Enzymatic hydrolysis of microcrystalline cellulose in reverse micelles

被引:37
|
作者
Chen, Nan [1 ]
Fan, Jun-Bao [1 ]
Xiang, Jin [1 ]
Chen, Jie [1 ]
Liang, Yi [1 ]
机构
[1] Wuhan Univ, Coll Life Sci, State Key Lab Virol, Wuhan 430072, Peoples R China
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2006年 / 1764卷 / 06期
基金
中国国家自然科学基金;
关键词
cellulase; microcrystalline cellulose; reverse micelle; enzymatic hydrolysis;
D O I
10.1016/j.bbapap.2006.03.015
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
The activities of cellulases from Trichoderma reesei entrapped in three types of reverse micelles have been investigated using microcrystalline cellulose as the substrate. The reverse micellar systems are formed by nonionic surfactant Triton X-100, anionic surfactant Aerosol OT (AOT), and cationic surfactant cetyltrimethyl ammonium bromide (CTAB) in organic solvent mediae, respectively. The influences of the molar ratio of water to surfactant too, one of characteristic parameters of reverse micelles, and other environmental conditions including pH and temperature, on the enzymatic activity have been studied in these reverse micellar systems. The results obtained indicate that these three reverse micelles are more effective than aqueous systems for microcrystalline cellulose hydrolysis, and cellulases show "superactivity" in these reverse micelles compared with that in aqueous systems under the same pH and temperature conditions. The enzymatic activity decreases with the increase of too in both AOT and Triton X-100 reverse micellar systems, but reaches a maximum at omega(0) of 16.7 for CTAB reverse micelles. Temperature and pH also influence the cellulose hydrolysis process. The structural changes of cellulases in AOT reverse micelles have been measured by intrinsic fluorescence method and a possible explanation for the activity changes of cellulases has been proposed. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:1029 / 1035
页数:7
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