• Economic and Environmental Geology
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• v.47 no.1
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• pp.71-85
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• 2014

To study biogeochemical characteristics and origin organic matter, sediment samples were taken from Site of 1249C and Stie 1251B of ODP Leg 204. Data of Rock-Eval, isotope, and element analysis generally indicate dominance of marine organic matter in sediments deposited under marine sedimentary environment. Only Rock-Eval data are somewhat different from those of others owing to under-maturation of organic matter. Samples of Site 1249C show high content of gas hydrate, whereas Site 1251B low content of gas hydrate in some intervals of the core. This result may be accounted to different location of two cores and presence of transportation passage (Horizon A, BSR 2) of thermogenic gas in the core, 1249 C. However, Site 1251B Located in the basin of low accumulation of gas hydrate is presumed to be limited in the gas hydrate production. Because not only transportation passage is limited to move thermogenic gas from the core, but also gas supply was not enough. Therefore, the biogenic gas that resulted from diagenesis of there sediment is superior.

• Journal of Microbiology and Biotechnology
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• v.17 no.8
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• pp.1249-1253
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• 2007

A hyperthermostable endoglucanase from Pyrococcus horikoshii with the capability of hydrolyzing crystalline cellulose was analyzed. A protein engineering study was carried out to obtain a reduced-size mutant. Five amino acid residues at both the N- and C-terminus were found to be removable without any loss of activity or thermal stability. Site-directed mutagenesis was also performed on R102, N200, E201, H297, Y299, E342, and W377, residues possibly involved in the active center or in the recognition and binding of a cellulose substrate. The activity of the resulting mutants was considerably decreased, confirming that the mutated residues were all important for activity. A reduced-size enzyme, as active as the wild-type endoglucanase, was successfully obtained, plus the residues critical for its activity and specificity were confirmed. Consequently, an engineered enzyme with a reduced size was obtained, and the amino acids essential for activity were confirmed by site-directed mutagenesis and comparison with a known three-dimensional structure.