Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus
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...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2022-12-01
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| Series: | Food Chemistry: X |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157522002826 |
| _version_ | 1797985671612203008 |
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| author | Yuan Fu Chuanhao Liu Xiaohui Yan Guochuan Jiang Qiao Dang Liyan Wang Xuejun Liu |
| author_facet | Yuan Fu Chuanhao Liu Xiaohui Yan Guochuan Jiang Qiao Dang Liyan Wang Xuejun Liu |
| author_sort | Yuan Fu |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-11T07:21:53Z |
| format | Article |
| id | doaj.art-2dc249a3fb16441c9666910a52106766 |
| institution | Directory Open Access Journal |
| issn | 2590-1575 |
| language | English |
| last_indexed | 2024-04-11T07:21:53Z |
| publishDate | 2022-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj.art-2dc249a3fb16441c9666910a521067662022-12-22T04:37:11ZengElsevierFood Chemistry: X2590-15752022-12-0116100484Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidusYuan Fu0Chuanhao Liu1Xiaohui Yan2Guochuan Jiang3Qiao Dang4Liyan Wang5Xuejun Liu6College of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, ChinaExyte Shanghai Co., Ltd., Shanghai, ChinaFinance and Taxation College, Jilin Business and Technology College, No. 1666, Kalun Lake Street, Changchun 130102, Jilin, ChinaCollege of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, ChinaCollege of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, ChinaCollege of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, China; Corresponding authors.College of Food Science and Engineering, Jilin Agricultural University, No. 2888 Xincheng Street, Changchun 130118, China; Corresponding authors.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.http://www.sciencedirect.com/science/article/pii/S2590157522002826Hypomesus olidusMuscle protein fractionsPhysicochemical and functional properties |
| spellingShingle | Yuan Fu Chuanhao Liu Xiaohui Yan Guochuan Jiang Qiao Dang Liyan Wang Xuejun Liu Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus Food Chemistry: X Hypomesus olidus Muscle protein fractions Physicochemical and functional properties |
| title | Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus |
| title_full | Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus |
| title_fullStr | Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus |
| title_full_unstemmed | Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus |
| title_short | Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus |
| title_sort | physicochemical and functional properties of the muscle protein fraction of hypomesus olidus |
| topic | Hypomesus olidus Muscle protein fractions Physicochemical and functional properties |
| url | http://www.sciencedirect.com/science/article/pii/S2590157522002826 |
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