Biotechnical production of trehalose through the trehalose synthase pathway: current status and future prospects
Trehalose (α-d-glucopyranosyl-(1 → 1)-α-d-glucopyranoside) is a non-reducing disaccharide composed of two glucose molecules linked by an α,α-1,1-glycosidic bond. It possesses physicochemical properties, which account for its biological roles in a variety of prokaryotic and eukaryotic organisms and invertebrates. Intensive studies of trehalose gradually uncovered its functions, and its applications in foods, cosmetics, and pharmaceuticals have increased every year. Currently, trehalose is industrially produced by the two-enzyme method, which was first developed in 1995 using maltooligosyltrehalose synthase (EC 22.214.171.124) and subsequently using maltooligosyltrehalose trehalohydrolase (EC 126.96.36.199), with starch as the substrate. This biotechnical method has lowered the price of trehalose and expanded its applications. However, when trehalose synthase (EC 188.8.131.52) was later discovered, this method for trehalose production using maltose as the substrate soon became a popular topic because of its simplicity and potential in industrial production. Since then, many trehalose synthases have been studied. This review summarizes the sources and characteristics of reported trehalose synthases, and the most recent advances on structural analysis of trehalose synthase, catalytic mechanism, molecular modification, and usage in industrial production processes.
KeywordsTrehalose Trehalose synthase Biological production Physicochemical properties Structural analysis
This work was funded by the 863 Project of China (No. 2013AA102102) and the National Natural Science Foundation of China (No. 31371788).
Compliance with ethical standards
Conflict of interest
The authors declare that they have no competing interests.
This article does not contain any studies with human participants or animals performed by any of the authors.
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