Separation and some properties of collagens from <i>Ctenopharyngodon idella</i> scales

Nguyen Thi Kim An; Dam Xuan Thang; Nguyen Ngoc Thanh; Nguyen Thi Huong; Le Thi Bich Thao

doi:10.15625/2525-2518/22294

Author affiliations

Authors

Nguyen Thi Kim An \(^1\) Hanoi University of Industry, 298 Cau Dien Street, Tay Tuu Ward, Ha Noi, Viet Nam https://orcid.org/0000-0002-2592-4950
Dam Xuan Thang \(^1\) Hanoi University of Industry, 298 Cau Dien Street, Tay Tuu Ward, Ha Noi, Viet Nam https://orcid.org/0000-0002-3940-6935
Nguyen Ngoc Thanh \(^1\) Hanoi University of Industry, 298 Cau Dien Street, Tay Tuu Ward, Ha Noi, Viet Nam https://orcid.org/0000-0003-0280-0370
Nguyen Thi Huong \(^1\) Hanoi University of Industry, 298 Cau Dien Street, Tay Tuu Ward, Ha Noi, Viet Nam
Le Thi Bich Thao \(^2\) Institute of Biology, Vietnam Academy of Science and Technology (VAST), 18 Hoang Quoc Viet, Nghia Do Ward, Ha Noi, Viet Nam https://orcid.org/0000-0002-9191-3635

DOI:

https://doi.org/10.15625/2525-2518/22294

Keywords:

Ctenopharyngodon idella, grass carp, fish scales, type I collagen, amino acid sequence

Abstract

Collagen was successfully extracted from scales of grass carp (Ctenopharyngodon idella) at room temperature (20–25 °C) using acid alone, as well as with pepsin or protease assistance. SDS-PAGE analysis revealed that acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) contained characteristic α-chains of approximately 120 kDa, consistent with type I collagen, whereas protease-solubilized collagen (PrSC) exhibited lower molecular weight chains (35–60 kDa). MS/MS spectrometry analysis confirmed that the isolated collagen was type I. Herein, the amino acid sequence of collagen isolated from grass carp cultivated in Viet Nam is reported for the first time, along with physicochemical properties, morphology, and elemental composition of the collagen. According to the research, grass carp scales represent a potential source for type I collagen extraction. Pepsin efficiently yields collagen with high purity and an intact triple-helix structure, while protease effectively produces collagen with lower molecular weight. These properties highlight the potential of both enzymes for various industrial and biomedical applications.

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