Purification and characterization of an extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, a Thermococcus sp

Article Abstract:

The extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, Thermococcus sp strain B-1001, clearly belongs to the genus Thermococcus based on its G+C content and 16S rRNA sequence. Such classification is consistent with the strain's morphological and physiological characteristics, which are similar to the characteristics of the Thermococcus genus. These were gleaned from the purification and characterization of the extremely thermophilic anaerobic archaeon strain B1001, isolated from a hot-spring environment in Japan.

Anaerobic bacteria

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Alteration of specific activity and stability of thermostable neutral protease by site-directed mutagenesis

Article Abstract:

Astructure-activity relationship analysis was conducted on the neutral protease (NprM) of Bacillus stearothermophilus using site-directed mutagenesis. Replacement of the Glu-143 residue with Gln or Asp resulted in loss of enzyme activity, confirming this site's function as an active site. Proteolytic activity could be enhanced by substituting Ala, Trp and Trp for Phe-114, Tyr-110 and Tyr-211, respectively. In addition, a more stable protease was obtained by replacing the autolysis site, Tyr-93 with either Gly or Ser.

Analysis, Usage, Proteases, Enzymes, Mutagenesis

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Characterization of DNA polymerase from Pyrococcus sp. strain KOD1 and its application to PCR

Article Abstract:

Isolation and characterization of a DNA polymerase from the archaebacteria Pyrococcus sp. strain KOD1 were undertaken to determine the suitability of this polymerase in polymerase chain reaction techniques. Results indicate that KOD DNA polymerase has characteristics superior to that of other DNA polymerases particularly in terms of mutation frequency. Further, KOD DNA polymerase-based polymerase chain reactions have shorter reaction time.

Physiological aspects, DNA polymerases

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