2024-03-29T05:09:08Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1872752019-09-27T10:53:32Zcom_10261_101com_10261_5col_10261_354
00925njm 22002777a 4500
dc
Izquierdo, Diana Flor
author
Barbosa, Oveimar
author
Burguete, M. Isabel
author
Lozano, Pedro
author
Luis, Santiago V.
author
Fernández-Lafuente, Roberto
author
García-Verdugo, Eduardo
author
2014
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.
RSC Advances 4: 6219-6225 (2014)
http://hdl.handle.net/10261/187275
10.1039/c3ra47069e
2046-2069
http://dx.doi.org/10.13039/501100003329
Tuning lipase B from Candida antarctica C-C bond promiscuous activity by immobilization on poly-styrene-divinylbenzene beads