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多粘芽孢杆菌天然的、锌制备的和锰制备的金属蛋白酶的物理化学性质

Physiochemical properties of the native, zinc- and manganese-prepared metalloprotease of Bacillus polymyxa.

作者信息

Griffin P J, Fogarty W M

出版信息

Appl Microbiol. 1973 Aug;26(2):191-5. doi: 10.1128/am.26.2.191-195.1973.

Abstract

The neutral protease of Bacillus polymyxa had a broad pH optimum (6.0 to 7.2) for activity at 37 C. The enzyme was most stable at pH 5.6 to 5.8. The protease had an optimum temperature of 37 C and was quite thermostable up to 35 C, but at higher temperatures the stability decreased rapidly. The substrate specificity of the protease was similar to that of the neutral proteases of other members of the genus Bacillus. The enzyme was shown to be a zinc metalloprotease. However, manganous ions had a greater activating and stabilizing influence on the activity of this enzyme than zinc. Replacement of zinc in the native enzyme by manganese resulted in a 50% increase in activity. In addition, the prepared manganese metalloprotease had higher temperature and more alkaline pH optima than the native enzyme.

摘要

多粘芽孢杆菌的中性蛋白酶在37℃时活性的最适pH范围较宽(6.0至7.2)。该酶在pH 5.6至5.8时最稳定。该蛋白酶的最适温度为37℃,在高达35℃时相当耐热,但在较高温度下稳定性迅速下降。该蛋白酶的底物特异性与芽孢杆菌属其他成员的中性蛋白酶相似。该酶被证明是一种锌金属蛋白酶。然而,锰离子对该酶活性的激活和稳定作用比锌更大。用锰替代天然酶中的锌导致活性增加50%。此外,制备的锰金属蛋白酶比天然酶具有更高的温度和更碱性的最适pH。

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