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Michael W. Bauer
North Carolina State University
EnzymeGlycoside hydrolasePyrococcus furiosusBiochemistryBiology
11Publications
10H-index
508Citations
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Publications 11
Newest
#1Jun GaoH-Index: 1
#2Michael W. BauerH-Index: 10
Last. Robert M. KellyH-Index: 53
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Pyrococcus furiosus was found to grow on chitin, adding this polysacharide to the inventory of carbohydrates utilized by this hyperthermophilic archaeon. Accordingly, two open reading frames (chiA [Pf1234] and chiB [Pf1233]) were identified in the genome of P. furiosus, which encodes chitinases with sequence similarity to proteins from the glycosyl hydrolase family 18 in less-thermophilic organisms. Both enzymes contain multiple domains that consist of at least one binding domain and one catalyt...
67 CitationsSource
#1Susan G CadyH-Index: 1
#2Michael W. BauerH-Index: 10
Last. Robert M. KellyH-Index: 53
view all 7 authors...
Publisher Summary Glycosylhydrolases have been isolated from a variety of heterotrophic hyperthermophiles and include glucanases, hemicellulases, and cellulases. Pyrococcus furiosus , a hyperthermophilic heterotroph isolated by Fiala and Stetter from geothermal regions of Vulcano Island, Italy, grows on a wide range of α - and β -1inked carbohydrates, a property supported by the enzyme inventory revealed in its genome sequence. This chapter describes the approaches used for the cloning and expre...
9 CitationsSource
#1Stephen T ChangH-Index: 1
#2Kimberley N ParkerH-Index: 6
Last. Robert M. KellyH-Index: 53
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Publisher Summary Hyperthermophilic α-glucosidases could also provide valuable insights into protein function, structure, and stability at high temperatures. Indeed, it is the intrinsic high temperature activity and stability of these proteins that have fueled considerable effort into the development of these and other glycosylhydrolases for use in starch conversion technology. Currently employed mesophilic enzymes exhibit limited tolerance to the high temperatures and pH variations encountered ...
11 CitationsSource
#1Lance E. Driskill (NCSU: North Carolina State University)H-Index: 4
#2Kevin Kusy (NCSU: North Carolina State University)H-Index: 1
Last. Robert M. Kelly (NCSU: North Carolina State University)H-Index: 53
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Utilization of a range of carbohydrates for growth by the hyperthermophile Pyrococcus furiosus was investigated by examining the spectrum of glycosyl hydrolases produced by this microorganism and the thermal labilities of various saccharides. Previously, P. furiosus had been found to grow in batch cultures on several α-linked carbohydrates and cellobiose but not on glucose or other β-linked sugars. Although P. furiosus was not able to grow on any nonglucan carbohydrate or any form of cellulose i...
34 Citations
#1Lance E. Driskill (NCSU: North Carolina State University)H-Index: 4
#2Michael W. Bauer (NCSU: North Carolina State University)H-Index: 10
Last. Robert M. Kelly (NCSU: North Carolina State University)H-Index: 53
view all 3 authors...
The synergistic interaction among three β-specific glycosidases from the hyperthermophilic archaeon Pyrococcus furiosus, namely two endoglucanases (EglA and LamA) and an exo-acting β-glucosidase (Bgl), on barley-glucan and laminarin, was examined. In addition to following glucose release and the generation of reducing sugar ends, the distribution and amounts of oligomeric products from β-1,3- and β-1,4-linked substrates were determined as a function of extent of hydrolysis at 98°C. Positive inte...
21 CitationsSource
#1Michael W. Bauer (NCSU: North Carolina State University)H-Index: 10
#2Lance E. Driskill (NCSU: North Carolina State University)H-Index: 4
Last. Robert M. Kelly (NCSU: North Carolina State University)H-Index: 53
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The eglA gene, encoding a thermostable endoglucanase from the hyperthermophilic archaeon Pyrococcus furiosus, was cloned and expressed in Escherichia coli. The nucleotide sequence of the gene predicts a 319-amino-acid protein with a calculated molecular mass of 35.9 kDa. The endoglucanase has a 19-amino-acid signal peptide but not cellulose-binding domain. The P. furiosus endoglucanase has significant amino acid sequence similarities, including the conserved catalytic nucleophile and proton dono...
115 Citations
Comparisons of catalytic mechanisms have not previously been performed for homologous enzymes from hyperthermophilic and mesophilic sources. Here, the β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus was recombinantly produced in Escherichia coli and shown to have biophyscial and biochemical properties identical to those of the wild-type enzyme. Moreover, the recombinant enzyme was subjected to a detailed kinetic investigation at 95 °C to compare its catalytic mechanism to t...
42 CitationsSource
#1Michael W. Bauer (NCSU: North Carolina State University)H-Index: 10
#2Lance E. Driskill (NCSU: North Carolina State University)H-Index: 4
Last. Robert M. Kelly (NCSU: North Carolina State University)H-Index: 53
view all 3 authors...
Abstract Glycosyl hydrolases from hyperthermophiles are, thus far, the most widely studied enzyme class from these organisms. Not only are there many biotechnological opportunities for these enzymes, but the rapidly increasing amount of information about their genetic, biochemical and biophysical characteristics (recently genomic sequencing data for both P. furiosus and P. horikoshi have been published on the Internet) make them ideal candidates for the study of biocatalysis and protein thermost...
45 CitationsSource
The hyperthermophilic archaeon Pyrococcus furiosus grows optimally at 100(deg)C by the fermentation of peptides and carbohydrates. From this organism, we have purified to homogeneity an intracellular protease, previously designated PfpI (P. furiosus protease I) (S. B. Halio, I. I. Blumentals, S. A. Short, B. M. Merrill, and R. M. Kelly, J. Bacteriol. 178:2605-2612, 1996). The protease contains a single subunit with a molecular mass of approximately 19 kDa and exists in at least two functional co...
34 Citations
#1Michael W. Bauer (NCSU: North Carolina State University)H-Index: 10
#2Edward J. BylinaH-Index: 1
Last. Robert M. Kelly (NCSU: North Carolina State University)H-Index: 53
view all 4 authors...
Abstract 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 to the one previously purified by Kengen et al. (Kengen, S. W. M., Luesink, E. J., Stams, A. J. M., and Zehnder, A. J. B. (1993) Eur. J. Biochem. 213, 305-312), and a β-mannosidase. The β-mannosidase and β-glucosidase genes were isolated from a genomic library by expression screening. The nucle...
101 CitationsSource
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