Huijuan Yang , Zhizhao Chen , Haifeng Wang , Danping Jin , Xiaoqi Wang , Fan Wang , Xuejiang Cen , Jinsong Liu , Qing Shen
{"title":"揭示冷冻处理提高肌纤维蛋白溶解度的流变特性基础","authors":"Huijuan Yang , Zhizhao Chen , Haifeng Wang , Danping Jin , Xiaoqi Wang , Fan Wang , Xuejiang Cen , Jinsong Liu , Qing Shen","doi":"10.1016/j.crfs.2023.100651","DOIUrl":null,"url":null,"abstract":"<div><p>Myofibrillar proteins (MPs) are an important nutritional supplement and have great significance in sports training and rehabilitation therapy. Currently, MPs preservation is still disputed since they are vulnerable to degradation, polymerization, and denaturation. Freeze-drying is an emerging technology for protein preservation, its effects on the functionality of MPs from different sources have not yet been thoroughly studied. This study aims to evaluate the performance differences of freeze-drying in maintaining the functional characteristics of MPs from fish and mammalian sources, providing valuable insights for the processing and preservation of MPs, and providing nutritional support for nursing and rehabilitation. The results showed that freeze-drying was an efficient method for protein preservation, and the effects of freeze-drying on both fish and mammalian sources MPs were significant (<em>p</em> < 0.05) consistent. Specifically, whether before and after freeze-drying, the solubility of fish MPs (FMPs) was significant (<em>p</em> < 0.05) lower than that of mammalian MPs, while the foaming and emulsifying properties were significant (<em>p</em> < 0.05) higher than those of beef and sheep MPs (BMPs and SMPs, respectively). Furthermore, the most efficient protein concentration for freeze-drying was 10 mg/mL, and with this concentration, the gel strengths of BMPs and SMPs showed an insignificant difference (<em>p</em> > 0.05) after freeze-drying.</p></div>","PeriodicalId":10939,"journal":{"name":"Current Research in Food Science","volume":"8 ","pages":"Article 100651"},"PeriodicalIF":6.2000,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2665927123002198/pdfft?md5=11965e9e8a655f6583513c0a30adb9bf&pid=1-s2.0-S2665927123002198-main.pdf","citationCount":"0","resultStr":"{\"title\":\"Uncovering the rheological properties basis for freeze drying treatment-induced improvement in the solubility of myofibrillar proteins\",\"authors\":\"Huijuan Yang , Zhizhao Chen , Haifeng Wang , Danping Jin , Xiaoqi Wang , Fan Wang , Xuejiang Cen , Jinsong Liu , Qing Shen\",\"doi\":\"10.1016/j.crfs.2023.100651\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Myofibrillar proteins (MPs) are an important nutritional supplement and have great significance in sports training and rehabilitation therapy. Currently, MPs preservation is still disputed since they are vulnerable to degradation, polymerization, and denaturation. Freeze-drying is an emerging technology for protein preservation, its effects on the functionality of MPs from different sources have not yet been thoroughly studied. This study aims to evaluate the performance differences of freeze-drying in maintaining the functional characteristics of MPs from fish and mammalian sources, providing valuable insights for the processing and preservation of MPs, and providing nutritional support for nursing and rehabilitation. The results showed that freeze-drying was an efficient method for protein preservation, and the effects of freeze-drying on both fish and mammalian sources MPs were significant (<em>p</em> < 0.05) consistent. Specifically, whether before and after freeze-drying, the solubility of fish MPs (FMPs) was significant (<em>p</em> < 0.05) lower than that of mammalian MPs, while the foaming and emulsifying properties were significant (<em>p</em> < 0.05) higher than those of beef and sheep MPs (BMPs and SMPs, respectively). Furthermore, the most efficient protein concentration for freeze-drying was 10 mg/mL, and with this concentration, the gel strengths of BMPs and SMPs showed an insignificant difference (<em>p</em> > 0.05) after freeze-drying.</p></div>\",\"PeriodicalId\":10939,\"journal\":{\"name\":\"Current Research in Food Science\",\"volume\":\"8 \",\"pages\":\"Article 100651\"},\"PeriodicalIF\":6.2000,\"publicationDate\":\"2024-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.sciencedirect.com/science/article/pii/S2665927123002198/pdfft?md5=11965e9e8a655f6583513c0a30adb9bf&pid=1-s2.0-S2665927123002198-main.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Research in Food Science\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2665927123002198\",\"RegionNum\":2,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Research in Food Science","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2665927123002198","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Uncovering the rheological properties basis for freeze drying treatment-induced improvement in the solubility of myofibrillar proteins
Myofibrillar proteins (MPs) are an important nutritional supplement and have great significance in sports training and rehabilitation therapy. Currently, MPs preservation is still disputed since they are vulnerable to degradation, polymerization, and denaturation. Freeze-drying is an emerging technology for protein preservation, its effects on the functionality of MPs from different sources have not yet been thoroughly studied. This study aims to evaluate the performance differences of freeze-drying in maintaining the functional characteristics of MPs from fish and mammalian sources, providing valuable insights for the processing and preservation of MPs, and providing nutritional support for nursing and rehabilitation. The results showed that freeze-drying was an efficient method for protein preservation, and the effects of freeze-drying on both fish and mammalian sources MPs were significant (p < 0.05) consistent. Specifically, whether before and after freeze-drying, the solubility of fish MPs (FMPs) was significant (p < 0.05) lower than that of mammalian MPs, while the foaming and emulsifying properties were significant (p < 0.05) higher than those of beef and sheep MPs (BMPs and SMPs, respectively). Furthermore, the most efficient protein concentration for freeze-drying was 10 mg/mL, and with this concentration, the gel strengths of BMPs and SMPs showed an insignificant difference (p > 0.05) after freeze-drying.
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.
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