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Production and further characterization of an alkaline elastase produced by alkalophilic bacillus strain ya-B. 1988

Y C Tsai, and R Y Juang, and S F Lin, and S W Chen, and M Yamasaki, and G Tamura
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.

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.

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