Tuning lipase B from Candida antarctica C–C bond promiscuous activity by immobilization on poly-styrene-divinylbenzene beads
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Título
Tuning lipase B from Candida antarctica C–C bond promiscuous activity by immobilization on poly-styrene-divinylbenzene beadsAutoría
Fecha de publicación
2013-12Editor
Royal Society of ChemistryCita bibliográfica
IZQUIERDO, Diana F., et al. Tuning lipase B from Candida antarctica C–C bond promiscuous activity by immobilization on poly-styrene-divinylbenzene beads. RSC Advances, 2014, 4.12: 6219-6225.Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://pubs.rsc.org/en/Content/ArticleLanding/2014/RA/c3ra47069e#!divAbstractPalabras clave / Materias
Resumen
Lipase B from Candida antarctica (CALB) is able to catalyze C–C bond formation. After immobilization onto a hydrophobic PS-DVB support, the activity increases when compared to that of the soluble or tan – the commer ... [+]
Lipase B from Candida antarctica (CALB) is able to catalyze C–C bond formation. After immobilization onto a hydrophobic PS-DVB support, the activity increases when compared to that of the soluble or tan – the commercially available Novozyme 435 (being up to 6 fold more active). Our results show that although this activity is not related to the catalytic group, the promiscuous activity of CALB may be tuned via immobilization. In addition, we have show that the secondary structure of both immobilized enzymes is quite different, using FT-ATR-IR spectroscopy. [-]
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RSC Adv., 2014,4Derechos de acceso
© The Royal Society of Chemistry 2014
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