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中国精品科技期刊2020
祝赫,马堃,刘波,等. 葡萄籽原花青素对三文鱼片在冷藏期间品质及蛋白氧化的影响J. 食品工业科技,2026,47(4):1−9. doi: 10.13386/j.issn1002-0306.2025040203.
引用本文: 祝赫,马堃,刘波,等. 葡萄籽原花青素对三文鱼片在冷藏期间品质及蛋白氧化的影响J. 食品工业科技,2026,47(4):1−9. doi: 10.13386/j.issn1002-0306.2025040203.
ZHU He, MA Kun, LIU Bo, et al. Effect of Grape Seed Proanthocyanidins on Quality Characteristics and Protein Oxidation of Salmon salar Fillets during RefrigerationJ. Science and Technology of Food Industry, 2026, 47(4): 1−9. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2025040203.
Citation: ZHU He, MA Kun, LIU Bo, et al. Effect of Grape Seed Proanthocyanidins on Quality Characteristics and Protein Oxidation of Salmon salar Fillets during RefrigerationJ. Science and Technology of Food Industry, 2026, 47(4): 1−9. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2025040203.

葡萄籽原花青素对三文鱼片在冷藏期间品质及蛋白氧化的影响

Effect of Grape Seed Proanthocyanidins on Quality Characteristics and Protein Oxidation of Salmon salar Fillets during Refrigeration

  • 摘要: 目的:为探究葡萄籽原花青素(Grape seed proanthocyanidin,GSP)对水产品的保鲜作用。方法:本研究以三文鱼为对象,探究冷藏(4 ℃)过程(0、3、6、9、12 d)中不同浓度GSP对其理化性质、新鲜度、质构特性、肌肉微观结构及蛋白氧化等品质特性的调控作用。通过荧光光谱和圆二色光谱技术分析GSP对肌原纤维蛋白(Myofibrillar protein,MP)结构的影响机制。结果:至贮藏期结束,与对照组相比,GSP处理组pH变化减小,持水力显著提高(P<0.05),菌落总数(TVC)的增长显著减缓(P<0.05),0.75 mg/mL GSP处理组挥发性盐基氮(Total volatile basic nitrogen,TVB-N)可延缓3 d超出上限值,MP的羰基含量降低7.31%~18.27%,总巯基保留率提高2.8%~12.1%,肌纤维束结构完整性显著改善。荧光光谱分析显示,GSP通过静态猝灭机制与MP结合,抑制色氨酸残基暴露;圆二色光谱结果表明,0.75 mg/mL GSP处理组α-螺旋比例下降率(19%)显著低于对照组(34%),证实其对蛋白质二级结构的稳定作用。结论:综合表明,GSP通过调控蛋白氧化路径和分子构象,更有效维持三文鱼贮藏品质。本研究可为水产品天然抗氧化保鲜技术提供理论依据。

     

    Abstract: Objective: To investigate the preservative effect of grape seed proanthocyanidin (GSP) on aquatic products. Methods: Salmon salar was utilized as the model subject. The regulatory effects of different GSP concentrations on quality characteristics, including physicochemical properties, freshness, texture properties, muscle microstructure, and protein oxidation, were investigated throughout refrigerated storage (4 ℃)at intervals (0 d, 3 d, 6 d, 9 d, 12 d). The mechanism by which GSP influences the structure of myofibrillar protein (MP) was analyzed using fluorescence spectroscopy and circular dichroism (CD) spectroscopy. Results: By the end of storage, compared with the control group, pH variations were reduced and water-holding capacity was significantly increased (P<0.05) in GSP-treated groups. The increase in total viable count (TVC) was significantly inhibited (P<0.05). The exceeding of the upper limit for total volatile basic nitrogen (TVB-N) was delayed by 3 days in the 0.75 mg/mL GSP treatment group. The carbonyl content of MP was reduced by 7.31%−18.27%, and the retention rate of total sulfhydryl groups was increased by 2.8%−12.1%. The structural integrity of myofiber bundles was significantly improved. Fluorescence spectral analysis revealed that GSP bound to MP via a static quenching mechanism, inhibiting the exposure of tryptophan residues. CD spectroscopy results demonstrated that the reduction rate in α-helices proportion (19%) was significantly lower in the 0.75 mg/mL GSP group than in the control group (34%), confirming its stabilizing effect on protein secondary structure. Conclusion: It is comprehensively demonstrated that the quality of salmon during storage is more effectively maintained by GSP through the modulation of protein oxidation pathways and molecular conformation. This study can provide a theoretical basis for natural antioxidant preservation technologies in aquatic products.

     

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