Main structural targets for engineering lipase substrate specificity

Samah, H. A. and Masomian, Malihe * and Siti Nor Hasmah I, and Mohd Shukri MA, and Leow, Adam Thean and Fairolniza, M. S. and Noor Dina, M. N. and Raja Noor Zaliha, R. A. R. (2020) Main structural targets for engineering lipase substrate specificity. Catalysts, 10 (7). p. 747. ISSN 2073-4344

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Microbial lipases represent one of the most important groups of biotechnological biocatalysts. However, the high-level production of lipases requires an understanding of the molecular mechanisms of gene expression, folding, and secretion processes. Stable, selective, and productive lipase is essential for modern chemical industries, as most lipases cannot work in different process conditions. However, the screening and isolation of a new lipase with desired and specific properties would be time consuming, and costly, so researchers typically modify an available lipase with a certain potential for minimizing cost. Improving enzyme properties is associated with altering the enzymatic structure by changing one or several amino acids in the protein sequence. This review detailed the main sources, classification, structural properties, and mutagenic approaches, such as rational design (site direct mutagenesis, iterative saturation mutagenesis) and direct evolution (error prone PCR, DNA shuffling), for achieving modification goals. Here, both techniques were reviewed, with different results for lipase engineering, with a particular focus on improving or changing lipase specificity. Changing the amino acid sequences of the binding pocket or lid region of the lipase led to remarkable enzyme substrate specificity and enantioselectivity improvement. Site-directed mutagenesis is one of the appropriate methods to alter the enzyme sequence, as compared to random mutagenesis, such as error-prone PCR. This contribution has summarized and evaluated several experimental studies on modifying the substrate specificity of lipases

Item Type: Article
Uncontrolled Keywords: lipase; specificity; binding pocket; lid; oxyanion hole; protein engineering; chemoselectivity; regioselectivity; stereoselectivity
Subjects: Q Science > QR Microbiology > QR355 Virology
Divisions: Others > Non Sunway Academics
Sunway University > School of Engineering and Technology [formerly School of Science and Technology until 2020] > Centre for Virus and Vaccine Research moved to SMLS wef 2021
Depositing User: Dr Janaki Sinnasamy
Related URLs:
Date Deposited: 21 Sep 2020 06:07
Last Modified: 21 Sep 2020 06:07

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