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Construction of Aspergillus niger lipase mutants with oil–water interface independence

Paper ID Volume ID Publish Year Pages File Format Full-Text
17469 42671 2011 5 PDF Available
Title
Construction of Aspergillus niger lipase mutants with oil–water interface independence
Abstract

Based on previous bioinformational analytical results [Shu ZY, et al. Biotechnol Prog 2009;25:409–16], four A. niger lipase (ANL) mutants, ANL-Ser84Gly, ANL-Asp99Pro, ANL-Lys108Glu and ANL-EαH (obtained by replacing the lid domain of ANL with the corresponding domain from A. niger feruloyl esterase), were constructed to screen out ANL mutants with oil–water interface independence. ANL-S84G displayed a pronounced interfacial activation, while ANL-D99P and ANL-K108E displayed no interfacial activation. The specific activity of ANL-S84G towards p-nitrophenyl esters decreased from 29.8% to 76.5% compared with that of ANL, while the specific activity of ANL-D99P towards p-nitrophenyl palmitate increased 2.2-fold. The thermostability of ANL-K108E was almost unchanged, while the thermostability of ANL-S84G and ANL-D99P significantly decreased compared with that of ANL. The construction of oil–water interface-independent ANL mutants would help to further understand the mechanism of lipase interfacial activation.

Keywords
ANL, Wild type Aspergillus niger lipase; ANL-Ser84Gly (ANL-S84G), A. niger lipase mutant where Ser84 was replaced with Gly; ANL-Asp99Pro (ANL-D99P), A. niger lipase mutant where Asp99 was replaced with Pro; ANL-Lys108Glu (ANL-K108E), A. niger lipase mutan
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Construction of Aspergillus niger lipase mutants with oil–water interface independence
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 48, Issue 2, 8 February 2011, Pages 129–133
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
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Price after discount Only $4.95
100% Money Back Guarantee
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