Partial Purification and Some Properties of a Benzhydrylamide-bond Hydrolyzing Enzyme in Pseudomonas diminuta |
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| Authors: | Mineyuki Hayashi Masanaru Misawa |
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| Institution: | Tokyo Research Laboratory, Kyowa Hakko Kogyo Co., 3–6–6 Asahicho, Machida, Tokyo 194, Japan |
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| Abstract: | An enzyme in Pseudomonas diminuta showed hydrolyzing activity of a benzhydrylamide ( = diphenylmethylamide) bond in S-benzylcysteinylglycine benzhydrylamide. The enzyme was purified 225-fold by precipitation with ammonium sulfate, and column chromatography with ECTEOLA-cellulose, DEAE-cellulose and hydroxyapatite. It showed an optimum pH of 6 to 8 and it was markedly inhibited by Hg2 + or p-chloromercuribenzoate. The preparation was more specific against S-benzylcysteinylglycine benzhydrylamide than other substrates tested. |
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| Keywords: | anoretic activity enterostatin glycinin hypocholesterolemic activity soybean |
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