β乳球蛋白的制备及其亚硒酸化物的结构研究食品工程专业论文.docxVIP

l(ey l(ey wo rds： p-k屺toglobuliIl， seknious acid， structure research 万方数据 AB AB STRACT ThiS study waS aimed t0 f．md a new killd of orgallic selenjum compound of p-1 ．actoglobuliIl aIld seknium diox诅e iIl t11e vacum aI】d bw tempemtwe coI】ditbns．T ．he s仃ucture cl】an寥s of selenbus—D-hctoglobulill were reVea】ed by南urier仃ans南rm i11五ared specnDscopy(FT-IR)，c№ular dichroism(CD)，X-my dimaction(X-ray)，n眦kar mag豫tic resoname spectrum心MR)，MALDI—TOF-MS，two-diImnSioml e】ec廿0pboresi- s(2D)，di虢rential sca肌i119 calor沛etry(DSC)． FraCtiomtbn of p-hctogbbulill舶m 111i11(waS e冲bred by a舢m ni啪sulfate 疳actioIla【tioll，s印hadexG-50 column chom酏og泖hy and optirn娩ed men】bram s印姗tion procedm．The result showed t胁40％一70％anunoni啪sulf犯 cou】d em妯瑚st p—hctogbbulill．It waS妇optmJIll cond确n of SephadexG-50 coluITm chromatogmphy mat the sampk comel哇ration was 20m∥n1L，sa瑚ple Volume waS 2瑚_L and now rate was 4s per drops．The叩tj㈣conditiolls of ul衄矗1衄tbn were pressure O．25Mpa’time 50Ⅱ1i11．The pwity o邛-hctogbbulm啪s determilled by the KjeHahl method a耐2D and it could reach 92．5％． B1ended p-lactoglobulill with selenium diox订e，adjuSted pH to l，reacted i11-0．1 Mpa 南r 5 hours．FiIlally got sekIlious-p-hctoglobulill，矗s selellium corltent waS l 5．1 7m∥g． Selenjo时p-hctoglobu血was added Strong bands at 878crrf‘锄d 1043c面1，which be】!Dnged to Se=O and Se-0，con驴ared to p-hctogbbulill by FT—IR FiI】ally，the structure changes of seleniouS-p—lactoglobulill were studied．CD spectm results showed t11at，compared with the p-hctogbbulill，the secondary s扪℃tWe of selenj!。uS—p砌ctoglobulm waS changed signi6cantly and it i11ch】ded 卅11eliCal ratio illcreaSed 9％，D—sheet reduced of 14．2％，p—turns decreased 6％a11d random coil i11creaSed 11．2％．The collsequel】ce was also deIml】s缸ted by X-my．Tl】e resuhs of DSC showed tl】at 恤thermal s讪ility was reduced．NMR aI】alysis results a】so showed tbat tl】e tertiary s仃uctⅢe、)~懈c11anged．2DdiSplayed that sele曲us-p．hctoglobulill conta硫d tWo proteills，which the n的lecules quaIItity of om is铆o tiIlles of amtb