Enhanced catalytic activity of lipase encapsulated in PCL nanofibers

© 2012 American Chemical Society

Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 28(2012), 14 vom: 10. Apr., Seite 6157-62
1. Verfasser: Song, Jie (VerfasserIn)
Weitere Verfasser: Kahveci, Derya, Chen, Menglin, Guo, Zheng, Xie, Erqing, Xu, Xuebing, Besenbacher, Flemming, Dong, Mingdong
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Capsules Enzymes, Immobilized Esters Polyesters Solvents Water 059QF0KO0R polycaprolactone mehr... 24980-41-4 Lipase EC 3.1.1.3 Glycerol PDC6A3C0OX
Beschreibung
Zusammenfassung:© 2012 American Chemical Society
Use of biocatalysis for industrial synthetic chemistry is on the verge of significant growth. Enzyme immobilization as an effective strategy for improving the enzyme activity has emerged from developments especially in nanoscience and nanotechnology. Here, lipase from Burkholderia cepacia (LBC), as an example of the luxuriant enzymes, was successfully encapsulated in polycaprolactone (PCL) nanofibers, proven by X-ray photoelectron spectroscopy (XPS) and atomic force microscopy (AFM). Evaluated in both organic and aqueous medium, the activation factor of the encapsulated enzymes in the hydrolysis reaction was generally higher than that in the transesterification reaction. Enhanced catalytic activities were found when 5-20 w/w % of LBC was loaded. The effect of different solvents pretreatment on the activity of immobilized LBC was also investigated. The highest activation factor was found up to 14 for the sample containing acetone-treated LBC/PCL (10 w/w %). The encapsulated lipase reserved 50% of its original activity after the 10th run in the transesterification reaction in hexane medium. The mechanism of activation of lipase catalytic ability based on active PCL nanofiberous matrix is proposed
Beschreibung:Date Completed 06.08.2012
Date Revised 21.11.2013
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/la300469s