本文選題：食品色素 + 牛血清白蛋白�。� 參考：《西華師范大學(xué)》2017年碩士論文

【摘要】：食品色素常用來維持和改善食品的表觀顏色,當(dāng)其被吸收進(jìn)入血液循環(huán)系統(tǒng)與血清白蛋白結(jié)合時(shí),它的分布和自由濃度將受到顯著影響,因此,可以通過分析食品色素與蛋白質(zhì)間的結(jié)合特性來獲得食品色素的重要信息。酸性紅92(AR92)、酸性紅26(AR26)、酸性黑1(AB1)、酸性綠9(AG9)和酸性藍(lán)9(AB9)是五種常見食品色素,本文采用多光譜法研究這五種食品色素與牛血清白蛋白(BSA)間的相互作用,并結(jié)合-極限理論進(jìn)行了更深入的分析。探討在不同p H(4.8、5.5、6.3和7.4;BSA-AR92體系在生理p H即p H 7.4條件下進(jìn)行研究)和不同溫度(293、298、304和310 K)條件下,鹽濃度的增加對(duì)這五種食品色素與BSA之間相互作用的影響。結(jié)果表明BSA-AR92/AR26/AB1/AG9/AB9體系的KSV值與溫度呈負(fù)相關(guān),對(duì)應(yīng)的Kq值比猝滅劑與生物分子的最大散射碰撞猝滅常數(shù)(2.0×1010 L·mol-1·s-1)高,且BSA的RLS光譜強(qiáng)度隨AG9/AB9的加入而逐漸增強(qiáng),暗示這五種食品色素對(duì)BSA的熒光猝滅機(jī)制均為靜態(tài)猝滅;同一條件下結(jié)合常數(shù)K值的大小表明這五種食品色素與BSA結(jié)合親和力遵循以下順序:AR92AR26AB1AG9AB9,其n值均約為1,表明它們?cè)贐SA上有一個(gè)獨(dú)立的結(jié)合位點(diǎn);位點(diǎn)標(biāo)記物競(jìng)爭(zhēng)實(shí)驗(yàn)表明AR92的結(jié)合位點(diǎn)為BSA上的位點(diǎn)I(子域IIA);乙醇對(duì)BSA與五種食品色素結(jié)合作用的影響進(jìn)一步確認(rèn)它們?cè)贐SA上有一個(gè)特異性結(jié)合位點(diǎn);熱力學(xué)參數(shù)ΔG00,ΔH00,ΔS00暗示BSA與AR92、AR26或AB1間的結(jié)合是以靜電力為主要驅(qū)動(dòng)力的自發(fā)放熱過程;對(duì)BSA-AG9/AB9體系,在較低鹽濃度(離子強(qiáng)度)時(shí)靜電力是結(jié)合作用的主要作用力,當(dāng)鹽濃度增加到一定值時(shí),BSA與AG9/AB9之間的主導(dǎo)力由靜電力轉(zhuǎn)變?yōu)榉庆o電力(即:氫鍵作用和范德華力),相互作用時(shí)的移動(dòng)或局部運(yùn)動(dòng)因此受阻,同時(shí),從這兩個(gè)體系觀察到焓-熵補(bǔ)償(EEC);運(yùn)用-極限理論分析離子強(qiáng)度對(duì)BSA-AR26/AB1/AG9/AB9體系結(jié)合作用的影響,計(jì)算-理論分析參數(shù),結(jié)果表明BSA的局部電荷主導(dǎo)BSA-AR26/AB1/AG9/AB9體系的相互作用,而不是它的整體或表面電荷;分析不存在和存在AG9/AB9時(shí)Hurea值的變化來探討B(tài)SA的結(jié)構(gòu)穩(wěn)定性;此外,UV-vis吸收、同步熒光和FT-IR光譜研究結(jié)果表明五種食品色素與BSA間的相互作用導(dǎo)致BSA的構(gòu)象發(fā)生改變。
[Abstract]:Food pigment is often used to maintain and improve the apparent color of food. When it is absorbed into the circulatory system and binds to serum albumin, its distribution and free concentration are significantly affected. The important information of food pigments can be obtained by analyzing the binding properties between food pigments and proteins. Acid red 92C AR92N, acidic red 26AAR26, acidic black 1Ab1, acid green 9Ag-AG9) and acid blue 9A9A9) are five common food pigments. The interaction between these five food pigments and bovine serum albumin (BSA) was studied by multispectral method in this paper. And combined with the-limit theory to carry out a more in-depth analysis. The effects of salt concentration on the interaction between the five food pigments and BSA were studied under physiological pH (pH 7.4) and temperature (293298304 and 310K) in different pH 4.85.5K and 7.4 BSA-AR92 systems. The results show that the KSV value of BSA-AR92/AR26/AB1/AG9/AB9 system is negatively correlated with temperature, and the corresponding KQ value is higher than the maximum scattering quenching constant (2.0 脳 1010 L mol-1 s-1) of the quencher and biomolecules, and the RLS spectral intensity of BSA increases with the addition of AG9/AB9. It was suggested that the fluorescence quenching mechanism of the five food pigments to BSA was static quenching. Under the same condition, the binding constant K value indicated that the binding affinity of the five food pigments to BSA followed the following order: AR92AR26AB1AG9AB9, and their n values were about 1, indicating that they had an independent binding site on BSA. The competitive assay of locus marker showed that the binding site of AR92 was IIAA on BSA, and the effect of ethanol on the binding of BSA to five kinds of food pigments confirmed that they had a specific binding site on BSA. The thermodynamic parameters 螖 G _ (00), 螖 H _ (00), 螖 S _ (00) imply that the binding between BSA and AR92N / AR26 or AB1 is a self-releasing heat process driven mainly by static electricity, and that for BSA-AG9/AB9 system, electrostatic force is the main binding force at lower salt concentration (ionic strength). When the concentration of salt increases to a certain value, the dominant force between BSA and AG9/AB9 changes from hydrostatic to non-hydrostatic (i.e. hydrogen bond interaction and van der Waals force), the movement or local movement of the interaction is hindered, and at the same time, Enthalpy entropy compensation was observed in these two systems, the influence of ionic strength on the binding of BSA-AR26/AB1/AG9/AB9 system was analyzed by using the limit theory, and the parameters were calculated and analyzed. The results show that the local charge of BSA dominates the interaction of BSA-AR26/AB1/AG9/AB9 system. Rather than its whole or surface charge, the structural stability of BSA was investigated by analyzing the changes of Hurea values in the absence and presence of AG9/AB9. The results of synchronous fluorescence and FT-IR spectra showed that the interaction of five food pigments with BSA resulted in the conformation change of BSA.
【學(xué)位授予單位】：西華師范大學(xué)
【學(xué)位級(jí)別】：碩士
【學(xué)位授予年份】：2017
【分類號(hào)】：O657.3;TS264.4

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