Production of Trehalose from Maltose by Whole Cells of Permeabilized Recombinant Corynebacterium glutamicum

Abstract

Trehalose (α-D-glucopyranosyl-1,1-α-D-glucopyranoside) is a stable and nonreducing disaccharide; can be used as sweetener, stabilizer, and humectant; and has many applications in the food, pharmaceutical, and cosmetic industries. Trehalose production from maltose catalyzed by trehalose synthase (TreS) is simple and economically feasible for industrial-scale application. Reducing the cost and enhancing the efficiency of TreS synthesis and the conversion of maltose to trehalose is critical for trehalose production. In this study, the homologous TreS was constitutively overexpressed in Corynebacterium glutamicum ATCC13032 by removing the repressor gene lacIq fragment in the plasmid, and TreS expression could be exempt from the inducer addition and induction process. For cell permeabilization, Triton X-100 was used as a permeabilization agent, and the treatment time was 3 h. In the conversion system, the permeabilized cells of recombinant C. glutamicum were used as biocatalysts, 300 g/L maltose was used as a substrate, and 173.7 g/L trehalose was produced within 12 h under 30 °C and pH 7.0 conditions. In addition, the whole-cell biocatalysts showed promising reusability. This study provides a safe, convenient, practical, and low-cost pathway for the production of trehalose.