Macromolecular cross-linked enzyme aggregates (M-CLEAs) of α-amylase

被引:130
作者
Nadar, Shamraja S. [1 ]
Muley, Abhijeet B. [2 ]
Ladole, Mayur R. [2 ]
Joshi, Pranoti U. [3 ]
机构
[1] Inst Chem Technol, Dept Chem Engn, Bombay 400019, Maharashtra, India
[2] North Maharashtra Univ, Univ Inst Chem Technol, Dept Food Technol, Jalgaon 425001, India
[3] Kolhapur Inst Technol, Dept Biotechnol Engn, Coll Engn, Kolhapur 416234, Maharashtra, India
关键词
alpha-Amylase CLEAs; Cross-linkers; Glutaraldehyde; Macromolecular substrate; Immobilization; IMMOBILIZATION; GLUTARALDEHYDE; PERFORMANCE; STABILITY; PECTIN;
D O I
10.1016/j.ijbiomac.2015.11.082
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
Macromolecular cross-linked enzyme aggregates (M-CLEAs) of alpha-amylase were prepared by precipitation and subsequent cross-linking. The non-toxic, biodegradable, biocompatible, renewable polysaccharide based macromolecular cross-linkers viz. agar, chitosan, dextran, and gum arabic were used as a substitute for traditional glutaraldehyde to augment activity recovery toward macromolecular substrate. Macro molecular cross-linkers were prepared by periodate mediated controlled oxidation of polysaccharides. The effects of precipitating agent, concentration and different cross-linkers on activity recovery of a amylase CLEAs were investigated. or-Amylase aggregated with ammonium sulphate and cross-linked by dextran showed 91% activity recovery, whereas glutaraldehyde CLEAs (G-CLEAs) exhibited 42% activity recovery. M-CLEAs exhibited higher thermal stability in correlation with alpha-amylase and G-CLEAs. Moreover, dextran and chitosan M-CLEAs showed same affinity for starch hydrolysis as of free alpha-amylase. The changes in secondary structures revealed the enhancements in structural and conformational rigidity attributed by cross-linkers. Finally, after five consecutive cycles dextran M-CLEAs retained 1.25 times higher initial activity than G-CLEAs. (C) 2015 Elsevier B.V. All rights reserved.
引用
收藏
页码:69 / 78
页数:10
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