Identification of a hot-spot to enhance Candida rugosa lipase thermostability by rational design methods.

ABSTRACT: Lipase is one of the most widely used classes of enzymes in biotechnological applications and organic chemistry. Candida rugosa lipases (CRL) can catalyze hydrolysis, esterification and transesterification with high regio-, stereo- and enantio-selectivity. However, thermal inactivation above 45 °C limits CRL's applications. Studies on improving the thermal stability of CRL are often limited by its slow-growing eukaryotic expression host, which is not suitable for large-scale screening. Identification of thermally stable mutants by rational design, regarded as an efficient substitution of experimental efforts, would provide a method for site-directed improvement of CRL. In this study, mutation-induced stability changes in CRL Lip1 were predicted by three rational design methods. Foll

SUBMITTER: Li G 

PROVIDER: S-EPMC9077275 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature