Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insights

Arginine (Arg), a safe basic amino acid, modulates interprotein interactions and impacts the processing characteristics of myofibrillar proteins (MP) in meat products, as numerous studies have demonstrated. This study aimed to explore the effects of varying concentrations of Arg (0.025, 0.050, 0.100, 0.200 %) on the physicochemical properties and gel behavior of yak MP. Utilizing yak MP as the substrate, we assessed and analyzed the physicochemical attributes and gel performance of the MP-Arg composite system. The findings revealed that Arg facilitates MP unfolding and internal group exposure, effectively mitigating oxidative tertiary structure alterations. Arg exerts potent antioxidant activity on MP, augmenting their water-holding capacity, which ameliorates gel properties. In this experiment, 0.05 % Arg maximally inhibited oxidative damage to MP, with protection being concentration-dependent. Collectively, these findings suggest that Arg effectively inhibits the oxidative degradation of MP structure and promotes the formation of enhanced gel characteristics.

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Publication Details

Journal
Food Chemistry X
Published
2024-09-16
DOI
https://doi.org/10.1016/j.fochx.2024.101839
Citations
6
Primary Topic
Muscle metabolism and nutrition
Type
article
Field-Weighted Citation Impact
1.96

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article

Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insights

Yuqi Wang, Rongsheng Du, Na Li, Lina Wang et al.
6 citations
Food Chemistry X
Muscle metabolism and nutrition
1.96
article

Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insights

Yuqi Wang, Rongsheng Du, Na Li, Lina Wang, Shulin Zhang, Qiuyu Wang, Honghong He, Yi-Wen Mei, Linlin Wang, Xiaofang Dao
article en
6 citations

Abstract

Arginine (Arg), a safe basic amino acid, modulates interprotein interactions and impacts the processing characteristics of myofibrillar proteins (MP) in meat products, as numerous studies have demonstrated. This study aimed to explore the effects of varying concentrations of Arg (0.025, 0.050, 0.100, 0.200 %) on the physicochemical properties and gel behavior of yak MP. Utilizing yak MP as the substrate, we assessed and analyzed the physicochemical attributes and gel performance of the MP-Arg composite system. The findings revealed that Arg facilitates MP unfolding and internal group exposure, effectively mitigating oxidative tertiary structure alterations. Arg exerts potent antioxidant activity on MP, augmenting their water-holding capacity, which ameliorates gel properties. In this experiment, 0.05 % Arg maximally inhibited oxidative damage to MP, with protection being concentration-dependent. Collectively, these findings suggest that Arg effectively inhibits the oxidative degradation of MP structure and promotes the formation of enhanced gel characteristics.

Food Chemistry XVol. 24
Xinjiang Agricultural University (CN), Sichuan Academy of Agricultural Sciences (CN), Southwest Minzu University (CN)
Natural Science Foundation of Xinjiang Province, National Natural Science Foundation of China, Natural Science Foundation of Xinjiang
Zero hunger
Openalex Percentile: Top 15%
Muscle metabolism and nutrition
1.96
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