Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus

Yuan Fu; Chuanhao Liu; Xiaohui Yan; Guochuan Jiang; Qiao Dang; Liyan Wang; Xuejun Liu

Food Chemistry: X (Dec 2022)

Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus

Yuan Fu,
Chuanhao Liu,
Xiaohui Yan,
Guochuan Jiang,
Qiao Dang,
Liyan Wang,
Xuejun Liu

Affiliations

Yuan Fu: College of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, China
Chuanhao Liu: Exyte Shanghai Co., Ltd., Shanghai, China
Xiaohui Yan: Finance and Taxation College, Jilin Business and Technology College, No. 1666, Kalun Lake Street, Changchun 130102, Jilin, China
Guochuan Jiang: College of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, China
Qiao Dang: College of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, China
Liyan Wang: College of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, China; Corresponding authors.
Xuejun Liu: College of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, China; Corresponding authors.

Journal volume & issue: Vol. 16
p. 100484

Abstract

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The physicochemical and functional properties of myofibrillar protein (MP), sarcoplasmic protein (SP), and myostromin (MY) in Hypomesus olidus muscle were evaluated and reported in this study. These fractions are rich in Glu. Three proteins exhibited significantly different morphologies, colors, and particle sizes. The main protein bands of MP, SP, and MY are 15–220 kDa, 26–60 kDa, and 15–245 kDa, respectively. In particular, MP is more hydrophobic. Three proteins exhibited a maximum UV absorption peak at 270 nm, and all amide I secondary structures were shown to be composed of repetitive units (e.g., α-helices and β-sheets). The three proteins demonstrated a predominantly amorphous halo, with Td values of 52.22 °C, 59.16 °C, and 58.09 °C. Regarding their properties in water/oil absorption, emulsification, and foaming, MP is the most preferred, followed by SP and MY. In conclusion, Hypomesus olidus muscle proteins are novel and potential functional nutrition ingredients for the food industry.

Published in Food Chemistry: X

ISSN: 2590-1575 (Online)
Publisher: Elsevier
Country of publisher: Netherlands
LCC subjects: Technology: Home economics: Nutrition. Foods and food supply; Technology: Chemical technology: Food processing and manufacture
Website: https://www.journals.elsevier.com/food-chemistry-x

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