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《Acta Microbiologica Sinica》 1984-01
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A STUDY ON THE PURIFICATION AND SOME PROPERTIES OF ALKALINE PROTEINASE FROM BACILLUS PUMILUS STRAIN 209

Qiu Xiubao;Cheng Xiulan Institute of Microbiology, Academia Sinica, Beijing  
An alkaline proteinase produced by Ba-cillus pumilus was partially purified througha process involving ammonium sulfate pre-ciptation, Sephadex G-25 filtration, chroma-tography on DEAE-cellulose and lyophyliza-tion, and a final product, a white powderwas obtained. The specific activity of en-zyme preparation after purification increased2.6 times. The optimum pH and tempera-ture for casein hydrolysis were 9.0 and 50℃,respectively. The enzyme was stable overthe pH range from 6 to 10. Ca~(2+) enhancedthe heat stability of the enzyme. The enzyme was completely inactivitedafter treatment with DFP (2.5 mM ) or NBS(1×10~(-3)M), but not with PCMB and O-PTH. Theccation such as Cu~(2+), Fe~(2+) andHg~+ (1×10~3-M ) inhibited the enzyme ac-tivity, while Mn~(2+) trends to stimulate acti-vity. Casein, haemoglobin, snake venom pro-tein and fibrin were susceptible to enzymatichydrolysis.
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