Maltooligosyl trehalose synthase mutant with improved thermal stability

Abstract

The present disclosure discloses a maltooligosyl trehalose synthase mutant with improved thermal stability, and belongs to the technical fields of enzyme engineering and protein engineering. The residual enzyme activities of the MTSase mutants S361R, S444E, S361R/S444E, S361K/S444E, G415P/S361R/S444E and G415P consistent with the present disclosure after treatment at 60° C. for 10 min are respectively 70.3%, 50.1%, 83.5%, 65.9%, 100% and 80.7%, which are respectively 1.6, 1.1, 1.9, 1.5, 2.3 and 1.9 times of that of the wild type. The half-lives of the S361R/S444E and G415P/S361R/S444E at 60° C. are respectively 14.9 min and 90.8 min which are respectively 3.2 and 19.7 times of that of the wild type, indicating that the thermal stability of the MTSase mutant consistent with the present disclosure is significantly improved than that of the wild type.

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