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凝乳酶生化特性的研究。

Investigations on biochemical properties of milk-clotting enzymes.

作者信息

Braun I, Kunath H

机构信息

VEB Ostra Dresden, Betrieb im VEB Kombinat Milchwirtschaft Dresden, DDR.

出版信息

Nahrung. 1988;32(4):375-81. doi: 10.1002/food.19880320419.

Abstract

The properties of proteolytic enzymes produces from calf maws and from an Ascomycete were studied. Both milk-clotting proteases have their optimum activity at pH 5.2 and 45 degrees C. The microbiological rennin has a second maximum activity at pH 3.5 and 55 degrees C. Temperatures above 55 degrees C cause a rapid decrease of activity. The behaviour of enzyme activity is similar with varying substrate and enzyme concentrations. However, increasing amounts of enzyme in ratio to the substrate lead to reaction rates of the calf rennin differing clearly from that of the microbiological rennet complex.

摘要

对从小牛胃和一种子囊菌中提取的蛋白水解酶的特性进行了研究。两种凝乳蛋白酶在pH 5.2和45摄氏度时具有最佳活性。微生物凝乳酶在pH 3.5和55摄氏度时具有第二个最大活性。温度高于55摄氏度会导致活性迅速下降。在底物和酶浓度变化时,酶活性的表现相似。然而,与底物相比,酶量的增加导致小牛凝乳酶的反应速率与微生物凝乳酶复合物的反应速率明显不同。

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