Fabrication of heterogeneous biocatalyst tethering artificial prosthetic groups to obtain omega-3-fatty acids by selective hydrolysis of fish oils

S. Moreno-Pérez; G. Fernández-Lorente; O. Romero; J. M. Guisán; F. López-Gallego

doi:10.1039/c6ra21121f

Fabrication of heterogeneous biocatalyst tethering artificial prosthetic groups to obtain omega-3-fatty acids by selective hydrolysis of fish oils

S. Moreno-Pérez, G. Fernández-Lorente, O. Romero, J. M. Guisán, F. López-Gallego

SCHOOL OF BIOCHEMICAL ENGINEERING

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Abstract

The active site of lipase from Bacillus thermocathenolatus was selectively modified with allyl and naphthyl chains at different positions. Lipase immobilization and selective tethering of a naphthyl side chain to its position 320 improve both the hydrolysis rate of fish oils and the selectivity towards the eicosapentaenoic acid acyl chains.

Original language	English
Pages (from-to)	97659-97663
Number of pages	5
Journal	RSC Advances
Volume	6
Issue number	100
DOIs	https://doi.org/10.1039/c6ra21121f
State	Published - 2016

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abstract = "The active site of lipase from Bacillus thermocathenolatus was selectively modified with allyl and naphthyl chains at different positions. Lipase immobilization and selective tethering of a naphthyl side chain to its position 320 improve both the hydrolysis rate of fish oils and the selectivity towards the eicosapentaenoic acid acyl chains.",

author = "S. Moreno-P{\'e}rez and G. Fern{\'a}ndez-Lorente and O. Romero and Guis{\'a}n, {J. M.} and F. L{\'o}pez-Gallego",

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T1 - Fabrication of heterogeneous biocatalyst tethering artificial prosthetic groups to obtain omega-3-fatty acids by selective hydrolysis of fish oils

AU - Moreno-Pérez, S.

AU - Fernández-Lorente, G.

AU - Romero, O.

AU - Guisán, J. M.

AU - López-Gallego, F.

N1 - Publisher Copyright: © The Royal Society of Chemistry 2016.

PY - 2016

Y1 - 2016

N2 - The active site of lipase from Bacillus thermocathenolatus was selectively modified with allyl and naphthyl chains at different positions. Lipase immobilization and selective tethering of a naphthyl side chain to its position 320 improve both the hydrolysis rate of fish oils and the selectivity towards the eicosapentaenoic acid acyl chains.

AB - The active site of lipase from Bacillus thermocathenolatus was selectively modified with allyl and naphthyl chains at different positions. Lipase immobilization and selective tethering of a naphthyl side chain to its position 320 improve both the hydrolysis rate of fish oils and the selectivity towards the eicosapentaenoic acid acyl chains.

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U2 - 10.1039/c6ra21121f

DO - 10.1039/c6ra21121f

M3 - Article

AN - SCOPUS:84992179813

SN - 2046-2069

VL - 6

SP - 97659

EP - 97663

JO - RSC Advances

JF - RSC Advances

IS - 100

ER -

Fabrication of heterogeneous biocatalyst tethering artificial prosthetic groups to obtain omega-3-fatty acids by selective hydrolysis of fish oils

Abstract

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