Research Article: Isolation, characterization and biocompatibility evaluation of collagen from Thunnus tonggol skin

Publish Year: 1400
نوع سند: مقاله ژورنالی
زبان: English
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JR_JIFRO-21-2_016

تاریخ نمایه سازی: 16 خرداد 1401

Abstract:

Acid-soluble collagen could be isolated from fish skin using acetic acid. In recent years, much attention has been paid to collagen from marine sources, mainly arising from the fact that there is no risk of contagious diseases. Moreover, by processing the fish, significant amounts of waste materials are produced which can be considered as a substitute for these collagen sources. Thunnus tonggol skin collagen was extracted by acid and base methods and evaluated by SDS-PAGE, FTIR and UV spectrophotometry and amino acid composition analysis. To determine biocompatibility, growth, and proliferation of extracted collagen, MTT and H&E staining methods were used. The results, predicated on SDS-PAGE and amino acid analysis, demonstrated that the fish skin collagen was of type I consisting of two α chains (α۱ and α۲) with molecular weight of ۱۳۵ kDa and mass fraction of β. FTIR analysis also revealed helical compositions of both collagens, and UV spectrophotometry in T. tonggol skin collagen indicated a maximum absorption of ۲۳۵ nm. The amount of collagen extracted from T. tonggol skin turned out to be ۱۷.۳% dry weight. Analysis of extracted collagen amino acids from the mentioned fish showed that glycine was the predominant amino acid. Human fibroblast culture presented a superior growth and good biocompatibility on extracted collagen. So, this type of collagen could be used in tissue engineering as a proper scaffold.

Authors

M.H. Samiei

Department of Natural Resources and Environment, Science and Research Branch, Islamic Azad University, Tehran, Iran

S. Jamili

Iranian Fisheries Science Research Institute (IFSRI), Agricultural Research, Education and Extension Organization (AREEO), Tehran, Iran

H. Nikukar

Medical Nanotechnology and Tissue Engineering Research Center, Yazd Reproductive Sciences Institute, Shahid Sadoughi University of Medical Sciences, Yazd, Iran

V. Razban

Department of Molecular Medicine, School of Advanced Medical Sciences and Technologies, Shiraz University of Medical Sciences, Shiraz, Iran

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