Enhancing trehalose production via <i>Bacillus</i> species G1 cyclodextrin glucanotransferase mutants: modifying disproportionation characteristics and thermal stability.

ABSTRACT: Inefficient conversion of small molecule maltooligosaccharides into trehalose greatly affects the cost of the production of trehalose by double enzyme method [maltooligosyl trehalose synthase (MTSase) and maltooligosyl trehalose trehalohyrolase (MTHase)]. This study used directed evolution to increase oligosaccharide utilization by the cyclomaltodextrin glucanotransferase (CGTase) from Bacillus species G1. This enzyme was chosen for its adaptability and stability in trehalose production. Model analysis revealed that the hydrogen bond distance between the N33K mutant and maltose reduced from 2.6 Å to 2.3 Å, increasing maltose affinity and boosting transglycosylation activity by 2.1-fold compared to the wild type. Further mutations improved thermal stability and optimum temperature, r

SUBMITTER: Miao B 

PROVIDER: S-EPMC11611815 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature