Formation lipase cross-linked enzyme aggregates on octyl-modified mesocellular foams with oxidized sodium alginate.

Autor: Jin W; The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, PR China., Xu Y; The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, PR China., Yu XW; The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, PR China. Electronic address: yuxw@jiangnan.edu.cn.
Jazyk: angličtina
Zdroj: Colloids and surfaces. B, Biointerfaces [Colloids Surf B Biointerfaces] 2019 Dec 01; Vol. 184, pp. 110501. Date of Electronic Publication: 2019 Sep 11.
DOI: 10.1016/j.colsurfb.2019.110501
Abstrakt: Supported cross-linked enzyme aggregates were prepared by immobilization of Candida antarctica lipase B onto hydrophobic surface of octyl-modified mesocellular foams (MCFs-C8). Oxidized sodium alginate was used as a substitute for traditional glutaraldehyde. Supported cross-linked enzyme aggregates using oxidized sodium alginate (SA-CLEAs@MCFs-C8) exhibited significantly improved thermal stability and organic solvents tolerance compared to the free lipase, lipase adsorbed onto MCFs-C8 and supported cross-linked enzyme aggregates using glutaraldehyde (G-CLEAs@MCFs-C8). Then immobilized lipases were employed for biodiesel production by transesterification of soybean oil with methanol. In the optimization condition, SA-CLEAs@MCFs-C8 were quite stable and still showed high fatty acid methyl esters (FAME) yield after 5 repeated cycles (from 89% to 78%), whereas MCFs-C8-CALB retained 67% FAME yield (about 72% for G-CLEAs@MCFs-C8).
(Copyright © 2019. Published by Elsevier B.V.)
Databáze: MEDLINE
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