Novel, thermostable family-13-like glycoside hydrolase fromMethanococcus jannaschii
- Cite this article as:
- Kim, J.W., Terc, H.A., Flowers, L.O. et al. Folia Microbiol (2001) 46: 475. doi:10.1007/BF02817989
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A novel glycoside hydrolase from the hyperthermophilic archaeonMethanococcus jannaschii has been cloned intoEscherichia coli. Extremely thermoactive and thermostable amylolytic activity was confirmed in partially purified enzyme solution. This enzyme exhibited a temperature optimum of 100 °C and a pH optimum pH 5.0–8.0. Hydrolysis of large 1,6-α- and 1,4-α-linked polysaccharides yielded glucose polymers of 1–7 units. Incubation with amylose displayed the highest activity. The catalyst was activated and stabilized by Ca2+ and exhibited extreme thermostability at 100 °C with a half-life of 78 h.