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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.

Modification of natural pigskin collagen via cryogrinding: a focused study on its physiochemical properties