Abstract
Dehydrothermal (DHT) treatment was used to improve the properties of collagen casings because of its non-cytotoxicity. Understanding the effects of DHT treatment on the structure and mechanical properties of collagen films is beneficial to developing satisfying collagen casings. Herein, DHT treatment with various temperatures (85–145 °C) and timescales (1–7 days) were investigated. It was clarified that the chemical crosslinking covalent bond between collagen molecules was formed after the DHT treatment. Crosslinking density increased with increasing DHT treatment temperatures, contributing to the increase of tensile strength up to over three times of that of the untreated collagen film. The increased crosslinking density was also found when increasing the DHT treatment time, and the maximum was obtained in 3 days. Further DHT treatment time did not change the crosslinking density. The damage in the triple helix structure and the self-assembly of collagen molecules were observed from IR and SAXS. The extent of denaturation increased with increasing DHT treatment temperature and time, although the effect of the DHT treatment time on the denaturation was more moderate. When the DHT treatment temperature was as high as 145 °C or the DHT treatment time exceeded 5 days, serious denaturation occurs, leading to the deterioration of mechanical properties.
Highlights
Biocompatible, biodegradable, and edible biomaterials like protein have received a great deal of attention in wound dressing, scaffolds, and the food industry recently [1,2]
The well-organized self-assembly aggregation of collagen molecules gives a striation on the surface of fibril, the periodicity of which striation is about 64 nm based on different origins [6]
The morphological properties were assessed by scanning electron microscopy (SEM), and the water content of the collagen films after the DHT treatment was evaluated by thermogravimetry analysis (TGA)
Summary
Biocompatible, biodegradable, and edible biomaterials like protein have received a great deal of attention in wound dressing, scaffolds, and the food industry recently [1,2]. Our previous study showed that the artificial film prepared from natural collagen has poor mechanical properties and a high swelling ratio because of the layered structure with a large gap filled with fine collagen fibrils [9]. It is meaningful to clarify the relationship between the formation of crosslinking and the occurrence of the denaturation This is critical to obtain the favorable mechanical properties of collagen materials. Yunoki et al evaluated the extent of denaturation upon the application of DHT treatment at several specific temperatures for various periods of time without showing any information regarding mechanical properties [19]. To the best of our knowledge, there is no more information available about the effect of the relation between the extent of denaturation and the degree of crosslinking on the mechanical properties of collagen films in various DHT temperatures and timescales. The morphological properties were assessed by scanning electron microscopy (SEM), and the water content of the collagen films after the DHT treatment was evaluated by thermogravimetry analysis (TGA)
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