Abstract
Trehalose synthase (TreS) is an enzyme which produces trehalose from maltose through intramolecular transglycosylation. In this study, a gene (cg2529) encoding for TreS from Corynebacterium glutamicum (CgTS) was cloned and expressed in Escherichia coli. The hexahistidinetagged CgTS showed an optimum temperature and pH of 35°C and pH 7.0, respectively. This enzyme was not thermostable, but stable in a broad pH range from pH 5.0 to 8.5. Its activity slightly increased by 5 mM Mg2+ and Fe2+, while it was strongly inhibited by 5 mM sodium dodecyl sulfate (SDS). CgTS catalyzed the conversion from maltose into trehalose, and vice versa. Lowering reaction temperature by 5°C from the optimum temperature significantly reduced hydrolysis activity to produce glucose as a by-product compared to transglycosylation activity to produce trehalose, leading to increase in the conversion yields from maltose into trehalose. Consequently, the maximum conversion yield by CgTS reached 69% at 25°C after 9 hr of reaction.
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Kim, TK., Jang, JH., Cho, HY. et al. Gene cloning and characterization of a trehalose synthase from Corynebacterium glutamicum ATCC13032. Food Sci Biotechnol 19, 565–569 (2010). https://doi.org/10.1007/s10068-010-0079-x
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DOI: https://doi.org/10.1007/s10068-010-0079-x