{"title":"蛋白谷氨酰胺酶对酪蛋白脱氨的优化及其对结构和功能特性的影响","authors":"Deming Jiang, Ouyang Wei, Lingling Huang, Jinjin Niu, Zheng Zhang, Congli Jin, Siyi Gu, Mengmeng Liu, Zhongyi Chang, Yanning Niu, Chunjing Zou, Jing Huang, Caifeng Jia, Lihua Tang, Hongliang Gao","doi":"10.1007/s11947-024-03480-3","DOIUrl":null,"url":null,"abstract":"<p>Casein is a commonly used protein in the food industry, with its related products such as beverages and desserts. However, the further application of casein is limited by its solubility and stability. This study aimed to improve the functional of casein through protein-glutaminase (PG) deamination. The deamination of casein using PG was optimized through central composite design experiments, and its impact on the structure, solubility, and stability of casein was investigated. The results demonstrate that the optimal conditions for PG deamidation were determined at pH 6.0, E/S 15 U/g, and a temperature of 45 °C. The deamidation process alters the secondary structure of casein, resulting in a decrease in α-helix structure and an increase in β-sheet structure. The modification of casein improved emulsifying activity at pH 8.0 and 10.0, respectively, while significantly enhancing the solubility from 5.0 to 6.0. Furthermore, the deamidation of casein caused an increase in zeta potential and a decrease in particle size, resulting in improved stability of the protein solution due to reduced particle aggregation. The 3% deamidated casein-based beverage with carrageenan exhibited reduced precipitation rates compared to the control after sterilization at 121 °C for 15 min. In summary, PG deamidation offers a promising method for the modification and enhancement of the functional properties, including solubility, stability, and emulsifying activity of casein, thereby expanding its use of casein in the food industry.</p>","PeriodicalId":562,"journal":{"name":"Food and Bioprocess Technology","volume":null,"pages":null},"PeriodicalIF":5.3000,"publicationDate":"2024-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Optimization of Deamidation of Casein by Protein-Glutaminase and Its Effect on Structural and Functional Properties\",\"authors\":\"Deming Jiang, Ouyang Wei, Lingling Huang, Jinjin Niu, Zheng Zhang, Congli Jin, Siyi Gu, Mengmeng Liu, Zhongyi Chang, Yanning Niu, Chunjing Zou, Jing Huang, Caifeng Jia, Lihua Tang, Hongliang Gao\",\"doi\":\"10.1007/s11947-024-03480-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>Casein is a commonly used protein in the food industry, with its related products such as beverages and desserts. However, the further application of casein is limited by its solubility and stability. This study aimed to improve the functional of casein through protein-glutaminase (PG) deamination. The deamination of casein using PG was optimized through central composite design experiments, and its impact on the structure, solubility, and stability of casein was investigated. The results demonstrate that the optimal conditions for PG deamidation were determined at pH 6.0, E/S 15 U/g, and a temperature of 45 °C. The deamidation process alters the secondary structure of casein, resulting in a decrease in α-helix structure and an increase in β-sheet structure. The modification of casein improved emulsifying activity at pH 8.0 and 10.0, respectively, while significantly enhancing the solubility from 5.0 to 6.0. Furthermore, the deamidation of casein caused an increase in zeta potential and a decrease in particle size, resulting in improved stability of the protein solution due to reduced particle aggregation. The 3% deamidated casein-based beverage with carrageenan exhibited reduced precipitation rates compared to the control after sterilization at 121 °C for 15 min. In summary, PG deamidation offers a promising method for the modification and enhancement of the functional properties, including solubility, stability, and emulsifying activity of casein, thereby expanding its use of casein in the food industry.</p>\",\"PeriodicalId\":562,\"journal\":{\"name\":\"Food and Bioprocess Technology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":5.3000,\"publicationDate\":\"2024-06-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food and Bioprocess Technology\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1007/s11947-024-03480-3\",\"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":"Food and Bioprocess Technology","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1007/s11947-024-03480-3","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}
Optimization of Deamidation of Casein by Protein-Glutaminase and Its Effect on Structural and Functional Properties
Casein is a commonly used protein in the food industry, with its related products such as beverages and desserts. However, the further application of casein is limited by its solubility and stability. This study aimed to improve the functional of casein through protein-glutaminase (PG) deamination. The deamination of casein using PG was optimized through central composite design experiments, and its impact on the structure, solubility, and stability of casein was investigated. The results demonstrate that the optimal conditions for PG deamidation were determined at pH 6.0, E/S 15 U/g, and a temperature of 45 °C. The deamidation process alters the secondary structure of casein, resulting in a decrease in α-helix structure and an increase in β-sheet structure. The modification of casein improved emulsifying activity at pH 8.0 and 10.0, respectively, while significantly enhancing the solubility from 5.0 to 6.0. Furthermore, the deamidation of casein caused an increase in zeta potential and a decrease in particle size, resulting in improved stability of the protein solution due to reduced particle aggregation. The 3% deamidated casein-based beverage with carrageenan exhibited reduced precipitation rates compared to the control after sterilization at 121 °C for 15 min. In summary, PG deamidation offers a promising method for the modification and enhancement of the functional properties, including solubility, stability, and emulsifying activity of casein, thereby expanding its use of casein in the food industry.
期刊介绍:
Food and Bioprocess Technology provides an effective and timely platform for cutting-edge high quality original papers in the engineering and science of all types of food processing technologies, from the original food supply source to the consumer’s dinner table. It aims to be a leading international journal for the multidisciplinary agri-food research community.
The journal focuses especially on experimental or theoretical research findings that have the potential for helping the agri-food industry to improve process efficiency, enhance product quality and, extend shelf-life of fresh and processed agri-food products. The editors present critical reviews on new perspectives to established processes, innovative and emerging technologies, and trends and future research in food and bioproducts processing. The journal also publishes short communications for rapidly disseminating preliminary results, letters to the Editor on recent developments and controversy, and book reviews.