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

@article{Nagatomo2005PreparationAP,
  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},
  year={2005},
  volume={69},
  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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TLDR
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
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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.
TLDR
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
Immobilization of Enzymes in Protein Films Prepared Using Transglutaminase
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
Comparison of a β-Glucosidase and a β-Mannosidase from the Hyperthermophilic Archaeon Pyrococcus furiosus
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.
TLDR
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
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