A new alkaline elastase of an alkalophilic bacillus.
A new alkaline elastase was purified from the culture broth of an alkalophilic Bacillus sp. Ya-B. This was a serine proteinase. Molecular weight was 25,000. The optimum pH for elastin and casein was 11.75. The enzyme had very high specific activity, 12,400 units/mg protein for casein, and 2,440 units/mg protein for elastin at the optimum pH. It showed marked preference for elastin. The relative activity of elastin/casein of this enzyme was 17 and 6 times higher than those of subtilisin BPN' and subtilisin Carlsberg, respectively. This enzyme also had higher keratin and collagen hydrolyzing activity in comparison with subtilisin.
D001407:Bacillus / Q000201:enzymology*; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000302:isolation & purification* / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D012697:Serine Endopeptidases; D013379:Substrate Specificity
D011480:Protease Inhibitors; D010450:Endopeptidases; D012697:Serine Endopeptidases; C042629:alkaline elastase; D010196:Pancreatic Elastase