Journal
MICROBIOLOGICAL RESEARCH
Volume 178, Issue -, Pages 27-34Publisher
ELSEVIER GMBH
DOI: 10.1016/j.micres.2015.05.011
Keywords
Yarrowia lipolytica lipase 2; Aspergillus niger feruloyl esterase A; Site-directed mutagenesis; Interfacial activation; Divergent evolution
Categories
Funding
- National Natural Science Foundation of China [31070089, 31170078, J1103514]
- National High Technology Research and Development Program of China [2011AA02A204, 2014AA093510]
- Innovation Foundation of Shenzhen Government [JCYJ20120831111657864]
- Fundamental Research Funds for HUST [2014NY007, 2014QN119, 2012SHYJ004]
Ask authors/readers for more resources
Yarrowia lipolytica lipase 2 (YLLip2) and Aspergillus niger feruloyl esterase A (AnFaeA) are enzymes of similar structures but with different functions. They are both classified into the same homologous family in Lipase Engineering Database (LED). The major difference between the two enzymes is that YLLip2 exhibits interfacial activity while AnFaeA does not. In order to better understand the interfacial activation mechanisms of YLLip2, structure guided site-directed mutagenesis were performed, mutants were constructed, kinetics parameters and lipase properties were detected. Mutant enzymes showed enhanced catalytic efficiency towards p-nitrophenyl butyrin (pNPB) but their catalytic efficiency decreased towards p-nitrophenyl palmitate (pNPP), their catalysis behavior was more close to feruloyl esterase. Moreover, the mutant enzymes exhibited enhanced thermostability compared with their wild type. These results indicate that I100 and F129 are probably cut-off point of divergent functions between the two enzymes during evolution. (C) 2015 Elsevier GmbH. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available