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• W1544679009 abstract "Extracellular pullulanases were purified from cell-free culture supernatants of the marine thermophilic archaea Thermococcus litoralis (optimal growth temperature, 90°C) and Pyrococcus furiosus (optimal growth temperature, 98°C). The molecular mass of the T. litoralis enzyme was estimated at 119,000 Da by electrophoresis, while the P. furiosus enzyme exhibited a molecular mass of 110,000 Da under the same conditions. Both enzymes tested positive for bound sugar by the periodic acid-Schiff technique and are therefore glycoproteins. The thermoactivity and thermostability of both enzymes were enhanced in the presence of 5 mM Ca 2+ , and under these conditions, enzyme activity could be measured at temperatures of up to 130 to 140°C. The addition of Ca 2+ also affected substrate binding, as evidenced by a decrease in K m for both enzymes when assayed in the presence of this metal. Each of these enzymes was able to hydrolyze, in addition to the α-1,6 linkages in pullulan, α-1,4 linkages in amylose and soluble starch. Neither enzyme possessed activity against maltohexaose or other smaller α-1,4-linked oligosaccharides. The enzymes from T. litoralis and P. furiosus appear to represent highly thermostable amylopullulanases, versions of which have been isolated from less-thermophilic organisms. The identification of these enzymes further defines the saccharide-metabolizing systems possessed by these two organisms." @default.
• W1544679009 created "2016-06-24" @default.
• W1544679009 creator A5008964909 @default.
• W1544679009 creator A5081561177 @default.
• W1544679009 date "1993-08-01" @default.
• W1544679009 modified "2023-10-14" @default.
• W1544679009 title "Characterization of Amylolytic Enzymes, Having Both α-1,4 and α-1,6 Hydrolytic Activity, from the Thermophilic Archaea <i>Pyrococcus furiosus</i> and <i>Thermococcus litoralis</i>" @default.
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• W1544679009 doi "https://doi.org/10.1128/aem.59.8.2614-2621.1993" @default.
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