Institute of Paper Science and Technology, School of Chemical & Biomolecular Engineering, Georgia Institute of Technology, 500 10th Street, NW, Atlanta, GA 30332-0620, United States.
J Biotechnol. 2011 Jul 20;154(4):269-73. doi: 10.1016/j.jbiotec.2011.05.016. Epub 2011 Jun 12.
Cationic polyacrylamides (c-PAMs) increase the binding of cellulase to cellulose and of α-amylase to cornstarch. The c-PAMs increase the rate of hydrolysis of both substrates by about the same amount, which suggests that the increased binding is responsible for the enhanced rates. These results support our proposed mechanism where the c-PAM neutralizes the charge of the substrate through a "patching" mechanism, which reduces the charge repulsion between fiber and enzyme.
阳离子聚丙烯酰胺(c-PAMs)增加了纤维素酶与纤维素和α-淀粉酶与玉米淀粉的结合。c-PAMs 使这两种底物的水解速率增加大致相同的幅度,这表明增加的结合是导致增强的速率的原因。这些结果支持了我们提出的机制,其中 c-PAM 通过“修补”机制中和底物的电荷,从而减少纤维和酶之间的电荷排斥。