A gene encoding an endo-β-1,3-glucanase from Thermotoga maritima MSB8 (TmβG) was cloned and expressed in Escherichia coli. The purified enzyme produced various β-1,3-glucooligosaccharides from soluble laminarin, and mainly β-1,3-glucooligosaccharides smaller than laminaritetrose from insoluble curdlan. The optimum pH and temperature of the enzyme were 5.0 and 80°C, respectively. TmβG inhibited the growth of Candida albicans, which indicates that the enzyme could potentially be used as an anti-fungal agent to control invasive infections.
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Acknowledgments This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) Grant funded by the Ministry of Education, Science and Technology (2012R1A1A2005524).
All Science Journal Classification (ASJC) codes
- Food Science
- Applied Microbiology and Biotechnology