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中国精品科技期刊2020
陈佩钰,刘学铭,唐道邦,等. 青梅多酚提取物对肌肉蛋白氧化及亚硝化调控作用[J]. 华体会体育,2025,46(7):1−8. doi: 10.13386/j.issn1002-0306.2024040192.
引用本文: 陈佩钰,刘学铭,唐道邦,等. 青梅多酚提取物对肌肉蛋白氧化及亚硝化调控作用[J]. 华体会体育,2025,46(7):1−8. doi: 10.13386/j.issn1002-0306.2024040192.
CHEN Peiyu, LIU Xueming, TANG Daobang, et al. Regulation of Prunus mume Polyphenols Extracts on Muscle Protein Oxidation and Nitrosation[J]. Science and Technology of Food Industry, 2025, 46(7): 1−8. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024040192.
Citation: CHEN Peiyu, LIU Xueming, TANG Daobang, et al. Regulation of Prunus mume Polyphenols Extracts on Muscle Protein Oxidation and Nitrosation[J]. Science and Technology of Food Industry, 2025, 46(7): 1−8. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024040192.

青梅多酚提取物对肌肉蛋白氧化及亚硝化调控作用

Regulation of Prunus mume Polyphenols Extracts on Muscle Protein Oxidation and Nitrosation

  • 摘要: 植物多酚调控肉制品的氧化及亚硝化是当前的研究热点,然而相关调控机制尚不明晰。鉴于此,本研究以青梅多酚提取物(Prunus mume polyphenols extracts,PMP)为例,在羟自由基模拟氧化体系下探究植物多酚对肌肉中主要蛋白(肌原纤维蛋白与肌浆蛋白)的氧化调控规律,并利用主成分分析法结合亚硝化过程中3-硝基酪氨酸(3-Nitrotyrosine,3-NT)和亚硝基二甲胺(Nitrosodimethylamine,NDMA)的变化探讨PMP抑制肌肉蛋白亚硝化的机制。结果表明,PMP的添加会延缓羟自由基介导的蛋白质氧化过程,表现为蛋白质羰基、二聚酪氨酸与游离氨基酸的形成得到抑制,巯基损失减少。当PMP添加量为100 mg/g蛋白时,模拟氧化后,3-NT含量为30.25±2.47 nmol/mg蛋白(肌原纤维蛋白)和37.54±2.30 nmol/mg蛋白(肌浆蛋白),相较氧化对照组(未添加PMP)显著减少39.89%与47.88%(P<0.05);NDMA含量为0.76±0.05 nmol/mg蛋白(肌原纤维蛋白)和0.67±0.06 nmol/mg蛋白(肌浆蛋白),相较氧化对照组(未添加PMP)显著减少24.30%与24.61%(P<0.05)。相关性分析的结果表明,NDMA的形成与蛋白质羰基、聚二酪氨酸以及巯基值显著相关(P<0.05),证实了PMP可通过蛋白质的氧化调控实现对亚硝胺形成的抑制。以上研究结果可为植物多酚在肉制品亚硝化调控的应用提供理论依据。

     

    Abstract: The regulation of plant polyphenols on oxidation and nitrosation of meat products has been a focus of current research, but the relevant regulatory mechanisms are still unclear. In view of this, the oxidative regulation of plant polyphenols on two major muscle proteins (myofibrillar protein and sarcoplasmic protein) under the simulated hydroxyl radical oxidation system was investigated with Prunus mume polyphenol extracts (PMP) as an example. The mechanism of inhibiting nitrosation of muscle protein by PMP was investigated by principal component analysis combined with the changes of 3-nitrotyrosine (3-NT) and nitrosodimethylamine (NDMA) during nitrosation. The results showed that the addition of PMP could delay the protein oxidation induced by hydroxyl radicals, which inhibited the protein carbonyls, dimerized tyrosine and free amino acids, and reduced the loss of sulfhydryl group. When the addition of PMP was 100 mg/g protein, after simulated oxidation, the 3-NT content was 30.25±2.47 nmol/mg protein (myofibrillar protein) and 37.54±2.30 nmol/mg protein (sarcoplasmic protein), respectively. Compared with the oxidation control group (without PMP), it was reduced by 39.89% and 47.88%, respectively. The content of NDMA was 0.76±0.05 nmol/mg protein (myofibrillar protein) and 0.67±0.06 nmol/mg protein (sarcoplasmic protein), respectively, which were decreased by 24.30% and 24.61% compared with oxidized control group (P<0.05). Correlation analysis showed that the formation of NDMA was significantly correlated with protein carbonyls, polydityrosine and sulfhydryl groups (P<0.05), confirming that PMP could inhibit the formation of nitrosamines through the oxidation regulation of proteins. The above results can provide theoretical basis for the application of plant polyphenols in nitrosation regulation of meat products.

     

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