木糖醇对大豆分离蛋白结构和起泡特性的影响
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摘要
研究添加不同质量分数木糖醇时大豆分离蛋白的结构、溶解性、表面疏水性、内源荧光强度以及起泡特性的变化情况,以期更加深入了解木糖醇对大豆分离蛋白结构和功能特性的影响。结果表明:在木糖醇的作用下,大豆分离蛋白的溶解性增加,而表面疏水性和内源荧光强度降低,原来暴露的酪氨酸和色氨酸残基则被包裹到分子内部。同时,大豆分离蛋白的结构也发生了改变,其二级结构变得更加有序、致密。由于大豆分离蛋白结构的变化,其起泡能力受到抑制。另外,木糖醇使大豆分离蛋白溶液的表观黏度增加,有利于提高其泡沫稳定性。
The effect of xylitol(0%–20%) on structural and functional properties of soy protein isolate(SPI) in phosphate buffer solution was studied by assessment of solubility, surface hydrophobicity, intrinsic fluorescence intensity, secondary conformational stability and foaming properties. The results showed that xylitol increased the solubility and decreased the surface hydrophobicity and intrinsic fluorescence intensity of SPI, resulting in encasement of the tyrosine and tryptophan residues initially exposed inside the protein molecule. In the presence of added xylitol, SPI exhibited a more compact and periodical secondary structure. These structural modifications, consequently, led to impaired foamability of SPI. In addition, an increase in the viscosity of SPI could be advantageous for enhancing its foam stability.
The effect of xylitol(0%–20%) on structural and functional properties of soy protein isolate(SPI) in phosphate buffer solution was studied by assessment of solubility, surface hydrophobicity, intrinsic fluorescence intensity, secondary conformational stability and foaming properties. The results showed that xylitol increased the solubility and decreased the surface hydrophobicity and intrinsic fluorescence intensity of SPI, resulting in encasement of the tyrosine and tryptophan residues initially exposed inside the protein molecule. In the presence of added xylitol, SPI exhibited a more compact and periodical secondary structure. These structural modifications, consequently, led to impaired foamability of SPI. In addition, an increase in the viscosity of SPI could be advantageous for enhancing its foam stability.
引文
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[30]MORO A,BAEZ G D,BUSTI P A,et al.Effects of heat-treatedβ-lactoglobulin and its aggregates on foaming properties[J].Food Hydrocolloids,2011,25(5):1009-1015.DOI:10.1016/j.foodhyd.2010.09.021.
[31]BAEZ G D,BUSTI P A,VERDINI R,et al.Glycation of heattreatedβ-lactoglobulin:Effects on foaming properties[J].Food Research International,2013,54(1):902-909.DOI:10.1016/j.foodres.2013.08.013.
[32]YANG X,FOEGEDING E A.Effects of sucrose on egg white protein and whey protein isolate foams:factors determining properties of wet and dry foams(cakes)[J].Food Hydrocolloids,2010,24(2):227-238.DOI:10.1016/j.foodhyd.2009.09.011.
[2]KEERATI M.Structural changes of soy proteins at the oil-water interface studied by fluorescence spectroscopy[J].Colloids and Surfaces B:Biointerfaces,2012,93(1):41-48.DOI:10.1016/j.colsurfb.2011.12.002.
[3]LIU C,WANG X,MA H,et al.Functional properties of protein isolates from soybeans stored under various conditions[J].Food Chemistry,2008,111(1):29-37.DOI:10.1016/j.foodchem.2008.03.040.
[4]CHANASATTRU W,DECKER E A,MCCLEMENTS D J.Modulation of thermal stability and heat-induced gelation ofβ-lactoglobulin by high glycerol and sorbitol levels[J].Food Chemistry,2007,103(2):512-520.DOI:10.1016/j.foodchem.2006.08.020.
[5]CHANASATTRU W,DECKER E A,MCCLEMENTS D J.Impact of cosolvents(polyols)on globular protein functionality:ultrasonic velocity,density,surface tension and solubility study[J].Food Hydrocolloids,2008,22(8):1475-1484.DOI:10.1016/j.foodhyd.2007.09.007.
[6]USHA R,RAMAN S S,SUBRAMANIAN V,et al.Role of polyols(erythritol,xylitol and sorbitol)on the structural stabilization of collagen[J].Chemical Physics,2006,430(4/5/6):391-396.DOI:10.1016/j.cplett.2006.09.023.
[7]WOLEVER T M S,PIEKARZ A,HOLLANDS M,et al.Sugar alcohols and diabetes:a review[J].Canadian Journal of Diabetes,2002,26(4):356-362.
[8]MAKINEN K K.Sugar alcohols,caries incidence,and remineralization of caries lesions:a literature review[J].International Journal of Dentistry,2010,2010:1-23.DOI:10.1155/2010/981072.
[9]MCCLEMENTS D J.Modulation of globular protein functionality by weakly interacting cosolvents[J].Critical Reviews in Food Science and Nutrition,2002,42(5):417-471.DOI:10.1080/20024091054210.
[10]TIMASHEFF S N.Control of protein stability and reactions by weakly interacting cosolvents:the simplicity of the complicated[J].Advances in Protein Chemistry,1998,51(1):355-432.DOI:10.1016/S0065-3233(08)60656-7.
[11]TIMASHEFF S N.Protein hydration,thermodynamic binding,and preferential hydration[J].Biochemistry,2002,41(46):13473-13482.DOI:10.1021/bi020316e.
[12]CONTI M,GALASSI M,BOSSI A,et al.Capillary isoelectric focusing:the problem of protein solubility[J].Journal of Chromatography A,1997,757(96):237-245.DOI:10.1016/S0021-9673(96)00666-8.
[13]JIANG J,CHEN J,XIONG Y L.Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes[J].Journal of Agricultural and Food Chemistry,2009,57(16):7576-7583.DOI:10.1021/jf901585n.
[14]CHEN H,WU F,XIANG D,et al.Characterization of emulsions prepared by egg yolk phosvitin with pectin,glycerol and trehalose[J].Food Hydrocolloids,2013,30(1):123-129.DOI:10.1016/j.foodhyd.2012.05.007.
[15]LEE K H,RYU H S,RHEE K C.Protein solubility characteristics of commercial soy protein products[J].Journal of Oil&Fat Industries,2003,80(1):85-90.DOI:10.1007/s11746-003-0656-6.
[16]KATO A,NAKAI S.Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins[J].Biochim Biophys Acta,1980,624(1):13-20.DOI:10.1016/0005-2795(80)90220-2.
[17]ZHANG J,LIANG L,TIAN Z,et al.Preparation and in vitro evaluation of calcium-induced soy protein isolate nanoparticles and their formation mechanism study[J].Food Chemistry,2012,133(2):390-399.DOI:10.1016/j.foodchem.2012.01.049.
[18]FLANAGAN J,FITZGERALD R J.Functionality of Bacillus proteinase hydrolysates of sodium caseinate[J].International Dairy Journal,2002,12(9):737-748.DOI:10.1016/S0958-6946(02)00067-5.
[19]ANTIPOVA A S,SEMENOVA M G.Influence of sucrose on the thermodynamic properties of the 11S globulin of Vicia faba-dextranaqueous solvent system[J].Food Hydrocolloids,1997,11(4):415-421.DOI:10.1016/S0268-005X(97)80039-2.
[20]SEMENOVA M G,ANTIPOVA A S,BELYAKOVA L E.Food protein interactions in sugar solutions[J].Current Opinion in Colloid&Interface Science,2002,7(5/6):438-444.DOI:10.1016/S1359-0294(02)00079-1.
[21]GUZEY D,MCCLEMENTS D J,WEISS J.Adsorption kinetics of BSA at air-sugar solution interfaces as affected by sugar type and concentration[J].Food Research International,2003,36(7):649-660.DOI:10.1016/S0963-9969(03)00004-8.
[22]RAIBEKAS A A,MASSEY V.Glycerol-assisted restorative adjustment of flavoenzyme conformation perturbed by site-directed mutagenesis[J].Journal of Biological Chemistry,1997,272(35):22248-22252.DOI:10.1074/jbc.272.35.22248.
[23]SAHU R K,PRAKASH V.Mechanism of prevention of aggregation of proteins:a case study of aggregation ofα-globulin in glycerol[J].International Journal of Food Properties,2008,11(3):613-623.DOI:10.1080/10942910701580367.
[24]ZHAO W,YANG R.The effect of pulsed electric fields on the inactivation and structure of lysozyme[J].Food Chemistry,2008,110(2):334-343.DOI:10.1016/j.foodchem.2008.02.008.
[25]LANGE R,BALNY C.UV-visible derivative spectroscopy under high pressure[J].Biochimica et Biophysica Acta,2002,1595(1/2):80-93.DOI:10.1016/S0167-4838(01)00336-3.
[26]ZHAO J,DONG F,LI Y,et al.Effect of freeze-thaw cycles on the emulsion activity and structural characteristics of soy protein isolate[J].Process Biochemistry,2015,50(10):1607-1613.DOI:10.1016/j.procbio.2015.06.021.
[27]LI Y,CHEN Z,MO H.Effects of pulsed electric fields on physicochemical properties of soybean protein isolates[J].LWT Food Science&Technology,2007,40(7):1167-1175.DOI:10.1016/j.lwt.2006.08.015.
[28]TONG P,GAO J,CHEN H,et al.Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin[J].Food Chemistry,2012,131(2):603-610.DOI:10.1016/j.foodchem.2011.08.084.
[29]XUE F,LI C,ZHU X,et al.Comparative studies on the physicochemical properties of soy protein isolate-maltodextrin and soy protein isolate-gum acacia conjugate prepared through Maillard reaction[J].Food Research International,2013,51(2):490-495.DOI:10.1016/j.foodres.2013.01.012.
[30]MORO A,BAEZ G D,BUSTI P A,et al.Effects of heat-treatedβ-lactoglobulin and its aggregates on foaming properties[J].Food Hydrocolloids,2011,25(5):1009-1015.DOI:10.1016/j.foodhyd.2010.09.021.
[31]BAEZ G D,BUSTI P A,VERDINI R,et al.Glycation of heattreatedβ-lactoglobulin:Effects on foaming properties[J].Food Research International,2013,54(1):902-909.DOI:10.1016/j.foodres.2013.08.013.
[32]YANG X,FOEGEDING E A.Effects of sucrose on egg white protein and whey protein isolate foams:factors determining properties of wet and dry foams(cakes)[J].Food Hydrocolloids,2010,24(2):227-238.DOI:10.1016/j.foodhyd.2009.09.011.