Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione

The effects of inulin (1.5%), glutathione (GSH, 0.05%), and their combination (1.5% inulin + 0.05% GSH) on the conformational structure and gel performance of pork myofibrillar protein (MP) under oxidation condition were examined. The addition of GSH significantly prevented oxidation-induced carbony...

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Main Authors: Wenhui Ma, Qi Yang, Xin Fan, Xianqi Yao, Jiwei Kuang, Cong Min, Yungang Cao, Junrong Huang
Format: Article
Language:English
Published: Elsevier 2022-06-01
Series:Food Chemistry: X
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S259015752200116X
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author Wenhui Ma
Qi Yang
Xin Fan
Xianqi Yao
Jiwei Kuang
Cong Min
Yungang Cao
Junrong Huang
author_facet Wenhui Ma
Qi Yang
Xin Fan
Xianqi Yao
Jiwei Kuang
Cong Min
Yungang Cao
Junrong Huang
author_sort Wenhui Ma
collection DOAJ
description The effects of inulin (1.5%), glutathione (GSH, 0.05%), and their combination (1.5% inulin + 0.05% GSH) on the conformational structure and gel performance of pork myofibrillar protein (MP) under oxidation condition were examined. The addition of GSH significantly prevented oxidation-induced carbonylation, reduction of α-helix content, and protein aggregation. As a result, treatment with GSH significantly reduced the particle size of oxidized MP by 35%, increased the solubility by 17.3%, and improved the gelling properties. The presence of inulin also obviously enhanced the gelling behavior of MP under oxidation condition, although it could hardly inhibit the modification of MP structure caused by oxidation. Treatment with inulin + GSH exhibited the highest cooking yield (84.2%) and the best textural characteristics, with a denser and more uniform network structure comprising evenly distributed small pores. The findings of this study provide a useful method for processing meat protein gel products with better oxidative stability and textural properties.
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spelling doaj.art-1047b1c01931450ab72776e57a196fb62022-12-22T03:31:12ZengElsevierFood Chemistry: X2590-15752022-06-0114100318Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathioneWenhui Ma0Qi Yang1Xin Fan2Xianqi Yao3Jiwei Kuang4Cong Min5Yungang Cao6Junrong Huang7School of Food and Biological Engineering, and Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi’an 710021, ChinaSchool of Food and Biological Engineering, and Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi’an 710021, ChinaSchool of Food and Biological Engineering, and Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi’an 710021, ChinaLinyi Jinluo Win Ray Food Co., Ltd., Linyi 276036, ChinaSchool of Food and Biological Engineering, and Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi’an 710021, ChinaSchool of Food and Biological Engineering, and Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi’an 710021, ChinaSchool of Food and Biological Engineering, and Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi’an 710021, China; Corresponding authors.School of Food and Biological Engineering, and Natural Food Macromolecule Research Center, Shaanxi University of Science and Technology, Xi’an 710021, China; Corresponding authors.The effects of inulin (1.5%), glutathione (GSH, 0.05%), and their combination (1.5% inulin + 0.05% GSH) on the conformational structure and gel performance of pork myofibrillar protein (MP) under oxidation condition were examined. The addition of GSH significantly prevented oxidation-induced carbonylation, reduction of α-helix content, and protein aggregation. As a result, treatment with GSH significantly reduced the particle size of oxidized MP by 35%, increased the solubility by 17.3%, and improved the gelling properties. The presence of inulin also obviously enhanced the gelling behavior of MP under oxidation condition, although it could hardly inhibit the modification of MP structure caused by oxidation. Treatment with inulin + GSH exhibited the highest cooking yield (84.2%) and the best textural characteristics, with a denser and more uniform network structure comprising evenly distributed small pores. The findings of this study provide a useful method for processing meat protein gel products with better oxidative stability and textural properties.http://www.sciencedirect.com/science/article/pii/S259015752200116XMyofibrillar proteinOxidationInulinGlutathioneGelation
spellingShingle Wenhui Ma
Qi Yang
Xin Fan
Xianqi Yao
Jiwei Kuang
Cong Min
Yungang Cao
Junrong Huang
Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione
Food Chemistry: X
Myofibrillar protein
Oxidation
Inulin
Glutathione
Gelation
title Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione
title_full Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione
title_fullStr Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione
title_full_unstemmed Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione
title_short Modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione
title_sort modification of myofibrillar protein gelation under oxidative stress using combined inulin and glutathione
topic Myofibrillar protein
Oxidation
Inulin
Glutathione
Gelation
url http://www.sciencedirect.com/science/article/pii/S259015752200116X
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