期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 71, 期 1-2, 页码 45-50出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2011.03.007
关键词
Burkholderia cepacia lipase; Immobilization; Bioimprinting; Interfacial activation; Circular dichroism; Conformation
资金
- National Natural Science Foundation of China (NSFC) [31070709]
- National High Technology Research and Development Program of China (863 Program) [2009AA03Z232, 2010AA101501]
- Program for New Century Excellent Talents in University [NCET-07-0336]
- Doctor Education Fund for New Teachers [20090142120090]
- Hubei Province Natural Science Fund [2008CDB359, 2009CDA046]
- Key Laboratory for Green Chemical Process of Ministry of Education [GCP201001]
The lipase from Burkholderia cepacia adsorbed on macroporous resin NKA was investigated by combined strategies of bioimprinting and interfacial activation to enhance its catalytic performance. The specific activity of the derivative lipase was 211,733.3 U/g-protein, which was 21.7-fold, 19.4% and 47% enhancement over the free lipase powder, non-bioimprinted and non-interfacial activation lipase, respectively. The derivative lipase exhibited a satisfactory thermal stability over a wide range of temperature (from 30 degrees C to 70 degrees C) and a strong tolerance to organic solvents such as methanol, ethanol and acetone with 50% concentration. After being used of 50 successive batches (400h), the derivative lipase still retained over 92% of its original activity (methyl esters yield decreased from 98% to 90%). Circular dichroism analysis indicated that the activity enhancement of the derivative lipase was ascribed to the secondary structure changes. The derivative lipase preparation in this work was probably a promising alternative to produce a biocatalyst of satisfactory thermo-stability, strong solvents tolerance and high operational reusability. (C) 2011 Elsevier B.V. All rights reserved.
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