Elucidation of hydration dynamics of locust bean gum–collagen composites by impedance and thermoporometry

•Systematic studies reveal rearrangement of bound water cluster of collagen due to LBG.•Non-covalent and covalent interactions reorder hydrogen bonding network.•Interconnected porous architecture of composites is LBG concentration dependent. The intricacy of the different parameters involved in the...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Carbohydrate polymers 2014-03, Vol.103, p.250-260
Hauptverfasser: Kanungo, Ivy, Fathima, Nishter Nishad, Jonnalagadda, Raghava Rao, Unni Nair, Balachandran
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:•Systematic studies reveal rearrangement of bound water cluster of collagen due to LBG.•Non-covalent and covalent interactions reorder hydrogen bonding network.•Interconnected porous architecture of composites is LBG concentration dependent. The intricacy of the different parameters involved in the hydration dynamics of collagen influences its performance as biomaterials. This work presents the molecular motions of collagen originating from the solvents and locust bean gum (LBG), which reveal the changes in solvation dynamics of the biopolymers affecting the surface as well as interfacial properties. Water, as a probe liquid bound in collagen has been investigated using a combination of thermoporometry, ATR-FTIR, circular dichroic spectroscopy, dielectric spectroscopy and SEM to explore the influence of LBG on collagen with respect to static and dynamic behaviour. The relaxation process of collagen in the frequency range of 0.01Hz to 105Hz and thermoporometry results indicate that the interfacial hydration dynamics are dependent on the applied concentration of LBG. This investigation explicitly reflects the rearrangements of the structural water clusters around the charged amino acids of collagen. These results can be employed to redesign the approach towards the development of collagen based biomaterials.
ISSN:0144-8617
1879-1344
DOI:10.1016/j.carbpol.2013.12.051