Repository of Research and Investigative Information

Repository of Research and Investigative Information

دانشگاه علوم پزشکی و خدمات بهداشتی درمانی زنجان

Covalent binding of hyper-activated Rhizomucor miehei lipase (RML) on hetero-functionalized siliceous supports

(2016) Covalent binding of hyper-activated Rhizomucor miehei lipase (RML) on hetero-functionalized siliceous supports. International Journal of Biological Macromolecules. pp. 208-215. ISSN 0141-8130

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Abstract

Physical adsorption onto hydrophobic supports has proven to be an effective way to improve the activity of lipases. Covalent binding, on the other hand, enhances the active lifetime of the immobilized biocatalysts. To combine the benefits of adsorption and covalent binding, immobilization of RML on new hetero-functional supports are reported. For this, chemical modification of silica and silica mesoporous nanoparticles was performed by the simultaneous use of two coupling linkers; Octyltriethoxysilane (OTES) for hydrophobic interaction and glycidoxypropyltrimethoxylsilane (GPTMS) for covalent linkage of RML. Altering the GPTMS/OTES ratio makes possible to have different amount of octyl and epoxy groups on the supports. The results showed that immobilization of RML on octyl-functionalized supports produces specific activity almost 1.5-2 folds greater than the specific activity of the free enzyme. The observed hyper-activation decreased with increasing epoxy groups on the supports confirming the enhancement of covalent nature of the attachment. Leaching experiment was also confirmed positive effect of the presence of epoxy groups on the supports. Regarding the specific activity of the immobilized preparations and desorption percentages of RML from each support, the most suitable carrier obtains from the functionalization of the supports in presence of GPTMS and OTES in the ratio of 1:1. (C) 2016 Elsevier B.V. All rights reserved.

Item Type: Article
Keywords: Covalent immobilization Physical adsorption Rhizomucor miehei lipase SBA-15 Silica gel FISH-OIL HYDROPHOBIC SUPPORTS EPOXY SUPPORTS IMMOBILIZATION HYDROLYSIS ENZYMES SELECTIVITY ADSORPTION Biochemistry & Molecular Biology Chemistry, Applied Polymer Science
Page Range: pp. 208-215
Journal or Publication Title: International Journal of Biological Macromolecules
Abstract and Indexing: ISI, Pubmed
Quartile : Q2
Volume: 86
Identification Number: https://doi.org/10.1016/j.ijbiomac.2016.01.076
ISSN: 0141-8130
Depositing User: خانم مریم زرقانی
URI: http://repository.zums.ac.ir/id/eprint/540

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