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Updated: Jun 15, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
Functional characterization of trehalose biosynthesis genes from E. coli: an osmolyte involved in stress tolerance
Toms C Joseph1, Lawrance Anbu Rajan, Nirmala Thampuran
1Microbiology, Fermentation and Biotechnology Division, Central Institute of Fisheries Technology, Matsyapuri P.O., Cochin, Kerala, India. tomscjoseph@gmail.com
Abstract:
Trehalose (1-alpha-D-glucopyranosyl-1-alpha-D-glucopyranoside), a non-reducing disaccharide is a major compatible solute, which maintains fluidity of membranes and protects the biological structure of organisms under stress. In this study, trehalose-6-phosphate synthase (otsA) and trehalose-6-phosphate phosphatase (otsB) genes encoding for trehalose biosynthesis from Escherichia coli was cloned as an operon and expressed in E. coli M15(pREP4). The recombinant E. coli strain showed a threefold increase in the activity of otsBA pathway enzymes, compared to the control strain. The transgenic E. coli accumulated up to 0.86 mg/l of trehalose. The sequence of otsA and otsB genes reported in this study contains several base substitutions with that of reported sequences in GenBank, resulting in the altered amino acid sequences of the translated proteins.
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