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Thermally stable collagen from Piranha and Rohu with improved physical, biochemical, and morphological properties
Author(s) -
Paul Esther Jemima,
Padmapriya B.
Publication year - 2021
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.50796
Subject(s) - collagen fibril , solubility , extraction (chemistry) , thermal stability , salt (chemistry) , chemistry , fish <actinopterygii> , biochemistry , biophysics , biology , chromatography , organic chemistry , fishery
Collagen is the most common structural protein pertinent to the skin and other tissues in humans. The market for collagen extends from food, cosmetics to therapeutics and is estimated to be $6.63 billion by 2025. Piranha and Rohu are some of the primarily consumed fish varieties in South India and the extraction of collagen from the scales of Piranha is reported for the first time through this study. Physical, biochemical, and morphological properties of the collagen extracted were compared with a freshwater variant, Rohu. The UV, IR spectra, amino acid, SDS PAGE analysis confirmed the presence of triple helical native conformation. Further, higher degree of solubility was observed at low pH and salt concentrations. The T d was 38.27 and 37.4°C and T m was 92.37 and 94.04°C for the scale collagen of Piranha and Rohu respectively and was comparable to bovine sources. Electron micrograph presented loose, parallel oriented long fibers with interconnected fibrils. Hence the collagen extracted, having retained the helical conformation and higher thermal stability, can be a safe alternative for various biomedical applications.