Chengkang Li , Peter A. Paulsen , Halise Gül Akıllıoğlu , Søren B. Nielsen , Kasper Engholm-Keller , Marianne N. Lund
{"title":"半胱氨酸残基是在加热乳清蛋白溶液中形成含硫异味的原因","authors":"Chengkang Li , Peter A. Paulsen , Halise Gül Akıllıoğlu , Søren B. Nielsen , Kasper Engholm-Keller , Marianne N. Lund","doi":"10.1016/j.fochms.2022.100120","DOIUrl":null,"url":null,"abstract":"<div><p>Odor-active volatile sulfur compounds are formed in heated food protein systems. In the present study, hydrogen sulfide (H<sub>2</sub>S) was found to be the most abundant sulfur volatile in whey protein solutions (whey protein isolate [WPI], a whey model system and single whey proteins) by gas chromatography-flame photometric detector (GC-FPD) analysis after heat treatments (60–90 °C for 10 min, 90 °C for 120 min and UHT-like treatment). H<sub>2</sub>S was detected in WPI after heating at 90 °C for 10 min, and was significantly increased at higher heat load (90 °C for 120 min and the UHT-like treatment). Site-specific LC-MS/MS-based proteomic analysis was conducted, monitoring desulfurization reactions in these protein systems to investigate the mechanism of H<sub>2</sub>S formation in heated WPI. Cysteine residues from beta-lactoglobulin were found to be responsible for the formation of H<sub>2</sub>S in heated WPI, presumably via beta-elimination.</p></div>","PeriodicalId":34477,"journal":{"name":"Food Chemistry Molecular Sciences","volume":"5 ","pages":"Article 100120"},"PeriodicalIF":4.1000,"publicationDate":"2022-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9294045/pdf/","citationCount":"2","resultStr":"{\"title\":\"Cysteine residues are responsible for the sulfurous off-flavor formed in heated whey protein solutions\",\"authors\":\"Chengkang Li , Peter A. Paulsen , Halise Gül Akıllıoğlu , Søren B. Nielsen , Kasper Engholm-Keller , Marianne N. Lund\",\"doi\":\"10.1016/j.fochms.2022.100120\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Odor-active volatile sulfur compounds are formed in heated food protein systems. In the present study, hydrogen sulfide (H<sub>2</sub>S) was found to be the most abundant sulfur volatile in whey protein solutions (whey protein isolate [WPI], a whey model system and single whey proteins) by gas chromatography-flame photometric detector (GC-FPD) analysis after heat treatments (60–90 °C for 10 min, 90 °C for 120 min and UHT-like treatment). H<sub>2</sub>S was detected in WPI after heating at 90 °C for 10 min, and was significantly increased at higher heat load (90 °C for 120 min and the UHT-like treatment). Site-specific LC-MS/MS-based proteomic analysis was conducted, monitoring desulfurization reactions in these protein systems to investigate the mechanism of H<sub>2</sub>S formation in heated WPI. Cysteine residues from beta-lactoglobulin were found to be responsible for the formation of H<sub>2</sub>S in heated WPI, presumably via beta-elimination.</p></div>\",\"PeriodicalId\":34477,\"journal\":{\"name\":\"Food Chemistry Molecular Sciences\",\"volume\":\"5 \",\"pages\":\"Article 100120\"},\"PeriodicalIF\":4.1000,\"publicationDate\":\"2022-12-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9294045/pdf/\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Chemistry Molecular Sciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S266656622200048X\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry Molecular Sciences","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S266656622200048X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Cysteine residues are responsible for the sulfurous off-flavor formed in heated whey protein solutions
Odor-active volatile sulfur compounds are formed in heated food protein systems. In the present study, hydrogen sulfide (H2S) was found to be the most abundant sulfur volatile in whey protein solutions (whey protein isolate [WPI], a whey model system and single whey proteins) by gas chromatography-flame photometric detector (GC-FPD) analysis after heat treatments (60–90 °C for 10 min, 90 °C for 120 min and UHT-like treatment). H2S was detected in WPI after heating at 90 °C for 10 min, and was significantly increased at higher heat load (90 °C for 120 min and the UHT-like treatment). Site-specific LC-MS/MS-based proteomic analysis was conducted, monitoring desulfurization reactions in these protein systems to investigate the mechanism of H2S formation in heated WPI. Cysteine residues from beta-lactoglobulin were found to be responsible for the formation of H2S in heated WPI, presumably via beta-elimination.
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