RELEASE OF THE FAD DOMAIN FROM CELLOBIOSE OXIDASE BY PROTEASES FROM CELLULOLYTIC CULTURES OF PHANEROCHAETE-CHRYSOSPORIUM

被引:48
作者
HABU, N
SAMEJIMA, M
DEAN, JFD
ERIKSSON, KEL
机构
[1] UNIV GEORGIA,CTR BIOL RESOURCE RECOVERY,DEPT BIOCHEM,ATHENS,GA 30602
[2] UNIV TOKYO,DEPT FOREST PROD,BUNKYO KU,TOKYO 113,JAPAN
关键词
CELLOBIOSE DEHYDROGENASE; CELLOBIOSE QUINONE OXIDOREDUCTASE; PROTEOLYSIS; CELLULOSE DEGRADATION; ANTIBODY;
D O I
10.1016/0014-5793(93)80162-N
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Evidence has previously suggested that cellobiose:quinone oxidoreductase (CBQ) in cellulolytic cultures of Phanerochaete chrysosporium might be produced from cellobiose oxidase (CBO) by proteolytic cleavage. This study demonstrates that the ratio of CBO activity to (CBO + CBQ) activity declines with decreasing culture pH, while protease activity increases. Furthermore, we demonstrate that endogenous P. chrysosporium proteases can only cleave CBO when the enzyme is bound to cellulose. This is the first demonstration that the proteases produced in cellulolytic cultures of P. chrysosporium can release the FAD domain from CBO.
引用
收藏
页码:161 / 164
页数:4
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