Effects of NaCl Concentration on Physicochemical Properties and Gel-forming Ability of Myofibrillar Protein from European Eel

YANG Yu; LI Jieyu; SHI Linfan; REN Zhongyang; WENG Wuyin

doi:10.13386/j.issn1002-0306.2022100301

Volume 44 Issue 17

Aug. 2023

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Science and Technology of Food Industry > 2023 > 44(17): 68-75. > DOI: 10.13386/j.issn1002-0306.2022100301

YANG Yu, LI Jieyu, SHI Linfan, et al. Effects of NaCl Concentration on Physicochemical Properties and Gel-forming Ability of Myofibrillar Protein from European Eel[J]. Science and Technology of Food Industry, 2023, 44(17): 68−75. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022100301.

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Effects of NaCl Concentration on Physicochemical Properties and Gel-forming Ability of Myofibrillar Protein from European Eel

1.
Fuqing Product Quality Inspection Institute, Fuqing 350300, China
2.
College of Food and Biological Engineering, Jimei University, Engineering Research Center of the Modern Technology for Eel Industry, Ministry of Education, Xiamen 361021, China

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Received Date: November 01, 2022
Available Online: July 05, 2023

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Abstract

Abstract

The effect of NaCl concentration on heat-induced gel forming ability of myofibrillar protein from European eel muscle was studied. The turbidity, surface hydrophobicity and reactive sulfhydryl groups of the protein was measured. Meanwhile, the properties of heat-induced gel of myofibrillar protein at 0.1, 0.3 and 0.5 mol/L NaCl concentration were investigated. It was found that turbidity, surface hydrophobicity and reactive sulfhydryl groups began to increase at 30, 35 and 40 ℃, respectively. With the increase of NaCl concentration, the temperature of endothermic peaks of myofibrillar protein decreased, while the storage modulus and loss modulus increased. The breaking strength of heat-induced protein gel prepared with 0.5 mol/L NaCl was 98.81 g, which was higher than that of the heat-induced protein gel prepared with low NaCl concentration. The increased NaCl concentration could promote the interaction between myosin heavy chain and actin according to the electrophoresis analysis. Based on the results of Fourier transform infrared spectra and scanning electron microscopy, heat-induced myofibrillar protein gel with 0.5 mol/L NaCl had a highest Amide II/Amide I intensity ratio and densest network. The result of this study suggested that myofibrillar protein from European eel muscle was prone to denature at above 35 ℃, and the gel strength and network structure of heat-induced myofibrillar protein gels could be improved by increasing the addition of NaCl. The obtained results will provide theoretical guidance for controlling the quality of eel based heat-processed food by using salt concentration and temperature.
- European eel,
- myofibrillar protein,
- gelling properties,
- heat induced gelation,
- microstructure

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