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Production and Further Characterization of an Alkaline Elastase Produced by Alkalophilic Bacillus Strain Ya-B

机译:嗜碱芽孢杆菌菌株Ya-B产生的碱性弹性蛋白酶的生产和进一步表征

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The characteristics of the obligate alkalophilic Bacillus sp. strain Ya-B, which produces alkaline elastase extracellularly, were examined. This strain grew at pH 7.0 only in the presence of 1% or more NaCl. Its fatty acid distribution pattern was similar to that of other Bacillus species in which iso-C15 and anteiso-C15 were the most abundant fatty acids. About 120 mg of enzyme was recovered from 1 liter of culture broth in a medium (pH 10.1) containing mainly glucose, soymeal, and glycerol. The antiserum against this enzyme did not recognize microbial proteinases, such as subtilisins, but reacted with proteinase C, which was purified from commercial pronase. Chemical modification studies revealed that certain histidine and tyrosine residues might be involved in the enzyme activity. This enzyme underwent a partial unfolding at pHs higher than 12.0, as indicated by the circular dichroism study.
机译:专性嗜碱芽孢杆菌的特征。检查了在细胞外产生碱性弹性蛋白酶的菌株Ya-B。该菌株仅在1%或更多的NaCl存在下在pH 7.0下生长。它的脂肪酸分布模式与其他芽孢杆菌属相似,其中异C15和前异C15是最丰富的脂肪酸。在主要含有葡萄糖,豆粕和甘油的培养基(pH 10.1)中,从1升培养液中回收到约120 mg酶。针对这种酶的抗血清不能识别微生物蛋白酶,例如枯草杆菌蛋白酶,但会与蛋白酶C反应,蛋白酶C是从商品链酶中纯化的。化学修饰研究表明,某些组氨酸和酪氨酸残基可能与酶的活性有关。如圆二色性研究所示,该酶在高于12.0的pH值下发生了部分解折叠。

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