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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Shu, Zhengyu Wu, Jiguang Xue, Longyin Lin, Ruifeng Jiang, Yongmei Tang, Lianghua Li, Xin Huang, Jianzhong |
| Description | Author Affiliation: Shu Z ( Engineering Research Center of Industrial Microbiology, Ministry of Education, Fujian Normal University, Fuzhou, Fujian 350108, PR China. shuzhengyu@gmail.com) |
| 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-E H (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. |
| File Format | HTM / HTML |
| ISSN | 01410229 |
| Issue Number | 2 |
| Volume Number | 48 |
| e-ISSN | 18790909 |
| Journal | Enzyme and Microbial Technology |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2011-02-08 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Microbiology Discipline Biochemistry Discipline Biotechnology Aspergillus Niger Enzymology Genetics Lipase Mutagenesis, Site-directed Mutation Amino Acid Sequence Enzyme Activation Enzyme Stability Fungal Proteins Metabolism Molecular Sequence Data Oils Pichia Polymerase Chain Reaction Structure-activity Relationship Substrate Specificity Water Evaluation Studies Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology |
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