PURIFICATION AND PROPERTIES OF A LOW-MOLECULAR-WEIGHT ALPHA-MANNOSIDASE FROM CELLULOMONAS SP

被引:3
|
作者
TAKEGAWA, K [1 ]
MIKI, S [1 ]
JIKIBARA, T [1 ]
IWAHARA, S [1 ]
机构
[1] KAGAWA UNIV,FAC AGR,DEPT BIORESOURCE SCI,MIKI,KAGAWA 76107,JAPAN
来源
关键词
D O I
10.1016/0922-338X(90)90201-7
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
Cellulomonas sp. isolated from soil produces a high level of α-mannosidase (α-mannanase) inductively in culture fluid. The enzyme had two different molecular weight forms, and the properties of the high-molecular-weight form were reported previously (Takegawa, K. et al.: Biochim. Biophys. Acta, 991, 431-437, 1989). The low-molecular-weight α-mannosidase was purified to homogeneity by polyacrylamide gel electrophoresis. The molecular weight of the enzyme was over 150,000 by gel filtration. Unlike the high-molecular-weight form, the low-molecular-weight enzyme readily hydrolyzed α-1,2- and α-1,3-linked mannose chains. © 1990.
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页码:129 / 131
页数:3
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