Recovery and Characterization of Keratin from Fish Scale Collagen Extraction Residue

Qiuyu LI; Hongmei LIU; Yan LI; Can LUO; Yan LIU

doi:10.13386/j.issn1002-0306.2020070321

Volume 42 Issue 9

Apr. 2021

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Science and Technology of Food Industry > 2021 > 42(9): 179-185. > DOI: 10.13386/j.issn1002-0306.2020070321

LI Qiuyu, LIU Hongmei, LI Yan, et al. Recovery and Characterization of Keratin from Fish Scale Collagen Extraction Residue[J]. Science and Technology of Food Industry, 2021, 42(9): 179−185. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2020070321.

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Recovery and Characterization of Keratin from Fish Scale Collagen Extraction Residue

Qiuyu LI^{1, 2,},
Hongmei LIU³,
Yan LI⁴,
Can LUO¹,
Yan LIU^{1, 2, ,}

1.
College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China
2.
Hunan Provincial Research Center of Engineering and Biotechnology for Fermentative Food, Changsha 410128, China
3.
Zhijiang Dong Autonomous County Bureau of Agriculture and Rural Areas, Zhijiang 419100, China
4.
School of Chemistry and Food Engineering, Changsha University of Science and Technology, Changsha 410128, China

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Received Date: July 26, 2020
Available Online: March 03, 2021

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Abstract

Abstract

In order to fully develop the economic value of fish scales, expand the source of keratin, in this study, the collagen-extracted grass carp fish scale residues were used as raw materials, single factor experiment and orthogonal experiment were used to determine the optimal extraction process of keratin, and the extracted fish scale keratin was characterized. The results showed that under the condition of 60 g pepsin in 1% citric acid solution at 4 ℃ for 24 h, the highest collagen removal ratew as obtained, with the best removal effect and structural integrit. The optimal process conditions for extracting grass carp scale keratin were as follows: Extraction temperature 60 ℃, sodium hydroxide concentration 9%, material-liquid ratio 1:12.5. The UV absorption peaks of fish scale keratin were at 218.2, 280.4 nm, respectively. SDS-PAGE electrophoresis showed that the apparent molecular weight of fish scale keratin was about 48 kDa. Infrared results showed that the secondary structure of keratin was α-helix, and the characteristics of amino acid components were basically the same as wool keratin.
- grass carp scales,
- keratin,
- separation and purification,
- structural identification,
- property analysis

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References (32)

References

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