A New Method of Gelatin Modified Collagen and Viscoelastic Study of Gelatin-Collagen Composite Hydrogel
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Article www.springer.com/13233 pISSN 1598-5032 eISSN 2092-7673
A New Method of Gelatin Modified Collagen and Viscoelastic Study of Gelatin-Collagen Composite Hydrogel Lang He†,1 Sheng Li†,1 Chengzhi Xu1 Benmei Wei1 Juntao Zhang1 Yuling Xu1 Beirong Zhu1 Yang Cao1 Xilin Wu1 Zhijin Xiong1 Rongrui Huang1 Jian Yang2 Haibo Wang*1
1
School of Chemical and Environmental Engineering, Wuhan Polytechnic University, Wuhan, Hubei, 430000, P. R. China 2 College of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, Hubei, 430000, P. R. China
Received February 1, 2020 / Revised March 21, 2020 / Accepted March 29, 2020
Abstract: Pure collagen materials are expensive with poor mechanical properties, which need modifications in most cases. As the degradation product of collagen, gelatin is cheap, degradable and biocompatible, but few literatures have reported the research about gelatin-collagen composite materials. This is because gelatin and collagen have different soluble temperatures—gelatin is soluble in hot water (≥30 oC) and swells in cold water. However, a low temperature (2-10 oC) is required to prepare and store collagen solution, and neutral collagen solution denatures quickly above the room temperature. In this study, gelatin was ground into powders and swelled in neutral bovine tendon pepsin-soluble collagen solution (BPSC) to form a homogeneous gelatin-collagen mixture, in light of the swelling characteristics of gelatin in cold water. The assembly properties and gel properties of this composite material were further studied. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) test results showed that the bovine tendon collagen had typical type-I collagen structural characterizations with two α chains of about 100 kDa and one β chain of about 200 kDa; while the SDS-PAGE pattern of gelatin displayed bands continuously distributed from 30 to 200 kDa. Amino acid composition analysis test indicated that the content of polar amino acids and the sum of acidic and base amino acids for gelatin were higher than that of BPSC. Studies on gel properties demonstrated that gelatin-collagen mixed solution had collagenlike assembly characteristics and assembly kinetics. The moduli of the assembled gel at 35 oC were equivalent to that of pure bovine tendon collagen system; moreover, the system moduli didn’t change with time with elastic moduli (G') of about 40 Pa. However, at 25 oC, the moduli of gelatin-collagen composite hydrogel increased with the extension of time, its G' increased about 18 times within 8 h, and the ratio of elastic modulus to viscous modulus (G'') increased 4.6 times, showing a significant aging effect of structural strength. Meanwhile, the mechanical strength of the composite hydrogel was also regulated by temperature—the gel was highly elastic (G'≈3,000 Pa, G'>>G'') at a low temperature (5 oC); as the temperature rose, the system moduli gradually decreased and the elastic gel transformed into waterlike fluid at 50 oC little by little. What’s more, gelatin-collagen composite hy
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