Abstract
The endopolysaccharide accumulated by Thermococcus hydrothermalis was extracted and purified from a 4 h culture. It presented an “amylopectin-like” structure with an average chain length of 14 and a ramification degree of 7.5%. The glucosyltransferase was isolated, partially purified and characterized. The molecular mass was 42 kDa by SDS PAGE and 85 ± 5 kDa by gel filtration. This enzyme was able to use both Uridine-5′-DiPhosphoGlucose (UDPG) and Adenosine-5′-DiPhosphoGlucose (ADPG) as substrates. Optimal pH and temperature for the enzyme were 5.5 and 80°C, respectively. In the presence of 3.2 mM ADPG, the half life of the protein was 6 min at 110°C. The apparent K m value with the two substrates was 0.9 mM, but the V max was 9.7 fold higher for ADPG. A branching activity was also detected at high temperature, up to 80°C by different methods: phosphorylase stimulation, iodine, and branching linkage assays.
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Gruyer, S., Legin, E., Bliard, C. et al. The Endopolysaccharide Metabolism of the Hyperthermophilic Archeon Thermococcus hydrothermalis: Polymer Structure and Biosynthesis. Curr Microbiol 44, 206–211 (2002). https://doi.org/10.1007/s00284-001-0029-1
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DOI: https://doi.org/10.1007/s00284-001-0029-1