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An Improved Method for the Preparation of Type I Collagen From Skin

An Improved Method for the Preparation of Type I Collagen From Skin

Published on: January 21, 2014

Functional Properties of Collagen Extracted from Catfish (Silurus triostegus) Waste

Ayat A Abbas¹, Khalida A Shakir², Marie K Walsh³

¹Biotechnology Research Center, University of AL-Nahrain, Baghdad 64074, Iraq.

Foods (Basel, Switzerland)

|March 10, 2022

Abstract:

Collagen is used for a variety of biomedical and pharmaceutical uses, such as osteoarthritis-related pain management, hypertension, tissue engineering, and human implants, and is generally derived from porcine or bovine. Collagen from these animals has limitations due to the risk of disease transmission and religious constraints. Therefore, this study investigated the extraction of collagen from catfish (Silurus triostegus) waste. Acid-solubilized collagen and pepsin-solubilized collagen were extracted from catfish skin, fin, head, bone, and muscle. SDS-PAGE patterns of the extracted collagen showed that the protein molecular weights ranged from 97 to 200 kDa and skin, bone, and fin collagen consisted of 2 distinct α chains, which is typical of type 1 collagen. The proximate composition (moisture, protein, fat, and ash) and yield of the obtained extracts were determined. Skin collagen extracts were selected for further investigation due to the high collagen yield. The effects of the pH and salt concentration on solubility, and the denaturation temperature, FTIR spectra, reverse-phase HPLC, and SEM analysis were investigated to characterize the collagen samples. Based on the characterization of catfish skin collagen, this waste material has potential for use in the pharmaceutical and food industries.

Keywords:

acid solubilized catfish collagen pepsin solubilized

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