Institute of Biochemistry, National Yang-Ming Medical College, Taipei, Taiwan 11221, Republic of China, and Department of Agricultural Chemistry, The University of Tokyo, Tokyo 113, Japan.
Appl Environ Microbiol. 1988 Dec;54(12):3156-61. doi: 10.1128/aem.54.12.3156-3161.1988.
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-C(15) and anteiso-C(15) 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.
研究了产碱性弹性蛋白酶的专性嗜碱芽孢杆菌 Ya-B 菌株的特性。该菌株仅在 pH7.0 并添加 1%或更多 NaCl 的条件下生长。其脂肪酸分布模式与其他芽孢杆菌相似，其中异-C15 和anteiso-C15 是最丰富的脂肪酸。在含有主要为葡萄糖、豆粕和甘油的培养基（pH10.1）中，从 1 升培养液中回收了约 120mg 的酶。该酶的抗血清不识别枯草菌素等微生物蛋白酶，但与从商业蛋白酶中纯化的蛋白酶 C 反应。化学修饰研究表明，某些组氨酸和酪氨酸残基可能参与了酶的活性。圆二色性研究表明，该酶在 pH 高于 12.0 时会发生部分展开。
