Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stress

The effects of eugenol (EG; 0, 5, 20, and 50 mg/g protein) on the structure and gel properties of pork myofibrillar protein (MPs) under a hydroxyl radical-generating system were explored in this study. The results revealed that the addition of a high concentration of EG (50 mg/g protein) markedly re...

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Main Authors: Deyin Pan, Jinming Ma, Jingjing Diao, Jiaqi Li, Hongsheng Chen
Format: Article
Language:English
Published: Elsevier 2023-12-01
Series:Food Chemistry: X
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2590157523003899
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author Deyin Pan
Jinming Ma
Jingjing Diao
Jiaqi Li
Hongsheng Chen
author_facet Deyin Pan
Jinming Ma
Jingjing Diao
Jiaqi Li
Hongsheng Chen
author_sort Deyin Pan
collection DOAJ
description The effects of eugenol (EG; 0, 5, 20, and 50 mg/g protein) on the structure and gel properties of pork myofibrillar protein (MPs) under a hydroxyl radical-generating system were explored in this study. The results revealed that the addition of a high concentration of EG (50 mg/g protein) markedly reduced the carbonyl content and enhanced the fluorescence intensity, surface hydrophobicity, and protected the secondary structure of MPs, compared to oxidized MPs. In addition, the high concentration group noticeably increased the storage modulus (G′), gel strength, and water-holding capacity (WHC), and significantly hindered the oxidation-induced transformation of immobilized water of the MPs gel to free water and basically favored the formation of a finer and more homogeneous three-dimensional network structure, This work verified that the adding of EG could effectively improve the gel quality of oxidized MPs and more successfully delay oxidation-induced damage to muscle protein structure.
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spelling doaj.art-2cdc9c3faaca44a1b235180269228cf82023-12-21T07:36:41ZengElsevierFood Chemistry: X2590-15752023-12-0120100946Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stressDeyin Pan0Jinming Ma1Jingjing Diao2Jiaqi Li3Hongsheng Chen4College of Food Science, Heilongjiang Bayi Agricultural University, Daqing, Heilongjiang 163319, China; Heilongjiang Food and Biotechnology Innovation and Research Center (International Cooperation), Daqing, HeilongJiang 163319, ChinaCollege of Food Science, Heilongjiang Bayi Agricultural University, Daqing, Heilongjiang 163319, China; Heilongjiang Food and Biotechnology Innovation and Research Center (International Cooperation), Daqing, HeilongJiang 163319, ChinaCollege of Food Science, Heilongjiang Bayi Agricultural University, Daqing, Heilongjiang 163319, China; Heilongjiang Food and Biotechnology Innovation and Research Center (International Cooperation), Daqing, HeilongJiang 163319, ChinaCollege of Food Science, Heilongjiang Bayi Agricultural University, Daqing, Heilongjiang 163319, China; Heilongjiang Food and Biotechnology Innovation and Research Center (International Cooperation), Daqing, HeilongJiang 163319, ChinaCollege of Food Science, Heilongjiang Bayi Agricultural University, Daqing, Heilongjiang 163319, China; Heilongjiang Food and Biotechnology Innovation and Research Center (International Cooperation), Daqing, HeilongJiang 163319, China; Corresponding author at: College of Food Science, Heilongjiang Bayi Agricultural University, Daqing, Heilongjiang 163319, China.The effects of eugenol (EG; 0, 5, 20, and 50 mg/g protein) on the structure and gel properties of pork myofibrillar protein (MPs) under a hydroxyl radical-generating system were explored in this study. The results revealed that the addition of a high concentration of EG (50 mg/g protein) markedly reduced the carbonyl content and enhanced the fluorescence intensity, surface hydrophobicity, and protected the secondary structure of MPs, compared to oxidized MPs. In addition, the high concentration group noticeably increased the storage modulus (G′), gel strength, and water-holding capacity (WHC), and significantly hindered the oxidation-induced transformation of immobilized water of the MPs gel to free water and basically favored the formation of a finer and more homogeneous three-dimensional network structure, This work verified that the adding of EG could effectively improve the gel quality of oxidized MPs and more successfully delay oxidation-induced damage to muscle protein structure.http://www.sciencedirect.com/science/article/pii/S2590157523003899EugenolProtein oxidationMyofibrillar proteinRheologyWater distribution
spellingShingle Deyin Pan
Jinming Ma
Jingjing Diao
Jiaqi Li
Hongsheng Chen
Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stress
Food Chemistry: X
Eugenol
Protein oxidation
Myofibrillar protein
Rheology
Water distribution
title Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stress
title_full Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stress
title_fullStr Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stress
title_full_unstemmed Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stress
title_short Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stress
title_sort effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical induced oxidative stress
topic Eugenol
Protein oxidation
Myofibrillar protein
Rheology
Water distribution
url http://www.sciencedirect.com/science/article/pii/S2590157523003899
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