Effect of protein load on stability of immobilized enzymes

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• 作者：Laura Fernandez-Lopez^a ; ¹ ; Sara G. Pedrero^a ; ¹ ; Nerea Lopez-Carrobles^a ; Beatriz C. Gorines^a ; Jose J. Virgen-Ortí ; z^a ; ^b ; ^{juanvirgen@hotmail.com} ; Roberto Fernandez-Lafuente^a ; ^{rfl@icp.csic.es} ; ^{rfernandezlafuente@hotmail.com}
• 关键词：Control of immobilization rate ; Enzyme stability ; Immobilized enzyme interactions ; Enzyme crowding ; Octyl agarose
• 刊名：Enzyme and Microbial Technology
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：98
• 期：Complete
• 页码：18-25
• 全文大小：1347 K
• 卷排序：98

文摘

Several lipases were rapidly immobilized on octyl-agarose. Usually, diffusion limitations make that stability apparently increases with support loading. CALB-OC stability decrease only in thermal inactivations. This loading negative effect on stability was reversed by slowing down the immobilization rate.