Proteolytic activities of suparen and rennilase on buffalo, cow, and goat whole casein and beta-casein.
The proteolytic specificity and activity of Mucor miehei protease (Rennilase) and Endothia parasitica protease (Suparen) on buffalo, cow, and goat whole casein and beta-casein (CN) were studied by analyzing the degradation products. The results suggest that Rennilase hydrolyzes casein of the three species in a manner similar to that of chymosin, resulting in the formation of alpha(s1)-I and beta-I, -II, -III as initial degradation fragments of alpha(s1)- and beta-CN. alpha(s1)-I was also the initial breakdown product of alpha(s1)-CN by Suparen. Contrary to Rennilase, Suparen showed a higher affinity toward beta-CN and hydrolyzes beta-CN, giving rise to degradation products characterized by mobility lower than that of beta-CN. Increasing NaCl concentration (>3%) reduced the proteolysis of beta-CN of the three species by Rennilase but not by Suparen. The hydrolysis of alpha(s1)-CN and alpha(s1)-I by the two enzymes was enhanced in the presence of NaCl.
Awad
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Laboratory of Dairy Science, Institute of Food Science, Swiss Federal Institute of Technology, CH-8092 Zürich, Switzerland.
Lüthi-Peng
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Puhan
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D000818:Animals; D002020:Buffaloes; D002364:Caseins / Q000378:metabolism*; D002417:Cattle; D012085:Chymosin / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D005260:Female; D006041:Goats; D006868:Hydrolysis; D020033:Protein Isoforms / Q000378:metabolism
D002364:Caseins; D020033:Protein Isoforms; D010450:Endopeptidases; C412900:rennilase; C412901:suparen; D012085:Chymosin