Abstract
Phospholipase B from Streptomyces hiroshimensis was purified 220-fold in specific activity by means of acetone treatment, gel filtration on Sephadex G–75 and isoelectric focusing, and the recovery of the activity was 60%. The isoelectric point was found to be around pH 7.3 and the molecular weight was about 15,000. The phospholipase B had an optimum pH of 9.0. The enzyme retained 80 % of the activity when heated for 60 min at 37°C. The activity was stimulated by Ca2+, Ba2+ and Triton X–100 and inhibited by Zn2+, Co2+, Fe3+, Al3+, Adekatol SO–120, sodium cholate, sodium deoxycholate, lauryl benzene sulfonate, Cation DT–205 and cetylpyridinium chloride. The enzyme attacked phosphatidylcholine more rapidly than phosphatidylethanolamine. Under the same condition, the enzyme also hydroly-zed the lysophospholipids, lysophosphatidylcholine and lysophosphatidylethanolamine.
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