Blackwell Publishing Journal Backfiles 1879-2005
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
Process Engineering, Biotechnology, Nutrition Technology
Two proteinases (A and B) were isolated from Atlantic menhaden muscle with molecular weights of 112,000 and 90,500 daltons, respectively. Proteinase B had higher activity than A for protein substrates except casein; proteinase B had no caseinolytic activity. Both proteinases hydrolyzed synthetic substrates such as Z-Phe-Arg-NMecand TAME, but not BAEE and BAPNA. Optimum Z-Phe-Arg-NMec hydrolyzing activity was shown at pH 7.4, 40 to 50 °C for both proteinases A and B. Activities of A and B in the presence of 3.0% NaCl were reduced to 71.2% and 62.2%, respectively. Both proteinases were inhibited by 1 mM TLCK, 1 mM benzamidine, 1% egg white, and 1% bovine plasma hydrolysate. Proteinases A and B are most likely tryptic serine type proteinases.
Type of Medium: