Abstract

Enzymatically crossliked gelatin hydrogel was submitted to two different drying methods: air drying and freeze drying. The resulting polymeric tridimensional arrangement (compact or porous, respectively) led to different thermal and swelling properties. Significant differences (p < 0.05) on thermal and mechanical characteristics as well as swelling in non-enzymatic gastric and intestinal simulated fluids (37 ºC) were detected. Water absorption data in such media was modelled according to Higuchi, Korsmeyer-Peppas, and Peppas-Sahlin equations. Freeze dried hydrogel showed Fickian diffusion behavior while air dried hydrogels presented poor adjustment to Higuchi model suggesting the importance of the relaxation mechanism at the beginning of swelling process. It was possible to conclude that the same gelatin hydrogel may be suitable to different applications depending on the drying process used.

Highlights

  • Hydrogels are a promising type of 3-dimensional crosslinked hydrophilic polymeric networks presenting interesting characteristics for biomedical applications since they do not dissolve in water at physiological temperature and pH conditions (Pal et al 2007)

  • Air dried hydrogel (ADH) has a vitreous aspect when compared to the freeze dried hydrogel (FDH) samples, which showed an opaque, whitish appearance

  • The air dried hydrogels (ADH) samples produced at the present work presented a smooth aspect at both surface and fracture suggesting that the drying method influenced the gelatin network conformation and interactions resulting in a smother microstructure

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Summary

Introduction

Hydrogels are a promising type of 3-dimensional crosslinked hydrophilic polymeric networks presenting interesting characteristics for biomedical applications since they do not dissolve in water at physiological temperature and pH conditions (Pal et al 2007). Gelatin hydrogels synthesis may be achieved by crosslinking with glutaraldehyde (Prata et al 2008), genipin (Devi and Maji 2010) or transglutaminase (Carvalho and Grosso 2006). Gelatin is a protein obtained by the hydrolysis of collagen from animals bones and skin and has been commonly used for pharmaceutical and medical applications because of its biodegradability and biocompatibility in physiological environments (Khan and Schneider 2013). Gelatin presents appealing physico-chemical properties such as (i) great capacity for modification at amino acids level, (ii) low immunogenicity and cytotoxicity, (iii) FDA approval as a clotting agent and exudate-absorbing construct, (iv) hydrogel formation by facile, low cost procedures (Einerson et al 2002)

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