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来自黄曲霉的一种真菌凝乳酶的生理学与特性

Physiology and characterization of a fungal milk-clotting enzyme from Aspergillus flavus.

作者信息

Foda M S, Ismail A A, Khorshid M A, El-Naggar M R

出版信息

Acta Microbiol Pol. 1976;25(4):337-43.

PMID:65107
Abstract

Aspergillus flavus produced extracellularly an active rennin-like enzyme when grown aerobically in whey media. The enzyme was detected at early stages of growth reaching a maximum after three to four days at 25 degrees. The activity was destroyed by heating to temperatures higher than 50 degrees, whereas the presence of skim milk during heating preserved the enzyme activity, at least, up to 70 degrees. Calcium chloride significantly stimulated the milk-clotting activity up to 1% final concentration. The clotting time was inversely proportional to protein concentration in the range 0.2-0.6 mg/ml and the enzyme exhibited marked stability when stored at 37 degrees at pH 6.

摘要

黄曲霉在乳清培养基中好氧生长时会分泌一种具有活性的类凝乳酶。该酶在生长早期即可检测到,在25摄氏度下培养三到四天后达到最大值。加热至高于50摄氏度时酶活性被破坏,而加热过程中存在脱脂牛奶至少可使酶活性保持至70摄氏度。氯化钙在终浓度达1%时可显著刺激凝乳活性。在0.2 - 0.6毫克/毫升范围内,凝结时间与蛋白质浓度成反比,并且该酶在pH值为6、37摄氏度下储存时表现出显著的稳定性。

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