Habu N, Samejima M, Dean J F, Eriksson K E
Department of Biochemistry, University of Georgia, Athens 30602-7229.
FEBS Lett. 1993 Jul 26;327(2):161-4. doi: 10.1016/0014-5793(93)80162-n.
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.
先前有证据表明，在黄孢原毛平革菌的纤维素分解培养物中，纤维二糖：醌氧化还原酶（CBQ）可能是由纤维二糖氧化酶（CBO）经蛋白水解裂解产生的。本研究表明，随着培养物pH值的降低，CBO活性与（CBO + CBQ）活性的比值下降，而蛋白酶活性增加。此外，我们证明，当该酶与纤维素结合时，黄孢原毛平革菌内源性蛋白酶才能裂解CBO。这首次证明了在黄孢原毛平革菌的纤维素分解培养物中产生的蛋白酶可从CBO释放FAD结构域。
