文献类型：期刊文献

英文题名：Comparative Study on Lipases Immobilized onto Bentonite and Modified Bentonites and Their Catalytic Properties

作者：Dong, Huaping[1];Li, Yimin[1];Li, Jianfa[1];Shen, Guodong[1];Chen, Hua[1]

机构：[1]Shaoxing Univ, Coll Chem & Chem Engn, Shaoxing 312000, Zhejiang, Peoples R China

年份：2013

卷号：52

期号：26

起止页码：9030

外文期刊名：INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH

收录：SCI-EXPANDED(收录号：WOS:000321541600042)、、EI(收录号：20132816495524)、Scopus(收录号：2-s2.0-84879847272)、WOS

基金：This work was supported by the National Natural Science Foundation of China (20977063), the Natural Science Foundation of Zhejiang Province, China (LY12B06003), and the Science and Technology Program of Shaoxing (2011A21056).

语种：英文

外文关键词：Adsorption - Adsorption isotherms - Catalyst activity - Cationic surfactants - Hydrophilicity - Hydrophobicity - Molecules - Reusability

外文摘要：The hydrophobic property and structure of Na-bentonite (Na-bent) were tuned by intercalation with cationic surfactants for lipase adsorption. The adsorption isotherms of lipase on Na-bent and modified bentonites demonstrated Langmuir-type shape, and Na-bent showed higher adsorption efficiency than modified bentonites. The observed overlap of lipase molecules on the support and the interactions between these molecules under high protein loading caused the reduction in the activity of immobilized lipase. The immobilized lipases on modified bentonites (Bent-DTAB-lipase, Bent-CTAB-lipase, and Bent-OTAB-lipase) exhibited higher catalytic activity than that on Na-bent, due to the hydrophobically interfacial activation of modified bentonites toward lipase. The highest catalytic activity and stability were observed on Bent-CTAB-lipase, resulting from the tunable hydrophilic/hydrophobic balance of the support's surface, while the excessive hydrophobic property showed negative influence on lipase's catalytic performance. The immobilized lipases onto modified bentonites with hydrophobic property showed higher thermal stability and reusability than Na-bent-lipase.