Article Abstract:
The molecular mass of the Themococurs litoralis enzyme was determined at 119,000 Da by electrophoresis, while the Pyrococcus furiosus displayed a molecular mass of 110,000 Da under the same conditions. Both enzyme tested positive for bound sugar by the periodic acid-Schiff method and hence are glycoproteins. Each enzyme was capable of hydrolizing, along with the alpha-1,4 linkages in amylose and soluble starch. The enzymaes from the Thermococcus litoralis and Pyrococcus furiosus represent highly thermostable amylopullulanases. The identification of these enzymes profilles the saccharide-metabolizing systems possessed by these two organisms.
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Article Abstract:
Pyrococcus furiosus cells require peptides for growth, and can utilize an alternative carbon and energy source only if they are present. Not even a mixture containing all amino acids can replace this requirement. This result suggests that P. furiosus is auxotrophic for one or more amino acids. Intracellular levels of proteolytic enzymes were also noted to increase with low peptide availability and decrease when exposed to high peptide concentrations. It appears that intracellular proteolytic activity of P. furiosus is strongly dependent on growth conditions.
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Article Abstract:
The role of glycosyl hydrolase on the growth of Pyrococcus furiosus on carbohydrate-based media has been studied. P. furiosus is a hyperthermophilic archaeon that grows optimally at 100 degrees C and can thrive on peptide-based media in the presence of alpha-linked polysaccharides. Results indicated significant bacterial growth at 98 degrees C in the presence of beta-1,3- and beta-1,3-beta-1,4-glucans. Oligosaccharides were found to be the nutrients most effective in stimulating the growth of P. furiosus.
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