Preparation and Properties of Gelatin-Immobilized β-Glucosidase from Pyrococcus furiosus

  title={Preparation and Properties of Gelatin-Immobilized $\beta$-Glucosidase from Pyrococcus furiosus},
  author={Hidetaka Nagatomo and Yoh-ichi Matsushita and Kazuhiro Sugamoto and Takanao Matsui},
  journal={Bioscience, Biotechnology, and Biochemistry},
  pages={128 - 136}
Hyperthermostable β-glucosidase from Pyrococcus furiosus was enclosed in gelatin gel by cross-linking with transglutaminase. Gelatin-immobilized β-glucosidase was considerably more thermostable than the native enzyme. Lyophilized immobilisate was stored at 90 °C for 1 month without loss of activity. The immobilized β-glucosidase catalyzed transglucosylation of 5-phenylpentanol with 10.0 equivalent of cellobiose at pH 5.0 and 70 °C for 12 h to afford 5-phenylpentyl β-D-glucopyranoside in 41… Expand
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N‐terminal fusion of a hyperthermophilic chitin‐binding domain to xylose isomerase from Thermotoga neapolitana enhances kinetics and thermostability of both free and immobilized enzymes
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Microbial Strain Development for Hyperproduction of â Glucosidase through ã Rays Mutagenesis And Expression Cloning
The mutant BGL proved to be 1.6 fold efficient for cellobiose hydrolysis with lower activation energy (Ea) and thermodynamically more stable against denaturants than parent BGL, which may have substantial applications in biofuel and biorefinery industries. Expand
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Catalytical Potency of β-Glucosidase from the Extremophile Pyrococcus furiosus in Glucoconjugate Synthesis
The extremely thermostable wild type and recombinant β-glucosidases, from Pyrococcus furiosus, served as catalysts for the biotransformation of new glucoconjugates at elevated temperatures, and seems to be a useful biocatalyst for regio- and stereoselective sugar derivative synthesis. Expand
Synthesis of oligosaccharides catalyzed by thermostable β-glucosidase fromPyrococcus furiosus
The thermostable β-glucosidase fromPyrococcus furiosus has been shown to produce tri-and tetrasaccharides with lactose as a substrate (0.73–1.44 mol/kg) at elevated temperatures (75–95°C). The enzymeExpand
An extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus : a comparison with other glycosidases
The cytoplasmic enzyme was purified to homogeneity and its properties were compared with those of other glycosidases, and a high similarity is observed with a β-galacto/glucosidase from... Expand
Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus.
Cell-free extracts of cellobiose-grown cells of the hyperthermophile Pyrococcus furiosus contain very high activities of a beta-glucosidase, which was purified 22-fold to apparent homogeneity, indicating that the enzyme comprises nearly 5% of the total cell protein. Expand
The catalytic potency of β-glucosidase from Pyrococcus furiosus in the direct glucosylation reaction
Abstract Enzymes from extremophiles operate at conditions that are different from their ‘normal’ counterparts, and are therefore a useful extension of the enzyme toolbox. In this paper, the directExpand
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An αsl-casein film prepared using transglutaminase was applied as a support for immobilized enzymes. That is, the enzyme, to be immobilized was added to a mixture of 5% ocsl-casein andExpand
Oligosaccharide synthesis by the hyperthermostable β-glucosidase from Pyrococcus furiosus: kinetics and modelling
Abstract Oligosaccharides can be synthesised from monosaccharides or disaccharides, using glycosidases as a catalyst. To investigate the potential of this synthesis with β-glycosidase from PyrococcusExpand
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Two distinct exo-acting, β-specific glycosyl hydrolases were purified to homogeneity from crude cell extracts of the hyperthermophilic archaeon Pyrococcus furiosus: a β-glucosidase, corresponding toExpand
Novel substrate specificity of a membrane‐bound β‐glycosidase from the hyperthermophilic archaeon Pyrococcus horikoshii
A β‐glycosidase gene homolog of Pyrococcus horikoshii (BGPh) was successfully expressed in Escherichia coli. The enzyme was localized in a membrane fraction and solubilized with 2.5% Triton X‐100 atExpand
Influence of gelatin matrices cross-linked with transglutaminase on the properties of an enclosed bioactive material using beta-galactosidase as model system.
The data suggest that the immobilization procedure only moderately affects the activity of enzymes catalysing the reaction of a small compound if gelatin with high jelly strength is cross-linked in a 10% solution with transglutaminase. Expand