Enhancing the Thermostability of Phytase to Boiling Point by Evolution-Guided Design.

ABSTRACT: The good thermostability of enzymes is an important basis for their wide application in industry. In this study, the phytase APPA from Yersinia intermedia was designed by evolution-guided design. Through the collection of homologous sequences in the NCBI database, we obtained a sequence set composed of 5,569 sequences, counted the number and locations of motif N-X-T/S, and selected the sites with high frequency in evolution as candidate sites for experiments. Based on the principle that N-glycosylation modification sites are located on the protein surface, 13 mutants were designed to optimize the number and location of N-glycosylation sites. Through experimental verification, 7 single mutants with improved thermostability were obtained. The best mutant, M14, with equal cataly

SUBMITTER: Wang Q 

PROVIDER: S-EPMC9195953 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature