Cysteine residues are responsible for the sulfurous off-flavor formed in heated whey protein solutions

IF 4.1 Q2 FOOD SCIENCE & TECHNOLOGY

Food Chemistry Molecular Sciences Pub Date : 2022-12-30 DOI:10.1016/j.fochms.2022.100120

Chengkang Li , Peter A. Paulsen , Halise Gül Akıllıoğlu , Søren B. Nielsen , Kasper Engholm-Keller , Marianne N. Lund

{"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>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.</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}

引用次数: 2

Abstract

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.

Abstract Image

查看原文本刊更多论文

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

具有气味活性的挥发性硫化合物在加热的食物蛋白质系统中形成。在本研究中，通过气相色谱-火焰光度检测器(GC-FPD)分析，发现硫化氢(H2S)是乳清蛋白溶液(乳清分离蛋白[WPI]，乳清模型系统和单一乳清蛋白)中最丰富的挥发性硫，经过热处理(60-90°C 10分钟，90°C 120分钟和uht处理)。在90°C加热10分钟后，在WPI中检测到H2S，并且在更高的热负荷(90°C加热120分钟和类似uht的处理)下显著增加。采用基于位点特异性LC-MS/ ms的蛋白质组学分析，监测这些蛋白质体系中的脱硫反应，探讨加热WPI中H2S形成的机制。β -乳球蛋白的半胱氨酸残基被发现在加热的WPI中负责H2S的形成，可能通过β -消除。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Food Chemistry Molecular Sciences Agricultural and Biological Sciences-Food Science

CiteScore

6.00

自引率

0.00%

发文量

审稿时长

82 days