Effect of oxidation on the process of thermal gelation of chicken breast myofibrillar protein

•Effect of oxidation on thermal gel formation process of myofibrillar protein was explored.•Degree of protein oxidation had a significant effect on thermal gelation formation.•Oxidation reduces G’ during thermal gel formation process of myofibrillar protein.•Oxidation affected water holding capacity...

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Veröffentlicht in:Food chemistry 2022-08, Vol.384, p.132368-132368, Article 132368
Hauptverfasser: Xia, Tianlan, Xu, Yujuan, Zhang, Yulong, Xu, Lina, Kong, Yawen, Song, Shangxin, Huang, Mingyuan, Bai, Yun, Luan, Yi, Han, Minyi, Zhou, Guanghong, Xu, Xinglian
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container_start_page 132368
container_title Food chemistry
container_volume 384
creator Xia, Tianlan
Xu, Yujuan
Zhang, Yulong
Xu, Lina
Kong, Yawen
Song, Shangxin
Huang, Mingyuan
Bai, Yun
Luan, Yi
Han, Minyi
Zhou, Guanghong
Xu, Xinglian
description •Effect of oxidation on thermal gel formation process of myofibrillar protein was explored.•Degree of protein oxidation had a significant effect on thermal gelation formation.•Oxidation reduces G’ during thermal gel formation process of myofibrillar protein.•Oxidation affected water holding capacity by changing immobile and free water amounts. In this study, the effect of protein oxidation on the thermal gelation of chicken breast myofibrillar proteins (MPs) was investigated. MP samples treated with different degrees of oxidation were heated (1.5 °C/min) to different end-point temperatures to simulate the thermal gelation process. The results showed that the water-holding capacity (WHC) significantly decreased with increasing temperature, and higher oxidation degree resulted in worse WHC of heat-induced gel. Compared with high degrees of oxidation, low degrees of MP oxidation reduced the migration of immobile water, inhibited its release as free water, enhanced WHC and favored the formation of β-sheet and β-turn structures. Therefore, low oxidation promoted the formation of β-sheet and β-turn structures to form a better gel microstructure with less formation of free water on the thermal gelation and therefore increased the WHC. High oxidation was just the opposite, and high temperature aggravated this negative effect.
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In this study, the effect of protein oxidation on the thermal gelation of chicken breast myofibrillar proteins (MPs) was investigated. MP samples treated with different degrees of oxidation were heated (1.5 °C/min) to different end-point temperatures to simulate the thermal gelation process. The results showed that the water-holding capacity (WHC) significantly decreased with increasing temperature, and higher oxidation degree resulted in worse WHC of heat-induced gel. Compared with high degrees of oxidation, low degrees of MP oxidation reduced the migration of immobile water, inhibited its release as free water, enhanced WHC and favored the formation of β-sheet and β-turn structures. Therefore, low oxidation promoted the formation of β-sheet and β-turn structures to form a better gel microstructure with less formation of free water on the thermal gelation and therefore increased the WHC. 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In this study, the effect of protein oxidation on the thermal gelation of chicken breast myofibrillar proteins (MPs) was investigated. MP samples treated with different degrees of oxidation were heated (1.5 °C/min) to different end-point temperatures to simulate the thermal gelation process. The results showed that the water-holding capacity (WHC) significantly decreased with increasing temperature, and higher oxidation degree resulted in worse WHC of heat-induced gel. Compared with high degrees of oxidation, low degrees of MP oxidation reduced the migration of immobile water, inhibited its release as free water, enhanced WHC and favored the formation of β-sheet and β-turn structures. Therefore, low oxidation promoted the formation of β-sheet and β-turn structures to form a better gel microstructure with less formation of free water on the thermal gelation and therefore increased the WHC. 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In this study, the effect of protein oxidation on the thermal gelation of chicken breast myofibrillar proteins (MPs) was investigated. MP samples treated with different degrees of oxidation were heated (1.5 °C/min) to different end-point temperatures to simulate the thermal gelation process. The results showed that the water-holding capacity (WHC) significantly decreased with increasing temperature, and higher oxidation degree resulted in worse WHC of heat-induced gel. Compared with high degrees of oxidation, low degrees of MP oxidation reduced the migration of immobile water, inhibited its release as free water, enhanced WHC and favored the formation of β-sheet and β-turn structures. Therefore, low oxidation promoted the formation of β-sheet and β-turn structures to form a better gel microstructure with less formation of free water on the thermal gelation and therefore increased the WHC. 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subjects Animals
Chickens - metabolism
Gels - chemistry
Muscle Proteins - chemistry
Myofibrillar proteins
Myofibrils - chemistry
Oxidation
Oxidation-Reduction
Thermal gel formation
Water - chemistry
Water-holding capacity
title Effect of oxidation on the process of thermal gelation of chicken breast myofibrillar protein
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