Characterization, heterologous expression and engineering of trehalase for biotechnological applications

Abstract

Trehalose is a non-reducing disaccharide connected by α-1,1-glycosidic bonds; it is widely distributed in bacteria, fungi, yeast, insects, and plant tissues and plays various roles. It can be hydrolyzed by trehalase into two glucose molecules. Trehalases from different sources have been expressed in Escherichia coli, Pichia pastoris, Saccharomyces cerevisiae, baculovirus-silkworm, and other expression systems; however, it is most common in E. coli. The structural characteristics of different glycoside hydrolase (GH) family trehalases and the sources of trehalase have been analyzed. The catalytic mechanism of GH37 trehalase has also been elucidated in detail. Moreover, the molecular modification of trehalase has mainly focused on directed evolution for improving enzyme activity. We comprehensively reviewed the current application status and adaptable transformations was comprehensively overviewed in the context of industrial performance. We suggest that the level of recombinant production is far from meeting industrial requirements, and the catalytic performance of trehalase needs to be improved urgently. Finally, we discuss developmental prospects and future trends.