Wan-ling Lin , Hui Huang , Ya-qun Liu , Han-xu Liu , Ya Wei , Yong-qiang Zhao , Yue-qi Wang , Yan-yan Wu , Sheng-jun Chen , Lai-hao Li
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We identified a total of 1085 proteins, 516 of which were shared across all the temperature treatments, indicating a core proteome responsible for CGC textural properties. Differential expression analysis revealed temperature-dependent changes, with significant alterations observed at 90 °C, suggesting denaturation or aggregation of proteins at higher temperatures. Functional enrichment analysis indicated that proteins involved in amino acid metabolism, glutathione metabolism, and nucleotide metabolism were particularly affected by heat. Textural analysis correlated these proteomic changes with alterations in CGC quality attributes, pinpointing 70 °C as the optimum temperature for maintaining the desired texture. A strong positive correlation between specific upregulated proteins was identified, such as the tubulin alpha chain and collagen alpha-1(IV) chain, and the improved textural properties of CGC during thermal processing, suggesting their potential as the potential biomarkers. This study offers a comprehensive proteomic view of the thermal stability and functionality of CGC proteins, delivering invaluable insights for both the culinary processing and scientific management of CGC. Our findings not only deepen the understanding of the molecular mechanisms underpinning the textural alterations in CGC during thermal processing but also furnish practical insights for the aquaculture industry. 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This study employed 4D label-free proteomics and data mining techniques to investigate the proteomic changes in CGC muscle tissue induced by various heating temperatures. CGC samples were subjected to a series of heat treatments at increasing temperatures from 20 °C to 90 °C. Proteins were extracted, digested, and analysed using high-resolution mass spectrometry. The proteomic data were then subjected to extensive bioinformatics analysis, including GO and KEGG pathway enrichment. We identified a total of 1085 proteins, 516 of which were shared across all the temperature treatments, indicating a core proteome responsible for CGC textural properties. Differential expression analysis revealed temperature-dependent changes, with significant alterations observed at 90 °C, suggesting denaturation or aggregation of proteins at higher temperatures. Functional enrichment analysis indicated that proteins involved in amino acid metabolism, glutathione metabolism, and nucleotide metabolism were particularly affected by heat. Textural analysis correlated these proteomic changes with alterations in CGC quality attributes, pinpointing 70 °C as the optimum temperature for maintaining the desired texture. A strong positive correlation between specific upregulated proteins was identified, such as the tubulin alpha chain and collagen alpha-1(IV) chain, and the improved textural properties of CGC during thermal processing, suggesting their potential as the potential biomarkers. This study offers a comprehensive proteomic view of the thermal stability and functionality of CGC proteins, delivering invaluable insights for both the culinary processing and scientific management of CGC. 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引用次数: 0
摘要
脆草鱼(CGC;Ctenopharyngodon idellus C. et V.)以其独特的口感和风味而闻名,是一种烹饪美食,其品质受热加工的影响很大。本研究采用 4D 无标记蛋白质组学和数据挖掘技术,研究了不同加热温度下 CGC 肌肉组织蛋白质组的变化。CGC 样品在 20 °C 至 90 °C 的温度范围内进行了一系列热处理。对蛋白质进行提取、消化,并使用高分辨率质谱进行分析。然后对蛋白质组数据进行广泛的生物信息学分析,包括 GO 和 KEGG 通路富集。我们共鉴定出 1085 个蛋白质,其中 516 个在所有温度处理中共享,这表明有一个核心蛋白质组负责 CGC 的纹理特性。差异表达分析表明,蛋白质的变化与温度有关,在 90 ℃ 时发生了显著变化,这表明蛋白质在较高温度下发生了变性或聚集。功能富集分析表明,参与氨基酸代谢、谷胱甘肽代谢和核苷酸代谢的蛋白质受热的影响特别大。质构分析将这些蛋白质组变化与 CGC 质量属性的改变联系起来,确定 70 °C 为保持理想质构的最佳温度。在热加工过程中,特定的上调蛋白质(如微管蛋白α链和胶原蛋白α-1(IV)链)与CGC质构特性的改善之间存在很强的正相关性,这表明它们有可能成为潜在的生物标记物。这项研究从蛋白质组学的角度全面审视了丙种球蛋白的热稳定性和功能性,为丙种球蛋白的烹饪加工和科学管理提供了宝贵的见解。我们的研究结果不仅加深了人们对热加工过程中CGC纹理变化的分子机制的理解,还为水产养殖业提供了实用的见解。这些见解可用于优化烹饪技术,从而提高丙种球蛋白产品的质量和对消费者的吸引力。
Integrated 4D label-free proteomics and data mining to elucidate the effects of thermal processing on crisp grass carp protein profiles
The crisp grass carp (CGC; Ctenopharyngodon idellus C. et V.), known for its unique texture and flavour, is a culinary delicacy whose quality is significantly influenced by thermal processing. This study employed 4D label-free proteomics and data mining techniques to investigate the proteomic changes in CGC muscle tissue induced by various heating temperatures. CGC samples were subjected to a series of heat treatments at increasing temperatures from 20 °C to 90 °C. Proteins were extracted, digested, and analysed using high-resolution mass spectrometry. The proteomic data were then subjected to extensive bioinformatics analysis, including GO and KEGG pathway enrichment. We identified a total of 1085 proteins, 516 of which were shared across all the temperature treatments, indicating a core proteome responsible for CGC textural properties. Differential expression analysis revealed temperature-dependent changes, with significant alterations observed at 90 °C, suggesting denaturation or aggregation of proteins at higher temperatures. Functional enrichment analysis indicated that proteins involved in amino acid metabolism, glutathione metabolism, and nucleotide metabolism were particularly affected by heat. Textural analysis correlated these proteomic changes with alterations in CGC quality attributes, pinpointing 70 °C as the optimum temperature for maintaining the desired texture. A strong positive correlation between specific upregulated proteins was identified, such as the tubulin alpha chain and collagen alpha-1(IV) chain, and the improved textural properties of CGC during thermal processing, suggesting their potential as the potential biomarkers. This study offers a comprehensive proteomic view of the thermal stability and functionality of CGC proteins, delivering invaluable insights for both the culinary processing and scientific management of CGC. Our findings not only deepen the understanding of the molecular mechanisms underpinning the textural alterations in CGC during thermal processing but also furnish practical insights for the aquaculture industry. These insights could be leveraged to optimize cooking techniques, thereby enhancing the quality and consumer appeal of CGC products.
期刊介绍:
Current Research in Food Science is an international peer-reviewed journal dedicated to advancing the breadth of knowledge in the field of food science. It serves as a platform for publishing original research articles and short communications that encompass a wide array of topics, including food chemistry, physics, microbiology, nutrition, nutraceuticals, process and package engineering, materials science, food sustainability, and food security. By covering these diverse areas, the journal aims to provide a comprehensive source of the latest scientific findings and technological advancements that are shaping the future of the food industry. The journal's scope is designed to address the multidisciplinary nature of food science, reflecting its commitment to promoting innovation and ensuring the safety and quality of the food supply.