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Biocatalysts and Bioreactor Design
Immobilization and stability of a Rhizopus oryzae lipase expressed in Pichia pastoris: Comparison between native and recombinant variants
Article first published online: 16 JUN 2011
DOI: 10.1002/btpr.654
Copyright © 2011 American Institute of Chemical Engineers (AIChE)
Additional Information
How to Cite
Guillén, M., Benaiges, M. D. and Valero, F. (2011), Immobilization and stability of a Rhizopus oryzae lipase expressed in Pichia pastoris: Comparison between native and recombinant variants. Biotechnol Progress, 27: 1232–1241. doi: 10.1002/btpr.654
Publication History
- Issue published online: 10 OCT 2011
- Article first published online: 16 JUN 2011
- Accepted manuscript online: 24 MAY 2011 10:28AM EST
- Manuscript Revised: 26 APR 2011
- Manuscript Received: 19 OCT 2010
Funded by
- Spanish Ministry of Science and Innovation 2009-SGR-281. Grant Number: CTQ2007-60347
- Reference Network in Biotechnology (XRB) (Generalitat de Catalunya)
- Grant FPU of the Spanish Ministry of Education and Science
- Abstract
- Article
- References
- Cited By
Keywords:
- recombinant;
- Rhizopus oryzae;
- lipase;
- immobilization;
- EP100;
- Eupergit®C;
- Pichia pastoris
Abstract
The stability of a soluble extract containing a recombinant lipase from Rhizopus oryzae (Cursive) lipase (rROL) produced by Pichia pastoris (Cursive), as well as that for the commercial extract containing the lipase produced by the native organism (nROL), was investigated. The results showed higher residual activity values of the commercial protein compared with the recombinant one. Moreover, two different kinds of support, the polypropylene powder EP100 and Eupergit®C, were tested to immobilize the enzymes. The residual activity of the immobilizated derivatives was also tested to determine whether their stability was enhanced. The results showed a slight improvement in rROL using both supports but a decrease in nROL using Eupergit®C. The study of the residual activity of soluble and immobilized enzymes was performed by means of a central composite rotatable experiment design. In addition, EP100 adsorption isotherms were determined. © 2011 American Institute of Chemical Engineers Biotechnol. Prog., 2011