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1、10968J.Agric.FoodChem.2007,55,1096810976ChangesinStructuresofMilkProteinsuponPhoto-oxidationTRINEK.DALSGAARD,DANIELOTZEN,,JACOBH.NIELSEN,ANDLOTTEB.LARSEN*DepartmentofFoodScience,UniversityofAarhus,P.O.Box50,DK-8830Tjele,DenmarkandInterdisciplinaryNanoscienceCentre(iNANO)DepartmentofMo
2、lecularBiology,GustarWiedsVej10C,UniversityofAarhus,8000AarhusC,DenmarkChangesinproteinstructuresasaresultofriboflavin-inducedphoto-oxidationwerestudiedforsixmilkproteins:R-casein,-casein,κ-casein,lactoferrin,R-lactalbumin,and-lactoglobulin.Themilkproteinsshowedsignificantvariabilityi
3、nsensitivitytophoto-oxidation.Afterphoto-oxidation,anincreaseincarbonylcontentbecauseofoxidationoftryptophan,histidine,andmethionine,aswellasformationofdityrosine,wasobservedforallproteinsstudied,althoughatverydifferentlevels.Generally,theincrementwashighestforR-and-caseinandwaslowes
4、tforlactoferrin.Lossoftryptophanbecauseofphoto-oxidationwaswell-correlatedwiththeformationofthetryptophanoxidationproducts,N-formylkynurenineandkynurenine.Changesatthetertiaryproteinstructurelevelwereobservedafterphoto-oxidationoftheglobularproteins,wheretryptophanfluorescenceemissioni
5、ndicatedunfoldingofR-lactalbuminand-lactoglobulin,whereaslactoferrinachievedamorecompacttertiarystructure.ChangesinsecondarystructurewereobservedforR-lactalbuminand-lactoglobulin,whereasthesecondarystructureoflactoferrindidnotchange.PolymerizationofR-and-caseinandoflactoferrinwasob
6、served,whereasκ-casein,R-lactalbumin,and-lactoglobulinshowedlittletendencytopolymerizeafterphoto-oxidation.Labilitytowardphoto-oxidationisdiscussedaccordingtothestructuralstabilitiesoftheglobularproteins.KEYWORDS:Photo-oxidation;milkproteins;riboflavin;proteinstructure;proteinoxidatio
7、nINTRODUCTIONreducecleavageoftheproteinsthatarenecessaryfortheclottingprocessinmilk.Reactiveoxidativespeciesarefoundinallfoodstuffs,Proteinoxidationinmilkcanbeinitiatedeitherenzymatically,includingmilkandmilk-derivedproducts.Traditionally,theforexample,bythelactoperoxidasesystem(3),by
8、photo