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Review

Main Structural Targets for Engineering Lipase Substrate Specificity

by
Samah Hashim Albayati
1,2,
Malihe Masomian
3,
Siti Nor Hasmah Ishak
1,2,
Mohd Shukuri bin Mohamad Ali
1,4,5,
Adam Leow Thean
1,5,6,
Fairolniza binti Mohd Shariff
1,2,
Noor Dina binti Muhd Noor
1,4 and
Raja Noor Zaliha Raja Abd Rahman
1,2,5,*
1
Enzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Bimolecular Science, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia
2
Department of Microbiology, Faculty of Biotechnology and Bimolecular Science, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia
3
Center for Virus and Vaccine Research, School of Science and Technology, Sunway University, Kuala Lumpur 47500, Selangor, Malaysia
4
Department of Biochemistry, Faculty of Biotechnology and Bimolecular Science, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia
5
Institute Bioscience, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia
6
Department of Cell and Molecular Biology, Faculty of Biotechnology and Bimolecular Science, Universiti Putra Malaysia, Serdang 43400, Selangor, Malaysia
*
Author to whom correspondence should be addressed.
Catalysts 2020, 10(7), 747; https://doi.org/10.3390/catal10070747
Submission received: 9 April 2020 / Revised: 3 May 2020 / Accepted: 5 May 2020 / Published: 6 July 2020
(This article belongs to the Special Issue Lipases and Phospholipases in Biocatalysis)
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Abstract

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.
Keywords: lipase; specificity; binding pocket; lid; oxyanion hole; protein engineering; chemoselectivity; regioselectivity; stereoselectivity lipase; specificity; binding pocket; lid; oxyanion hole; protein engineering; chemoselectivity; regioselectivity; stereoselectivity

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MDPI and ACS Style

Albayati, S.H.; Masomian, M.; Ishak, S.N.H.; Mohamad Ali, M.S.b.; Thean, A.L.; Mohd Shariff, F.b.; Muhd Noor, N.D.b.; Raja Abd Rahman, R.N.Z. Main Structural Targets for Engineering Lipase Substrate Specificity. Catalysts 2020, 10, 747. https://doi.org/10.3390/catal10070747

AMA Style

Albayati SH, Masomian M, Ishak SNH, Mohamad Ali MSb, Thean AL, Mohd Shariff Fb, Muhd Noor NDb, Raja Abd Rahman RNZ. Main Structural Targets for Engineering Lipase Substrate Specificity. Catalysts. 2020; 10(7):747. https://doi.org/10.3390/catal10070747

Chicago/Turabian Style

Albayati, Samah Hashim, Malihe Masomian, Siti Nor Hasmah Ishak, Mohd Shukuri bin Mohamad Ali, Adam Leow Thean, Fairolniza binti Mohd Shariff, Noor Dina binti Muhd Noor, and Raja Noor Zaliha Raja Abd Rahman. 2020. "Main Structural Targets for Engineering Lipase Substrate Specificity" Catalysts 10, no. 7: 747. https://doi.org/10.3390/catal10070747

APA Style

Albayati, S. H., Masomian, M., Ishak, S. N. H., Mohamad Ali, M. S. b., Thean, A. L., Mohd Shariff, F. b., Muhd Noor, N. D. b., & Raja Abd Rahman, R. N. Z. (2020). Main Structural Targets for Engineering Lipase Substrate Specificity. Catalysts, 10(7), 747. https://doi.org/10.3390/catal10070747

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