Intracellular acid carboxypeptidase ofPenicillium roqueforti isolated from blue cheese |
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| Authors: | Eiji Ichishima Michio Takeuchi Kazuo Yamamoto Yoshiyuki Sano toshihiko Kikuchi |
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| Affiliation: | (1) Laboratory of Enzymology and Microbial Chemistry, tokyo Noko University, Fuchu, 183 Tokyo, Japan;(2) Technical Laboratories of Snow Brand Milk Products Co., Kawagoe, 350 Saitama, Japan |
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| Abstract: | We found thatPenicillium roqueforti isolated from a commercial blue cheese produced an acid carboxypeptidase. The acid carboxypeptidase was present in mycelia and little was detected in the liquid medium. The optimum pH for benzyloxycarbonyl-Glu-Tyr was 3.6. The enzyme had the ability to liberate the carboxyterminal amino acid (leucine) of angiotensin I at pH 3.6. Furthermore, the enzyme liberated the carboxyterminal proline from benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro. The molecular weight of the enzyme determined by gel filtration on Sephadex G-200 was 155,000. The acid carboxypeptidase was inhibited by phenylmethanesulfonyl fluoride and hydrocinnamic acid. |
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