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...

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Main Authors: Yuqi Wang, Yiwen Mei, Rongsheng Du, Shulin Zhang, Qiuyu Wang, Xiaofang Dao, Na Li, Lina Wang, Linlin Wang, Honghong He
Format: Article
Language:English
Published: Elsevier 2024-12-01
Series:Food Chemistry: X
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Online Access:http://www.sciencedirect.com/science/article/pii/S2590157524007272
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author Yuqi Wang
Yiwen Mei
Rongsheng Du
Shulin Zhang
Qiuyu Wang
Xiaofang Dao
Na Li
Lina Wang
Linlin Wang
Honghong He
author_facet Yuqi Wang
Yiwen Mei
Rongsheng Du
Shulin Zhang
Qiuyu Wang
Xiaofang Dao
Na Li
Lina Wang
Linlin Wang
Honghong He
author_sort Yuqi Wang
collection DOAJ
description 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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issn 2590-1575
language English
publishDate 2024-12-01
publisher Elsevier
record_format Article
series Food Chemistry: X
spelling doaj-art-cf45a6a5451543d9ad3f4c85328a81082025-08-20T02:49:56ZengElsevierFood Chemistry: X2590-15752024-12-012410183910.1016/j.fochx.2024.101839Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insightsYuqi Wang0Yiwen Mei1Rongsheng Du2Shulin Zhang3Qiuyu Wang4Xiaofang Dao5Na Li6Lina Wang7Linlin Wang8Honghong He9College of Food Science and Technology, Southwest Minzu University, Chengdu, Sichuan 610041, PR ChinaCollege of Food Science and Technology, Southwest Minzu University, Chengdu, Sichuan 610041, PR ChinaSichuan Institute of Musk Deer Breeding, Chengdu, Sichuan 610016, PR ChinaCollege of Food Science and Technology, Southwest Minzu University, Chengdu, Sichuan 610041, PR ChinaCollege of Food Science and Technology, Southwest Minzu University, Chengdu, Sichuan 610041, PR ChinaCollege of Food Science and Technology, Southwest Minzu University, Chengdu, Sichuan 610041, PR ChinaCollege of Veterinary Medicine, Xinjiang Agricultural University, Urumqi City, Xinjiang 830000, ChinaCollege of Food Science and Technology, Southwest Minzu University, Chengdu, Sichuan 610041, PR ChinaCollege of Food Science and Technology, Southwest Minzu University, Chengdu, Sichuan 610041, PR China; Corresponding authors.College of Animal Science and Veterinary Sciences, Southwest Minzu University, Chengdu, Sichuan 610041, PR China; Corresponding authors.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.http://www.sciencedirect.com/science/article/pii/S2590157524007272ArginineMeat additivesAntioxidantMyofibrillar proteinGelationYak meat
spellingShingle Yuqi Wang
Yiwen Mei
Rongsheng Du
Shulin Zhang
Qiuyu Wang
Xiaofang Dao
Na Li
Lina Wang
Linlin Wang
Honghong He
Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insights
Food Chemistry: X
Arginine
Meat additives
Antioxidant
Myofibrillar protein
Gelation
Yak meat
title Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insights
title_full Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insights
title_fullStr Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insights
title_full_unstemmed Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insights
title_short Arginine as a regulator of antioxidant and gel formation in yak Myofibrillar proteins: Efficacy and mechanistic insights
title_sort arginine as a regulator of antioxidant and gel formation in yak myofibrillar proteins efficacy and mechanistic insights
topic Arginine
Meat additives
Antioxidant
Myofibrillar protein
Gelation
Yak meat
url http://www.sciencedirect.com/science/article/pii/S2590157524007272
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