Works (6)

Updated: July 5th, 2023 15:59

2010 article

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

Harris, J. M., Epting, K. L., & Kelly, R. M. (2010, March 18). Biotechnology Progress, Vol. 26, pp. 993–1000.

By: J. Harris n, K. Epting n & R. Kelly n

author keywords: xylose isomerase; hyperthermophile; Thermotoga neapolitana; chitin-binding domain
MeSH headings : Aldose-Ketose Isomerases / genetics; Aldose-Ketose Isomerases / metabolism; Chitin / metabolism; Enzyme Stability; Enzymes, Immobilized / genetics; Enzymes, Immobilized / metabolism; Kinetics; Protein Binding; Protein Structure, Tertiary / genetics; Protein Structure, Tertiary / physiology; Recombinant Proteins / genetics; Recombinant Proteins / metabolism; Thermotoga neapolitana / enzymology
topics (OpenAlex): Enzyme Catalysis and Immobilization; Biofuel production and bioconversion; Pancreatic function and diabetes
TL;DR: Molecular modeling results suggest that the N‐terminal fusion impacted subunit interactions, thereby contributing to the enhanced thermostability of both the unbound and immobilized CBD‐TNXI, and played a role in modifying active site structure. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2007 article

Probing the stability of native and activated forms of α2-macroglobulin

Kaczowka, S. J., Madding, L. S., Epting, K. L., Kelly, R. M., Cianciolo, G. J., & Pizzo, S. V. (2007, October 9). International Journal of Biological Macromolecules, Vol. 42, pp. 62–67.

By: S. Kaczowka*, L. Madding*, K. Epting n, R. Kelly n, G. Cianciolo* & S. Pizzo*

author keywords: alpha M-2; alpha(2)-macroglobulin; alpha(2)-macroglobulin and proteinase incorporation; alpha(2)-macroglobulin and norproteolytic incorporation of lysozyme; alpha(2)-macroglobulin stabilization
MeSH headings : Amino Acid Sequence; Animals; Hot Temperature; Humans; Ligands; Molecular Sequence Data; Peptide Hydrolases / chemistry; Protein Conformation; Transition Temperature; alpha-Macroglobulins / chemistry
topics (OpenAlex): Blood properties and coagulation; Protein purification and stability; Protease and Inhibitor Mechanisms
TL;DR: Differential scanning calorimetry and urea gel electrophoresis demonstrate that both bait region cleavage and covalent incorporation of protein ligands in the thioester pocket play critical roles in the stability of α 2 M complexes. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2006 article

Role of the β1 Subunit in the Function and Stability of the 20S Proteasome in the Hyperthermophilic ArchaeonPyrococcus furiosus

Madding, L. S., Michel, J. K., Shockley, K. R., Conners, S. B., Epting, K. L., Johnson, M. R., & Kelly, R. M. (2006, November 18). Journal of Bacteriology, Vol. 189, pp. 583–590.

By: L. Madding n, J. Michel n, K. Shockley n, S. Conners n, K. Epting n, M. Johnson n, R. Kelly n

MeSH headings : Archaeal Proteins / genetics; Archaeal Proteins / metabolism; Archaeal Proteins / physiology; Calorimetry, Differential Scanning; Genome, Archaeal; Hot Temperature; Molecular Chaperones / genetics; Molecular Chaperones / metabolism; Proteasome Endopeptidase Complex / genetics; Proteasome Endopeptidase Complex / metabolism; Proteasome Endopeptidase Complex / physiology; Protein Subunits / genetics; Protein Subunits / metabolism; Protein Subunits / physiology; Pyrococcus furiosus / genetics; Pyrococcus furiosus / metabolism; Temperature; Transcription, Genetic
topics (OpenAlex): Ubiquitin and proteasome pathways; Peptidase Inhibition and Analysis; Glycosylation and Glycoproteins Research
TL;DR: Results indicate that the β1 subunit in the P. furiosus 20S proteasome plays a thermostabilizing role and influences biocatalytic properties, suggesting that β subunit composition is a factor in archaeal proteasom function during thermal stress, when polypeptide turnover is essential to cell survival. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2005 article

Denaturation and Aggregation of Three α-Lactalbumin Preparations at Neutral pH

McGuffey, M. K., Epting, K. L., Kelly, R. M., & Foegeding, E. A. (2005, March 11). Journal of Agricultural and Food Chemistry, Vol. 53, pp. 3182–3190.

By: M. McGuffey n, K. Epting n, R. Kelly n & E. Foegeding n

author keywords: alpha-lactalbumin; whey proteins; denaturation and aggregation
MeSH headings : Calorimetry, Differential Scanning; Chemical Phenomena; Chemistry, Physical; Dimerization; Electrophoresis, Polyacrylamide Gel; Hot Temperature; Hydrogen-Ion Concentration; Lactalbumin / chemistry; Nephelometry and Turbidimetry; Protein Denaturation
topics (OpenAlex): Metabolism and Genetic Disorders; Probiotics and Fermented Foods; Infant Nutrition and Health
TL;DR: The denaturation and aggregation of reagent-grade, ion-exchange chromatography purified, and a commercial-grade alpha-lactalbumin were studied and the interrelationship between specific electrostatic interactions and hydrophobic attraction, in relation to the formation of disulfide-bonded products, is discussed. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2005 article

Influence of divalent cations on the structural thermostability and thermal inactivation kinetics of class II xylose isomerases

Epting, K. L., Vieille, C., Zeikus, J. G., & Kelly, R. M. (2005, March 1). FEBS Journal, Vol. 272, pp. 1454–1464.

By: K. Epting n, C. Vieille*, J. Zeikus* & R. Kelly n

author keywords: inactivation kinetics; metal cofactors; thermostability; xylose isomerases
MeSH headings : Aldose-Ketose Isomerases / antagonists & inhibitors; Aldose-Ketose Isomerases / chemistry; Aldose-Ketose Isomerases / metabolism; Bacillus / enzymology; Bacterial Proteins / antagonists & inhibitors; Bacterial Proteins / chemistry; Bacterial Proteins / metabolism; Cations, Divalent / pharmacology; Cobalt / pharmacology; Enzyme Stability; Escherichia coli / enzymology; Kinetics; Magnesium / pharmacology; Manganese / pharmacology; Protein Denaturation; Recombinant Proteins / antagonists & inhibitors; Recombinant Proteins / chemistry; Recombinant Proteins / metabolism; Thermodynamics; Thermotoga maritima / enzymology
topics (OpenAlex): Pancreatic function and diabetes; Biofuel production and bioconversion; Enzyme Structure and Function
TL;DR: The results reported here suggest that, unlike the other class II XIs examined, single metals are required for TNXI activity, but are not essential for its structural thermostability. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2002 article

Glucose‐to‐fructose conversion at high temperatures with xylose (glucose) isomerases from Streptomyces murinus and two hyperthermophilic Thermotoga species

Bandlish, R. K., Hess, J. M., Epting, K. L., Vieille, C., & Kelly, R. M. (2002, August 19). Biotechnology and Bioengineering, Vol. 80, pp. 185–194.

By: R. Bandlish n, J. Hess n, K. Epting n, C. Vieille* & R. Kelly n

author keywords: Thermotoga; xylose isomerase; Streptomyces murinus; hyperthermophile
MeSH headings : Aldose-Ketose Isomerases / chemistry; Aldose-Ketose Isomerases / classification; Aldose-Ketose Isomerases / metabolism; Bioreactors; Enzyme Activation; Enzymes, Immobilized / metabolism; Fructose / biosynthesis; Glucose / metabolism; Gram-Negative Anaerobic Straight, Curved, and Helical Rods / classification; Gram-Negative Anaerobic Straight, Curved, and Helical Rods / enzymology; Gram-Negative Anaerobic Straight, Curved, and Helical Rods / metabolism; Hot Temperature; Hydrogen-Ion Concentration; Sensitivity and Specificity; Species Specificity; Streptomyces / classification; Streptomyces / enzymology; Thermotoga maritima / classification; Thermotoga maritima / enzymology
topics (OpenAlex): Biofuel production and bioconversion; Diet, Metabolism, and Disease; Pancreatic function and diabetes
TL;DR: In the presence of both cations, these enzymes showed the potential to catalyze glucose-to-fructose conversion at 80 degrees C with estimated lifetime productivities on the order of 2000 kg fructose per kilogram enzyme, a value competitive with enzymes currently used at 55 degrees to 65 degrees C, but with the additional advantage of higher fructose concentrations. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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