Thermodynamics of ligand (substrate/end product) binding to endoxylanase from Chainia sp. (NCL-82-5-1)

Isothermal calorimetry and fluorescence titration studies

Subray Hegde, Ameeta R. Kumar, Krishna N. Ganesh, Chittoor P. Swaminathan, M. Islam Khan

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The binding of xylo-oligosaccharides to Chainia endoxylanase resulted in a decrease in fluorescence intensity of the enzyme with the formation of 1:1 complex. Equilibrium and thermodynamic parameters of ligand binding were determined by fluorescence titrations and titration calorimetry. The affinity of xylanase for the oligosaccharides increases in the order X2<X3<X4≤X5. Contributions from the enthalpy towards the free energy change decreased with increasing chain length from X2 to X4, whereas an increase in entropy was observed, the change in enthalpy and entropy of binding being compensatory. The entropically driven binding process suggested that hydrophobic interactions as well as hydrogen bonds play a predominant role in ligand binding. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)93-100
Number of pages8
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1388
Issue number1
DOIs
StatePublished - Oct 14 1998
Externally publishedYes

Fingerprint

Endo-1,4-beta Xylanases
Calorimetry
Entropy
Oligosaccharides
Titration
Thermodynamics
Enthalpy
Fluorescence
Ligands
Substrates
Hydrophobic and Hydrophilic Interactions
Chain length
Free energy
Hydrogen
Hydrogen bonds
Enzymes

Keywords

  • Chainia sp.
  • Endoxylanase
  • Fluorescence quenching
  • Isothermal calorimetry
  • Substrate binding

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

Cite this

Thermodynamics of ligand (substrate/end product) binding to endoxylanase from Chainia sp. (NCL-82-5-1) : Isothermal calorimetry and fluorescence titration studies. / Hegde, Subray; Kumar, Ameeta R.; Ganesh, Krishna N.; Swaminathan, Chittoor P.; Khan, M. Islam.

In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1388, No. 1, 14.10.1998, p. 93-100.

Research output: Contribution to journalArticle

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AB - The binding of xylo-oligosaccharides to Chainia endoxylanase resulted in a decrease in fluorescence intensity of the enzyme with the formation of 1:1 complex. Equilibrium and thermodynamic parameters of ligand binding were determined by fluorescence titrations and titration calorimetry. The affinity of xylanase for the oligosaccharides increases in the order X2<X3<X4≤X5. Contributions from the enthalpy towards the free energy change decreased with increasing chain length from X2 to X4, whereas an increase in entropy was observed, the change in enthalpy and entropy of binding being compensatory. The entropically driven binding process suggested that hydrophobic interactions as well as hydrogen bonds play a predominant role in ligand binding. Copyright (C) 1998 Elsevier Science B.V.

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