Effect of Interaction between Soy Protein Isolate and <i>Nemipterus virgatus</i> Myosin on Its Gel Properties

LIU Zhen; WANG Jinxiang; LI Xuepeng; GAO Ruichang; LI Jianrong; YI Shumin; YANG Qing; WEI Zhengpeng; JI Guangren

doi:10.13386/j.issn1002-0306.2022110207

Volume 44 Issue 16

Aug. 2023

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Science and Technology of Food Industry > 2023 > 44(16): 122-130. > DOI: 10.13386/j.issn1002-0306.2022110207

LIU Zhen, WANG Jinxiang, LI Xuepeng, et al. Effect of Interaction between Soy Protein Isolate and Nemipterus virgatus Myosin on Its Gel Properties[J]. Science and Technology of Food Industry, 2023, 44(16): 122−130. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022110207.

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Effect of Interaction between Soy Protein Isolate and Nemipterus virgatus Myosin on Its Gel Properties

1.
College of Food Science and Engineering, Bohai University, National Technology Research and Development Sub-center for Surimi and Surimi Products Processing, Jinzhou 121013, China
2.
College of Food and Biotechnology Engineering, Jiangsu University, Zhenjiang 212013, China
3.
Rongcheng Taixiang Food Products Co., Ltd., Ministry of Agriculture Key Laboratory of Frozen Prepared Marine Foods Processing, Weihai 234309, China
4.
Jinzhou Bijiashan Food Co., Ltd., Jinzhou 121007, China

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Received Date: November 20, 2022
Available Online: June 15, 2023

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Abstract

Abstract

In this study, myosin isolated from Nemipterus virgatus was added with 0%~8%（w/w）soybean protein isolate (SPI) and the physicochemical, spectroscopic, and gel properties of the composite system were analyzed, in order to investigate the effect of interaction between myosin and SPI on the gel properties of myosin. The results showed that after the addition of SPI, the endogenous fluorescence intensity of the composite system decreased, whereas the ultraviolet absorbance, the total sulfhydryl content, and hydrogen bond as well as hydrophobic interactions increased. These results indicated that there were the hydrophobic interactions, hydrogen bonds, disulfide bonds, and other covalent and non-covalent interactions between SPI and Nemipterus virgatus myosin, which altered the structure and conformation of myosin. Meanwhile, the gel strength, hardness, and β-sheet content of the myosin-SPI composite gels all increased initially and then decreased as the increase addition of SPI. Furthermore, the total sulfhydryl and hydrophobic contents of the myosin-SPI composite system got the highest values when added 4% SPI, which increased by 64.46% and 13.53% compared with the control group, respectively. The gel strength and hardness of the myosin-SPI composite gels were also reached the highest values when added 4% SPI, which increased by 8.66% and 9.21% compared with the control group, respectively. It was also found that a part of α-helices transformed into β-sheets and the gel network was most compact and homogeneous. Therefore, the moderate addition of SPI could promote the aggregation and cross-linking of myosin through the interaction forces such as hydrophobic interactions, hydrogen bonds, and disulfide bonds, and improve the gel properties of myosin.
- Nemipterus virgatus myosin,
- soybean protein isolate,
- interaction,
- gel property

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References (39)

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