Ionic liquid salt-induced inactivation and unfolding of cellulase from Trichoderma reesei

被引：329

作者：

Turner, MB ^{[1
]}

Spear, SK

Huddleston, JG

Holbrey, JD

Rogers, RD

机构：

[1] Univ Alabama, Ctr Green Mfg, Tuscaloosa, AL 35487 USA

[2] Univ Alabama, Dept Chem, Tuscaloosa, AL 35487 USA

来源：

GREEN CHEMISTRY | 2003年 / 5卷 / 04期

关键词：

D O I：

10.1039/b302570e

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The potential for performing cellulase-catalyzed reactions on cellulose dissolved in 1-butyl-3-methylimidazolium chloride ([bmim] Cl) has been investigated. We have carried out a systematic study on the irreversible solvent and ionic strength-induced inactivation and unfolding of cellulase from Trichoderma reesei ( E.C.#3.2.1.4). Experiments, varying both cellulase and IL solvent concentrations, have indicated that [bmim] Cl, and several other ILs, as well as dimethylacetamide-LiCl (a well-known solvent system for cellulose), inactivate cellulase under these conditions. Despite cellulase inactivity, results obtained from this study led to valuable insights into the requirements necessary for enzyme activity in IL systems. Enzyme stability was determined during urea, NaCl, and [bmim] Cl-induced denaturation observed through fluorescence spectroscopy. Protein stability of a PEG-supported cellulase in [bmim] Cl solution was investigated and increased stability/activity of the PEG-supported cellulase in both the [bmim] Cl and citrate buffer solutions were detected.

引用

页码：443 / 447

页数：5

共 20 条

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