CLEAVAGE OF BACILLUS-SUBTILIS ENDO-BETA-1,4-GLUCANASE BY B-MEGATERIUM PROTEASE

被引:9
作者
AHN, DH
KIM, H
PACK, MY
机构
[1] SUNCHON NATL UNIV,DEPT AGR CHEM,SUNCHON 540742,SOUTH KOREA
[2] KAIST,DEPT BIOTECHNOL,TAEJON 305338,SOUTH KOREA
关键词
D O I
10.1007/BF00133011
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A protease secreted by B. megaterium ATCC 14945 was purified by ammonium sulfate fractionation, Q-Sepharose, Sephadex G-75, and hydroxyapatite chromatography and its molecular weight was estimated to be 38 kD. The purified protease caused the cleavage of 52 kD B. subtilis endo-beta-1,4-glucanase expressed in B. megaterium. The enzyme was most active at pH 7.5 and 55-degrees-C. Calcium ion was required for the enzyme activity and the activity was almost completely inhibited by EDTA. The protease was not inhibited by phenylmethylsulfonyl fluoride.
引用
收藏
页码:127 / 132
页数:6
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