Engineering lipases for temperature adaptation: Structure function correlation

Publication date: Available online 8 August 2019Source: Biochimica et Biophysica Acta (BBA) - Proteins and ProteomicsAuthor(s): Rakesh Kumar, Shelly Goomber, Jagdeep KaurAbstractBacillus lipases are industrially attractive enzymes due to their broad substrate specificity and optimum alkaline pH. However, narrow temperature range of action and low thermostability restrain their optimal use and thus, necessitate attention. Several laboratories are engaged in protein engineering of Bacillus lipases to generate variants with improved attributes for decades using techniques such as directed evolution or rational design. This review summarizes the effect of mutations on the conformational changes through in silico modeling and their manifestation with respect to various biochemical parameters. Various studies have been put together to develop a perspective on the molecular basis of biocatalysis of lipases holding industrial importance.

Source: Biochimica et Biophysica Acta (BBA) Proteins and Proteomics - August 10, 2019 Category: Biochemistry Source Type: research