Description
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 systems (whey protein isolate (WPI), a whey model system and single whey proteins) by Gas Chromatography-Flame Photometric Detector (GC-FPD) analysis after different heat treatments (60-90 C for 10 min, 90 C for 120 min and a UHT-like condition). Site-specific LC-MS/MS-based proteomic analysis was conducted to monitor desulfurization reactions in these protein systems to investigate the mechanism of H2S formation in heated WPI. H2S was detected in WPI after heating at 90 C for 10 min, and significantly increased at higher heat load (90 C for 120 min and the UHT treatment), which revealed the temperature- and time-dependence of heat-induced H2S generation in WPI. Cysteine (Cys) residues from beta-lactoglobulin were found to be responsible for the formation of H2S in heated WPI, presumably via beta-elimination.
[doi:10.25345/C59W08]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Sulfur volatile ; hydrogen sulfide ; beta-lactoglobulin ; beta-elimination ; GC-FPD ; LC-MS/MS
Contact
Principal Investigators:
(in alphabetical order)
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Marianne Nissen Lund, Department of Food Science, University of Copenhagen, Denmark
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Submitting User: |
chengkang
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