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

dc.contributor.author	Deepthy, A
dc.contributor.author	Abraham, M
dc.contributor.author	Rajeev K. Sukumaran
dc.date.accessioned	2016-02-10T11:07:22Z
dc.date.available	2016-02-10T11:07:22Z
dc.date.issued	2014-09
dc.identifier.citation	Bioresource Technology 167:547-550,Sep 2014	en_US
dc.identifier.uri	http://ir.niist.res.in:8080/jspui/handle/123456789/2232
dc.description.abstract	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.	en_US
dc.language.iso	en	en_US
dc.publisher	Elsevier	en_US
dc.subject	Pseudozyma, Ethyl acetate, Lipase, Biodiesel, Magnetic nanoparticles	en_US
dc.title	Esterases immobilized on aminosilane modified magnetic nanoparticles as a catalyst for biotransformation reactions	en_US
dc.type	Article	en_US