Collagen from porcine skin: a method of extraction and structural properties

Abstract

This paper presents a study of the processing of collagen-containing raw material and its changes in the course of targeted complex processing by hydrolysis, including freeze-drying. The pH, chemical composition, penetration magnitude, and critical shear stress were determined. The dried samples were examined using Fourier-transform infrared spectroscopy, and their microstructures were characterized. The characteristic property of the product developed was determined to be the presence of a relatively homogeneous fibrillar structure that promotes the functional capacity of the proteinoid-forming fibres in the compositions of foods from different groups.

Mn2+ Ions Confined by Electrode Microskin for Aqueous Battery beyond Intercalation Capacity

“…Collagen hydrolysate (CH), also called hydrolyzed collagen, collagen peptide academically, or gelatin commercially, is a mixture of polypeptides extracted from bovine or porcine skin/bones via partial hydrolysis of collagens. [ 14,15 ] Collagen molecules exist in the form of continuous repetition with the G–X–Y sequence, where G is glycine (Gly), X is proline (Pro), and Y is hydroxyproline (Hyp) or any other amino acids (i.e., phenylalanine and tyrosine). Collagen tucks in a triple‐helical structure because of the specific abundance of Hyp, Pro, and Gly.…”

“…Figure S1a (Supporting Information) shows a top view SEM image of smooth microskin, which is similar to a real skin mainly composed of collagen from mammals. [ 14,15 ] The corresponding energy dispersive spectroscopy (EDS; Figure S1e, Supporting Information) depicts the elemental distribution of C, N, and O, accounting for 60.82%, 19.84%, and 19.34% of the atomic ratio, respectively. During the EMS fabrication process, the utilized amount of CH was optimized as a key parameter, resulting in various thicknesses of the EMS on the surface of the δ‐MnO 2 cathode (denoted by EMS1, EMS2, EMS3, and EMS4; Figure 1c; Figure S2, Supporting Information), where the thickness of EMS1, EMS2, EMS3, and EMS4 is 6.6, 8.7, 10.1, and 13.4 µm, respectively.…”

An Overview of the Use of Equine Collagen as Emerging Material for Biomedical Applications

“…The inability to reproduce the full-length collagen molecule with the native post-translational modifications (i.e., hydroxylation) decreased the interest in the use of both prokaryotic and eukaryotic hosts (i.e., yeast, bacteria, mammalian cells, insects or plants) for its synthesis [ 41 ]. As regards collagen extraction from animal tissues, several sources have been investigated [ 36 ], including mammals (bovine [ 42 ], porcine [ 43 ], ovine [ 44 ], equine [ 45 , 46 ], rat [ 47 ]), avian (chicken [ 48 ]) and fish (jellyfish, fish, sponges) [ 49 ], with the aim of finding the optimal one in terms of biocompatibility, safety and availability.…”

Applying Methods of Mathematical Modeling in Cattle Breeding

“…In some cases, the form of the expression of dependence makes it possible to significantly reduce the volume of field experiments, reduce their labor intensity [4,5,7]. For example, having constructed the function of connection of complex parts for the natural measurement of parts of an animal's body, it becomes possible in specific economic cases to refuse measurements of this parameter [8,9,11].…”