Oxidative Modification, Structural Conformation, and Gel Properties of Pork Paste Protein Mediated by Oxygen Concentration in Modified Atmosphere Packaging

The objective of this study was to investigate the effect of pork oxidation through modified atmosphere packaging (MAP) on gel characteristics of myofibrillar proteins (MP) during the heat-induced gelation process. The pork <i>longissimus thoracis</i> (LT) was treated by MAP at varying o...

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出版年:Foods
主要な著者: Rui Liu, Wen Guan, Wei Lv, Zhuangli Kang, Qingling Wang, Duxin Jin, Xinxin Zhao, Qingfeng Ge, Mangang Wu, Hai Yu
フォーマット: 論文
言語:英語
出版事項: MDPI AG 2024-01-01
主題:
オンライン・アクセス:https://www.mdpi.com/2304-8158/13/3/391
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author Rui Liu
Wen Guan
Wei Lv
Zhuangli Kang
Qingling Wang
Duxin Jin
Xinxin Zhao
Qingfeng Ge
Mangang Wu
Hai Yu
author_facet Rui Liu
Wen Guan
Wei Lv
Zhuangli Kang
Qingling Wang
Duxin Jin
Xinxin Zhao
Qingfeng Ge
Mangang Wu
Hai Yu
author_sort Rui Liu
collection DOAJ
container_title Foods
description The objective of this study was to investigate the effect of pork oxidation through modified atmosphere packaging (MAP) on gel characteristics of myofibrillar proteins (MP) during the heat-induced gelation process. The pork <i>longissimus thoracis</i> (LT) was treated by MAP at varying oxygen concentrations (0, 20, 40, 60, and 80% O<sub>2</sub>) with a 5-day storage at 4 °C for the detection of MP oxidation and gel properties. The findings showed the rise of O<sub>2</sub> concentration resulted in a significant increase of carbonyl content, disulfide bond, and particle size, and a decrease of sulfhydryl content and MP solubility (<i>p</i> < 0.05). The gel textural properties and water retention ability were significantly improved in MAP treatments of 0–60% O<sub>2</sub> (<i>p</i> < 0.05), but deteriorated at 80% O<sub>2</sub> level. As the concentration of O<sub>2</sub> increased, there was a marked decrease in the α-helix content within the gel, accompanied by a simultaneous increase in β-sheet content (<i>p</i> < 0.05). Additionally, a judicious oxidation treatment (60% O<sub>2</sub> in MAP) proved beneficial for crafting dense and uniform gel networks. Our data suggest that the oxidation treatment of pork mediated by O<sub>2</sub> concentration in MAP is capable of reinforcing protein hydrophobic interaction and disulfide bond formation, thus contributing to the construction of superior gel structures and properties.
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spelling doaj-art-9ea33fcfe06e438abeefa8bb725cf6642025-08-20T00:46:43ZengMDPI AGFoods2304-81582024-01-0113339110.3390/foods13030391Oxidative Modification, Structural Conformation, and Gel Properties of Pork Paste Protein Mediated by Oxygen Concentration in Modified Atmosphere PackagingRui Liu0Wen Guan1Wei Lv2Zhuangli Kang3Qingling Wang4Duxin Jin5Xinxin Zhao6Qingfeng Ge7Mangang Wu8Hai Yu9College of Food Science and Engineering, Yangzhou University, Yangzhou 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, ChinaSchool of Tourism and Cuisine, Engineering Technology Research Center of Yangzhou Prepared Cuisine, Yangzhou University, Yangzhou 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou 225127, ChinaThe objective of this study was to investigate the effect of pork oxidation through modified atmosphere packaging (MAP) on gel characteristics of myofibrillar proteins (MP) during the heat-induced gelation process. The pork <i>longissimus thoracis</i> (LT) was treated by MAP at varying oxygen concentrations (0, 20, 40, 60, and 80% O<sub>2</sub>) with a 5-day storage at 4 °C for the detection of MP oxidation and gel properties. The findings showed the rise of O<sub>2</sub> concentration resulted in a significant increase of carbonyl content, disulfide bond, and particle size, and a decrease of sulfhydryl content and MP solubility (<i>p</i> < 0.05). The gel textural properties and water retention ability were significantly improved in MAP treatments of 0–60% O<sub>2</sub> (<i>p</i> < 0.05), but deteriorated at 80% O<sub>2</sub> level. As the concentration of O<sub>2</sub> increased, there was a marked decrease in the α-helix content within the gel, accompanied by a simultaneous increase in β-sheet content (<i>p</i> < 0.05). Additionally, a judicious oxidation treatment (60% O<sub>2</sub> in MAP) proved beneficial for crafting dense and uniform gel networks. Our data suggest that the oxidation treatment of pork mediated by O<sub>2</sub> concentration in MAP is capable of reinforcing protein hydrophobic interaction and disulfide bond formation, thus contributing to the construction of superior gel structures and properties.https://www.mdpi.com/2304-8158/13/3/391pork pastemodified atmosphere packagingprotein oxidationtextural propertieswater holding capacity
spellingShingle Rui Liu
Wen Guan
Wei Lv
Zhuangli Kang
Qingling Wang
Duxin Jin
Xinxin Zhao
Qingfeng Ge
Mangang Wu
Hai Yu
Oxidative Modification, Structural Conformation, and Gel Properties of Pork Paste Protein Mediated by Oxygen Concentration in Modified Atmosphere Packaging
pork paste
modified atmosphere packaging
protein oxidation
textural properties
water holding capacity
title Oxidative Modification, Structural Conformation, and Gel Properties of Pork Paste Protein Mediated by Oxygen Concentration in Modified Atmosphere Packaging
title_full Oxidative Modification, Structural Conformation, and Gel Properties of Pork Paste Protein Mediated by Oxygen Concentration in Modified Atmosphere Packaging
title_fullStr Oxidative Modification, Structural Conformation, and Gel Properties of Pork Paste Protein Mediated by Oxygen Concentration in Modified Atmosphere Packaging
title_full_unstemmed Oxidative Modification, Structural Conformation, and Gel Properties of Pork Paste Protein Mediated by Oxygen Concentration in Modified Atmosphere Packaging
title_short Oxidative Modification, Structural Conformation, and Gel Properties of Pork Paste Protein Mediated by Oxygen Concentration in Modified Atmosphere Packaging
title_sort oxidative modification structural conformation and gel properties of pork paste protein mediated by oxygen concentration in modified atmosphere packaging
topic pork paste
modified atmosphere packaging
protein oxidation
textural properties
water holding capacity
url https://www.mdpi.com/2304-8158/13/3/391
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