The enzymatic hydrolysis rate of cellulose decreases with irreversible adsorption of cellobiohydrolase I
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- 作者：Anzhou Ma ; Qing Hu ; Yinbo Qu ; Zhihui Bai ; Weifeng Liu ; Guoqiang Zhuang
- 关键词：Cellobiohydrolase I ; Hydrolysis ; Irreversible adsorption ; Solid– ; liquid interface ; Rate retardation
- 刊名：Enzyme and Microbial Technology
- 出版年：2008
- 出版时间：5 June 2008
- 年：2008
- 卷：42
- 期：7
- 页码：543-547
- 全文大小：478 K
文摘
Protein adsorption onto solid substrates usually takes place in an irreversible fashion and this irreversible adsorption also occurs in some enzymatic reactions. In this work the adsorption behavior of intact β-1, 4-glucan-cellobiohydrolase (CBH I) from Trichoderma reesei onto microcrystalline cellulose was monitored by surface plasmon resonance and UV-spectral method. It was found that there existed reversible binding and irreversible binding of CBH I during its interaction with cellulose substrate. To evaluate the influence of adsorption on cellulose enzymatic hydrolysis, the reaction dynamics on pure cellulose were determined. A plot of the hydrolysis rate against the surface density of irreversibly adsorbed CBH I, revealed an inverse relationship in which an apparent decrease in the hydrolysis rate was observed with increasing surface density. Taken together, results presented here should be useful for modifying the binding characteristics of CBH I and making them more effective in cellulose hydrolysis.