Structural and functional insights into thermostable and organic solvent stable variant Pro247-Ser of Bacillus lipase

International Journal of Biological Macromolecules
Nisha ChopraJagdeep Kaur

Abstract

Thermostability of enzymes is an important issue in protein engineering and has been studied in detail. Still there is no hard and fast rule to define the conditions which will provide thermal stability. Understanding the various factors and mechanism responsible for thermal stability will add on new insights into our present knowledge in this area. Pro247-Ser variant was constructed based on homology modelling and rational design. It exhibited 60 fold increase in thermal stability at 60°C and+0.7M shift in C1/2 value for urea denaturation as compared to WT. Variant displayed noticeable tolerance to organic solvents. With decrease in Km, catalytic efficiency of Pro247-Ser variant was increased by 12 fold. The activity and stability assay including circular dichroism and fluorescence spectroscopy favoured increased thermal performance of variant. Hydrolytic activity of variant was found to be high in comparison to control for all p-nitrophenol esters investigated. The immobilized variant enzyme demonstrated nearly two fold enhanced conversion of methyl oleate than WT enzyme. The additional molecular interactions of variant residue might contribute to increased thermostability of lipase. The homology modeling predicted formation ...Continue Reading

Citations

Nov 7, 2019·Critical Reviews in Biotechnology·Zhe XuYu-Guo Zheng
Aug 1, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Siti Nor Hasmah IshakRaja Noor Zaliha Raja Abd Rahman
Sep 29, 2020·Frontiers in Bioengineering and Biotechnology·Lijun GuanShuwen Lu

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