Abstract
Agarose hydrogels which constitute a special class of soft matter are undoubtedly one of the most studied biopolymer gels. However, certain issues such as why the sulfate salts and sulfate content in the agarose molecules reduce the gel strength are still not very clear. The present work provides a detailed analysis of structural changes with respect to coil-helix transition or aggregation of helices in the aqueous agarose solutions and hydrogels that accompanied the systematic addition of sodium sulfate. A combined approach which includes the differential scanning calorimetry and temperature-dependent vacuum-ultraviolet circular dichroism measurements permitted the accurate estimates of the energy changes for coil-helix transition and helix-helix interactions. The hydration process of agarose molecule investigated from differential scanning calorimetry and concentration-dependent ultrasonic measurements indicated the loss of both the freeze bound and nonfreezable water molecules with the increase of sulfate content in the solution. Temperature-dependent fluorescence measurements using pyrene as a probe indicated polarity changes when the gel network is created in waters of different salt concentration. Changes in the hydrogen bonding of the water molecules confined in the gel network have been monitored from the intensity ratios of ice-like and liquid-like -OH stretching band of water Fourier transform infrared (FTIR) spectra. Analysis of the -OH stretching band showed the strengthening of hydrogen bonding of water molecules in the gel which tend to weaken with the subsequent addition of sodium sulfate.
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