Modification of natural pigskin collagen via cryogrinding: a focused study on its physiochemical properties
Author:
Xu Yuling1, Liu Jialin1, Dai Lei1, Wang Haibo1, He Lang1, Xu Chengzhi1, Wei Benmei1, Zhang Juntao1, Kou Huizhi1
Affiliation:
1. School of Chemical and Environmental Engineering , Wuhan Polytechnic University , Wuhan , Hubei 430000 , P.R. China
Abstract
Abstract
Natural pigskin was subjected to cryogrinding before extraction, and effects of the approach on extraction rate, structure, and properties of collagen were prospected systematically. It was found that the extraction rate multiplied gradually from 22% to 40% with an extended grinding duration from 0 to 20 min. Compared with natural collagen, the ground one soared by about 80% concerning the net yield. Electrophoresis revealed the stereo structures of the extracted collagen were not destroyed when ground, while a small amount of it degraded accordingly, whose conclusion was further corroborated by circular dichroism (CD) and infrared spectrometry. Results from contact angle (CA) test clarified that the hydrophilicity of collagen enhanced with prolonged grinding. Moreover, analysis of fibrillogenesis behavior verified that, after grinding, the assembly rate for collagen in the turbidity assay dented with a lengthened equilibrium time; finer fibril network with larger pore size and weakened elasticity was later observed. Methyl thiazolyl tetrazolium (MTT) analysis manifested that ground collagen was more conducive to cell proliferation. This polymer processing approach not only provides us with a facile approach to manipulate capacities of collagen but also sheds light on other potential substances beneath the same principle.
Funder
Application Foundation Frontier Project of Wuhan Science and Technology Bureau National Natural Science Foundation of China
Publisher
Walter de Gruyter GmbH
Subject
Materials Chemistry,Polymers and Plastics,General Chemical Engineering
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