{"title":"利用微生物蛋白酶从蛋白质废物中制备具有乳化特性的水解物","authors":"D. Padmapriya, C. Shanthi","doi":"10.1007/s10068-023-01490-z","DOIUrl":null,"url":null,"abstract":"<div><p>Plant-based protein hydrolysates have found applications in food industry for emulsification, foaming, and increasing shelf life of food products. The objective of this study is to isolate protease-secreting bacteria hydrolyzing protein waste, and subjecting the resultant hydrolysates for the characterization for application in the food industry. Peanut cake hydrolysates were prepared using proteases from two microorganisms selected for the purpose, viz., <i>Aneurinibacillus migulanus,</i> VITPM11 and <i>Aneurinibacillus aneurinilyticus,</i> VITPS07. The cleavage specificity of the proteases from VITPM11 and VITPS07 were found to be like plasmin and elastase respectively. The cleaving sites of proteases for peanut proteins were predicted using expasy tool. The protease of VITPM11 had maximal activity of 325.8 ± 0.1 U/mL in peanut-cake media. The degree of hydrolysis (32.03 ± 0.89%), solubility (88.5 ± 1.18%), emulsion stability index (89.76 ± 2.80) and foaming stability (68.67 ± 1.53%) properties of VITPM11 protease correlated well with results from bioinformatic studies.</p></div>","PeriodicalId":566,"journal":{"name":"Food Science and Biotechnology","volume":"33 8","pages":"1847 - 1857"},"PeriodicalIF":2.4000,"publicationDate":"2024-02-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Hydrolysates with emulsifying properties prepared from protein wastes using microbial protease\",\"authors\":\"D. Padmapriya, C. Shanthi\",\"doi\":\"10.1007/s10068-023-01490-z\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Plant-based protein hydrolysates have found applications in food industry for emulsification, foaming, and increasing shelf life of food products. The objective of this study is to isolate protease-secreting bacteria hydrolyzing protein waste, and subjecting the resultant hydrolysates for the characterization for application in the food industry. Peanut cake hydrolysates were prepared using proteases from two microorganisms selected for the purpose, viz., <i>Aneurinibacillus migulanus,</i> VITPM11 and <i>Aneurinibacillus aneurinilyticus,</i> VITPS07. The cleavage specificity of the proteases from VITPM11 and VITPS07 were found to be like plasmin and elastase respectively. The cleaving sites of proteases for peanut proteins were predicted using expasy tool. The protease of VITPM11 had maximal activity of 325.8 ± 0.1 U/mL in peanut-cake media. The degree of hydrolysis (32.03 ± 0.89%), solubility (88.5 ± 1.18%), emulsion stability index (89.76 ± 2.80) and foaming stability (68.67 ± 1.53%) properties of VITPM11 protease correlated well with results from bioinformatic studies.</p></div>\",\"PeriodicalId\":566,\"journal\":{\"name\":\"Food Science and Biotechnology\",\"volume\":\"33 8\",\"pages\":\"1847 - 1857\"},\"PeriodicalIF\":2.4000,\"publicationDate\":\"2024-02-03\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Science and Biotechnology\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s10068-023-01490-z\",\"RegionNum\":3,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Science and Biotechnology","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1007/s10068-023-01490-z","RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Hydrolysates with emulsifying properties prepared from protein wastes using microbial protease
Plant-based protein hydrolysates have found applications in food industry for emulsification, foaming, and increasing shelf life of food products. The objective of this study is to isolate protease-secreting bacteria hydrolyzing protein waste, and subjecting the resultant hydrolysates for the characterization for application in the food industry. Peanut cake hydrolysates were prepared using proteases from two microorganisms selected for the purpose, viz., Aneurinibacillus migulanus, VITPM11 and Aneurinibacillus aneurinilyticus, VITPS07. The cleavage specificity of the proteases from VITPM11 and VITPS07 were found to be like plasmin and elastase respectively. The cleaving sites of proteases for peanut proteins were predicted using expasy tool. The protease of VITPM11 had maximal activity of 325.8 ± 0.1 U/mL in peanut-cake media. The degree of hydrolysis (32.03 ± 0.89%), solubility (88.5 ± 1.18%), emulsion stability index (89.76 ± 2.80) and foaming stability (68.67 ± 1.53%) properties of VITPM11 protease correlated well with results from bioinformatic studies.
期刊介绍：
The FSB journal covers food chemistry and analysis for compositional and physiological activity changes, food hygiene and toxicology, food microbiology and biotechnology, and food engineering involved in during and after food processing through physical, chemical, and biological ways. Consumer perception and sensory evaluation on processed foods are accepted only when they are relevant to the laboratory research work. As a general rule, manuscripts dealing with analysis and efficacy of extracts from natural resources prior to the processing or without any related food processing may not be considered within the scope of the journal. The FSB journal does not deal with only local interest and a lack of significant scientific merit. The main scope of our journal is seeking for human health and wellness through constructive works and new findings in food science and biotechnology field.
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