Michael William Bauer

Works (9)

Updated: March 10th, 2025 12:14

2003 article

Growth of Hyperthermophilic Archaeon Pyrococcus furiosus on Chitin Involves Two Family 18 Chitinases

Gao, J., Bauer, M. W., Shockley, K. R., Pysz, M. A., & Kelly, R. M. (2003, June 1). Applied and Environmental Microbiology, Vol. 69, pp. 3119–3128.

By: J. Gao n, M. Bauer n, K. Shockley n, M. Pysz n & R. Kelly n 

MeSH headings : Amino Acid Sequence; Calorimetry; Chitin / metabolism; Chitinases / chemistry; Chitinases / classification; Chitinases / genetics; Chitinases / metabolism; Culture Media; Hexosaminidases / chemistry; Hexosaminidases / genetics; Hexosaminidases / metabolism; Hot Temperature; Molecular Sequence Data; Pyrococcus furiosus / enzymology; Pyrococcus furiosus / growth & development; Pyrococcus furiosus / metabolism; Recombinant Proteins / metabolism; Sequence Analysis, DNA
topics (OpenAlex): Studies on Chitinases and Chitosanases; Legume Nitrogen Fixing Symbiosis; Enzyme Production and Characterization
TL;DR: Two open reading frames (chiA and chiB) 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, indicating that these two enzymes work together to recruit chit in-based substrates for P.furiosus growth. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2001 journal article

alpha-Glucosidase from Pyrococcus furiosus

Hyperthermophilic Enzymes. Part A, 330, 260–269.

By: S. Chang, K. Parker, M. Bauer & R. Kelly 

Source: NC State University Libraries
Added: August 6, 2018

2001 journal article

beta-Endoglucanase from Pyrococcus furiosus

Hyperthermophilic Enzymes. Part A, 330, 346–354.

By: S. Cady, M. Bauer, W. Callen, M. Snead, E. Mathur, J. Short, R. Kelly 

Source: NC State University Libraries
Added: August 6, 2018

1999 journal article

An endoglucanase, eglA, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes beta-1,4 bonds in mixed-linkage(1 -> 3),(1 -> 4)-beta-D-glucans and cellulose

Journal of Bacteriology, 181(1), 284–290.

By: M. Bauer, L. Driskill, W. Callen, M. Snead, E. Mathur & R. Kelly 

Source: NC State University Libraries
Added: August 6, 2018

1999 journal article

Relationship between glycosyl hydrolase inventory and growth physiology of the hyperthermophile Pyrococcus furiosus on carbohydrate-based media

Applied and Environmental Microbiology, 65(3), 893–897.

By: L. Driskill, K. Kusy, M. Bauer & R. Kelly 

Source: NC State University Libraries
Added: August 6, 2018

1999 article

Synergistic interactions among β‐laminarinase, β‐1,4‐glucanase, and β‐glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus during hydrolysis of β‐1,4‐, β‐1,3‐, and mixed‐linked polysaccharides

Driskill, L. E., Bauer, M. W., & Kelly, R. M. (1999, January 1). Biotechnology and Bioengineering, Vol. 66, pp. 51–60.

By: L. Driskill n, M. Bauer n & R. Kelly n 

topics (OpenAlex): Enzyme Production and Characterization; Biofuel production and bioconversion; Polysaccharides and Plant Cell Walls
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Sources: NC State University Libraries, NC State University Libraries
Added: August 6, 2018

1998 article

Glycosyl hydrolases from hyperthermophilic microorganisms

Bauer, M. W., Driskill, L. E., & Kelly, R. M. (1998, April 1). Current Opinion in Biotechnology, Vol. 9, pp. 141–145.

By: M. Bauer*, L. Driskill n & R. Kelly n 

MeSH headings : Archaea / physiology; Bacterial Physiological Phenomena; Biotechnology; Enzyme Stability; Glycoside Hydrolases / classification; Glycoside Hydrolases / physiology; Temperature
topics (OpenAlex): Enzyme Production and Characterization; Biofuel production and bioconversion; Enzyme Catalysis and Immobilization
TL;DR: Glycosyl hydrolases from hyperthermophiles are, thus far, the most widely studied enzyme class from these organisms and make them ideal candidates for the study of biocatalysis and protein thermostability at extremely high temperatures. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

1998 article

The Family 1 β-Glucosidases from Pyrococcus furiosus and Agrobacterium faecalis Share a Common Catalytic Mechanism

Bauer, M. W., & Kelly, R. M. (1998, November 12). Biochemistry, Vol. 37, pp. 17170–17178.

By: M. Bauer n & R. Kelly n 

MeSH headings : 1-Deoxynojirimycin / pharmacology; Binding, Competitive; Calorimetry, Differential Scanning; Catalysis / drug effects; Gluconates / pharmacology; Glucose / pharmacology; Hot Temperature; Hydrogen-Ion Concentration; Lactones; Pyrococcus furiosus / enzymology; Recombinant Proteins / antagonists & inhibitors; Recombinant Proteins / chemistry; Recombinant Proteins / metabolism; Rhizobium / enzymology; Substrate Specificity / drug effects; Thioglucosides / pharmacology; beta-Glucosidase / antagonists & inhibitors; beta-Glucosidase / genetics; beta-Glucosidase / metabolism
topics (OpenAlex): Enzyme Production and Characterization; Enzyme Catalysis and Immobilization; Biofuel production and bioconversion
TL;DR: The recombinant beta-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. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

1997 journal article

Purification and characterization of two functional forms of intracellular protease PFPI from the hyperthermophilic Archaeon Pyrococcus furiosus

Applied and Environmental Microbiology, 63(1), 289–295.

By: S. Halio, M. Bauer, S. Mukund, M. Adams & R. Kelly 

Source: NC State University Libraries
Added: August 6, 2018

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