Esterases immobilized on aminosilane modified magnetic nanoparticles as a catalyst for biotransformation reactions

被引：31

作者：

Alex, Deepthy ^{[1
,2
]}

Mathew, Abraham ^{[1
,3
]}

Sukumaran, Rajeev K. ^{[1
]}

机构：

[1] CSIR, Natl Inst Interdisciplinary Sci & Technol, Ctr Biofuels, Div Biotechnol, Thiruvananthapuram 695019, Kerala, India

[2] Mar Ivanios Coll, Dept Biotechnol, Thiruvananthapuram 695015, Kerala, India

[3] St Peters Coll, Dept Bot, Ernakulam, Kerala, India

来源：

BIORESOURCE TECHNOLOGY | 2014年 / 167卷

关键词：

Pseudozyma; Ethyl acetate; Lipase; Biodiesel; Magnetic nanoparticles; LIPASE; BIODIESEL; OIL;

D O I：

10.1016/j.biortech.2014.05.110

中图分类号：

S2 [农业工程];

学科分类号：

0828 ;

摘要：

Magnetite nanoparticles were prepared by reacting ferrous and ferric salts in presence of aqueous ammonia. The magnetic nanoparticles (MNPs) were amino functionalized by treating with 3-aminopropyl triethoxy silane (APTES) and was coupled with glutaraldehyde. A novel solvent tolerant esterase from Pseudozyma sp. NII 08165 was immobilized on the MNPs through covalent bonding to the glutaraldehyde. The magnetite nanoparticles had a size range of 10-100 nm, confirmed by DLS. Lipases immobilized on MNPs were evaluated for biotransformation reactions including synthesis of ethyl acetate and transesterification of vegetable oil for producing biodiesel. The MNP immobilized esterase had prolonged shelf life and there was no loss in enzyme activity. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：547 / 550

页数：4

共 20 条

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