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Updated: Jul 4, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
Production of a thermophilic maltooligosyl-trehalose synthase in Lactococcus lactis
Donatella Cimini1, Mario De Rosa, Andrea Panariello
1Department of Experimental Medicine, Section of Biotechnology and Molecular Biology, Faculty of Medicine and Surgery, Second University of Naples, via De Crecchio 7, Naples, Italy.
Abstract:
The thermoacidophilic archaeon Sulfolobus solfataricus MT4 encodes a maltooligosyltrehalose synthase (MTS), that catalyzes an intramolecular transglycosylation process converting the glycosidic linkages at the reducing end of dextrins from alpha-1,4 into alpha-1,1. In this research the gene encoding MTS was cloned and expressed in Lactococcus lactis NZ9000 using the so-called NICE system. Growth conditions of the recombinant strain were optimized in flask experiments in relation to enzyme production. Batch experiments in 2 L-fermenters were performed on the best identified semidefined medium and 256 U L(-1) of recombinant MTS were produced. Purified recombinant MTS shows its optimal activity at 70 degrees C and pH 5.5, prefers maltoheptaose and maltohexaose as substrates, and demonstrates minimal side hydrolytic activity.
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