Tuning lipase B from Candida antarctica C–C bond promiscuous activity by immobilization on poly-styrene-divinylbenzene beads
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Tuning lipase B from Candida antarctica C–C bond promiscuous activity by immobilization on poly-styrene-divinylbenzene beadsAutoria
Data de publicació
2013-12Editor
Royal Society of ChemistryCita bibliogràfica
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.Tipus de document
info:eu-repo/semantics/articleVersió de l'editorial
http://pubs.rsc.org/en/Content/ArticleLanding/2014/RA/c3ra47069e#!divAbstractParaules clau / Matèries
Resum
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. [-]
Publicat a
RSC Adv., 2014,4Drets d'accés
© The Royal Society of Chemistry 2014
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