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 α-1,4 into α-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 °C and pH 5.5, prefers maltoheptaose and maltohexaose as substrates, and demonstrates minimal side hydrolytic activity.
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Acknowledgments
We gratefully thank Dr. Mariateresa Giuliano for the initial help, and Prof. Jeroen Hugenholtz (NIZO Food Research) for providing the pNZ8148 expression plasmid and NZ9000 L. lactis cells. We also thank Dr. Gerald Hofmann for helpful comments.
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Cimini, D., De Rosa, M., Panariello, A. et al. Production of a thermophilic maltooligosyl-trehalose synthase in Lactococcus lactis . J Ind Microbiol Biotechnol 35, 1079–1083 (2008). https://doi.org/10.1007/s10295-008-0384-z
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DOI: https://doi.org/10.1007/s10295-008-0384-z