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

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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.

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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。

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