpha(s1)- and beta-casein, respectively.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 6