糖基化反应对大豆分离蛋白/麦芽糊精体系酸诱导凝胶流变性及微观结构的影响
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摘要
将大豆分离蛋白(SPI)与麦芽糊精(MD)通过美拉德反应制成SPI/MD糖基化复合物,采用紫外—可见分光光度计测定游离氨基含量和接枝度,利用差示扫描量热法分析热性质,并对SPI/MD复合体系和混合体系酸诱导凝胶流变性和微观结构进行比较。结果表明:长时间热处理会使SPI与更多的MD发生糖基化反应,SPI与MD共价结合会使体系结构发生明显改变,SPI/MD复合体系的Tp增加且ΔH降低,表明体系的热稳定性增加。SPI/MD复合体系凝胶G′显著降低,随着热处理时间的延长,凝胶G′的降低趋势明显,这可能是由于MD的共价结合引起SPI结构的改变,使共价相互作用不能很好地支撑凝胶网络,导致SPI/MD复合体系凝胶的弱化。SPI/MD混合体系凝胶G′显著增加,这是由于两种高分子聚合物之间的相分离作用所致。此外,SPI/MD复合体系形成的酸凝胶微观结构不均一、疏松且有较大的孔洞,而SPI/MD混合体系能够形成均匀、致密的凝胶网络。
Soybean protein isolate(SPI) and maltodextrin(MD) were prepared into SPI/MD conjugate systems by Maillard reaction. Free amino groups content and degree of graft were measured by UV spectrophotometry. Thermal property was analyzed by differential scanning calorimetry. The SPI/MD conjugate and mixture systems were added with 0.6%of GDL, the systems were acidified with GDL at 25 ℃ for 5 h. Effect of Maillard reaction time on rheological property of SPI acid-induced gel was explored. At the same time, the comparison of rheological property and microstructure between SPI/MD conjugate and mixture systems was researched. Results showed that SPI could glycate more MD by heating for long time. The structure of SPI system changed significantly induced by covalent binding with MD. For SPI/MD conjugate systems, Tp increased and ΔH decreased, which indicated the increase in thermal stability. SPI/MD conjugate system gels G′ reduced remarkably, and the decreasing tendency of G′ was more obvious with increasing heat treatment time. It was possible that SPI structure was changed induced by covalent binding with MD, which might not be fully available for covalent interactions in gel network, leading to weakening of SPI/MD conjugate system gels. SPI/MD mixture system gels G′ enhanced significantly, which can be accounted by the phase-separation interactions between the two polymers.In addition, compared with SPI acid-induced gels, the microstructure of acid-induced gels formed by SPI/MD conjugate systems which had looser structure and larger hole was lack of homogeneity, while SPI/MD mixture systems could form homogeneous and compact gel network.
Soybean protein isolate(SPI) and maltodextrin(MD) were prepared into SPI/MD conjugate systems by Maillard reaction. Free amino groups content and degree of graft were measured by UV spectrophotometry. Thermal property was analyzed by differential scanning calorimetry. The SPI/MD conjugate and mixture systems were added with 0.6%of GDL, the systems were acidified with GDL at 25 ℃ for 5 h. Effect of Maillard reaction time on rheological property of SPI acid-induced gel was explored. At the same time, the comparison of rheological property and microstructure between SPI/MD conjugate and mixture systems was researched. Results showed that SPI could glycate more MD by heating for long time. The structure of SPI system changed significantly induced by covalent binding with MD. For SPI/MD conjugate systems, Tp increased and ΔH decreased, which indicated the increase in thermal stability. SPI/MD conjugate system gels G′ reduced remarkably, and the decreasing tendency of G′ was more obvious with increasing heat treatment time. It was possible that SPI structure was changed induced by covalent binding with MD, which might not be fully available for covalent interactions in gel network, leading to weakening of SPI/MD conjugate system gels. SPI/MD mixture system gels G′ enhanced significantly, which can be accounted by the phase-separation interactions between the two polymers.In addition, compared with SPI acid-induced gels, the microstructure of acid-induced gels formed by SPI/MD conjugate systems which had looser structure and larger hole was lack of homogeneity, while SPI/MD mixture systems could form homogeneous and compact gel network.
引文
[1]GOLOBERG T, CAI W, PEPPA M, et al. Advanced glycoxidation end products in commonly consumed foods[J]. Journal of the American Dietetic Association, 2004, 104(8):1287-1291.
[2]MILLER A, GERRARD J. The Maillard reaction and food protein crosslinking[J]. Progress in Food Biopolymer Research, 2005, 1(5):69-86.
[3]布冠好,张楠,陈复生.大豆蛋白-木糖复合物的抗原性、致敏性及结构特性研究[J].现代食品科技,2015, 31(11):33-38.
[4]OLIVER C M, MELTON L D, STANLEY R A.Creating protein with novel functionality via the Maillard reaction:a review[J]. Critical Review in Food Science and Nutrition, 2006, 46(4):337-350.
[5]EINHORN-STOLL U, ULBRICH M, SEVER S, et al. Formation of milk protein pectin conjugates with improved emulsifying properties by controlled dry heating[J]. Food Hydrocolloids, 2005, 19(2):329-340.
[6]HILLER B, LORENZEN P C. Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation[J]. Food Research International, 2010, 43(4):1155-1166.
[7]NIU L Y, JIANG S T, PAN L J, et al. Characteristics and functionalproperties of wheat germ protein glycated with saccharides through Maillardreaction[J].International Journal of Food Science&Technology,2011, 46(10):2197-2203.
[8]LIU J, RU Q, DING Y. Glycation a promising method for food protein modification:physicochemical properties and structure, a review[J]. Food Research International, 2012, 49(1):170-183.
[9]MEDRANO A, ABIRACHED C, PANIZZOLO L, et al. The effect of glycation on foam and structural properties ofβ-lactoglobulin[J]. Food Chemistry, 2009,113(1):127-133.
[10]HATTORI M, NAGASAWA K, AMETANI A, et al.Functional changes inβ-lactoglobulin by conjugation with carboxymethyl dextran[J]. Journal of Agricultural and Food Chemistry, 1994, 42(10):2120-2125.
[11]LAZARIDOU A, VAIKOUSI H, BILIADERIS C G.Impact of mixed-linkage(1-3, 1-4)β-glucans on physical properties of acid-set skim milk gels[J]. International Dairy Journal, 2008, 18(3):312-322.
[12]ROEFS S P F M, DE GROOT-MOSTERT A E A,VAN VLIET T. Structure of acid casein gels. 1.Formation and model of gel network[J]. Colloids and Surfaces, 1990, 50(11):141-159.
[13]ZHU D, DAMODARAN S, LUCEY J A. Physicochemical and emulsifying properties of whey protein isolate(WPI)-dextran conjugates produced in aqueous solution[J]. Journal of Agricultural and Food Chemistry, 2010, 58(5):2988-2994.
[14]MARTINEZ M J, FARíAS M E, PILOSOF A M R.The dynamics of heat gelation of casein glycomacropeptide-β-lactoglobulin mixtures as affected by interactions in the aqueous phase[J]. International Dairy Journal, 2010, 20(9):580-588.
[15]PAN H, XU X, TIAN Y, et al. Impact of phase separation of soy protein isolate/sodium alginate coblending mixtures on gelation dynamics and gels properties[J]. Carbohydrate Polymers, 2015, 125(7):169-179.
[16]SPOTTI M J, PERDUCA M, PIAGENTINI A, et al. Gel mechanical properties of milk whey proteinedextran conjugates obtained by Maillard reaction[J]. Food Hydrocolloids, 2013, 31(1):26-32.
[17]TAVARES C, MONTEIRO S R, MORENO N, et al. Does the branching degree of galactomannans influence their effect on whey protein gelation[J]. Colloids and Surfaces A:Physicochemical and Engineering Aspects, 2005, 270(12):213-219.
[18]SUN W, YU S, YANG X, et al. Study on the rheological properties of heat-induced whey protein isolateedextran conjugate gel[J]. Food Research International, 2011, 44(10):3259-3263.
[19]XU C, YANG X, YU J, et al. The effect of glycosylation with dextran chains of differing lengths on the thermal aggregation ofβ-conglycinin and glycinin[J]. Food Research International, 2010, 43(9):2270-2276.
[20]SPOTTI M J, MARTINEZ M J, PILOSOF A M R,et al. Rheological properties of whey protein and dextran conjugates at different reaction times[J]. Food Hydrocolloids, 2014, 38(7):76-84.
[21]HU H, FAN X, ZHOU Z, et al. Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments[J]. Ultrasonics Sonochemistry, 2013, 20(1):187-195.
[22]MU L, ZHAO M, YANG B, et al. Effect of ultrasonic treatment on the graft reaction between soy protein isolate and gum acacia and on the physicochemical properties of conjugates[J]. Journal of Agri cultural and Food Chemistry, 2010, 58(7):4494-4499.
[2]MILLER A, GERRARD J. The Maillard reaction and food protein crosslinking[J]. Progress in Food Biopolymer Research, 2005, 1(5):69-86.
[3]布冠好,张楠,陈复生.大豆蛋白-木糖复合物的抗原性、致敏性及结构特性研究[J].现代食品科技,2015, 31(11):33-38.
[4]OLIVER C M, MELTON L D, STANLEY R A.Creating protein with novel functionality via the Maillard reaction:a review[J]. Critical Review in Food Science and Nutrition, 2006, 46(4):337-350.
[5]EINHORN-STOLL U, ULBRICH M, SEVER S, et al. Formation of milk protein pectin conjugates with improved emulsifying properties by controlled dry heating[J]. Food Hydrocolloids, 2005, 19(2):329-340.
[6]HILLER B, LORENZEN P C. Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation[J]. Food Research International, 2010, 43(4):1155-1166.
[7]NIU L Y, JIANG S T, PAN L J, et al. Characteristics and functionalproperties of wheat germ protein glycated with saccharides through Maillardreaction[J].International Journal of Food Science&Technology,2011, 46(10):2197-2203.
[8]LIU J, RU Q, DING Y. Glycation a promising method for food protein modification:physicochemical properties and structure, a review[J]. Food Research International, 2012, 49(1):170-183.
[9]MEDRANO A, ABIRACHED C, PANIZZOLO L, et al. The effect of glycation on foam and structural properties ofβ-lactoglobulin[J]. Food Chemistry, 2009,113(1):127-133.
[10]HATTORI M, NAGASAWA K, AMETANI A, et al.Functional changes inβ-lactoglobulin by conjugation with carboxymethyl dextran[J]. Journal of Agricultural and Food Chemistry, 1994, 42(10):2120-2125.
[11]LAZARIDOU A, VAIKOUSI H, BILIADERIS C G.Impact of mixed-linkage(1-3, 1-4)β-glucans on physical properties of acid-set skim milk gels[J]. International Dairy Journal, 2008, 18(3):312-322.
[12]ROEFS S P F M, DE GROOT-MOSTERT A E A,VAN VLIET T. Structure of acid casein gels. 1.Formation and model of gel network[J]. Colloids and Surfaces, 1990, 50(11):141-159.
[13]ZHU D, DAMODARAN S, LUCEY J A. Physicochemical and emulsifying properties of whey protein isolate(WPI)-dextran conjugates produced in aqueous solution[J]. Journal of Agricultural and Food Chemistry, 2010, 58(5):2988-2994.
[14]MARTINEZ M J, FARíAS M E, PILOSOF A M R.The dynamics of heat gelation of casein glycomacropeptide-β-lactoglobulin mixtures as affected by interactions in the aqueous phase[J]. International Dairy Journal, 2010, 20(9):580-588.
[15]PAN H, XU X, TIAN Y, et al. Impact of phase separation of soy protein isolate/sodium alginate coblending mixtures on gelation dynamics and gels properties[J]. Carbohydrate Polymers, 2015, 125(7):169-179.
[16]SPOTTI M J, PERDUCA M, PIAGENTINI A, et al. Gel mechanical properties of milk whey proteinedextran conjugates obtained by Maillard reaction[J]. Food Hydrocolloids, 2013, 31(1):26-32.
[17]TAVARES C, MONTEIRO S R, MORENO N, et al. Does the branching degree of galactomannans influence their effect on whey protein gelation[J]. Colloids and Surfaces A:Physicochemical and Engineering Aspects, 2005, 270(12):213-219.
[18]SUN W, YU S, YANG X, et al. Study on the rheological properties of heat-induced whey protein isolateedextran conjugate gel[J]. Food Research International, 2011, 44(10):3259-3263.
[19]XU C, YANG X, YU J, et al. The effect of glycosylation with dextran chains of differing lengths on the thermal aggregation ofβ-conglycinin and glycinin[J]. Food Research International, 2010, 43(9):2270-2276.
[20]SPOTTI M J, MARTINEZ M J, PILOSOF A M R,et al. Rheological properties of whey protein and dextran conjugates at different reaction times[J]. Food Hydrocolloids, 2014, 38(7):76-84.
[21]HU H, FAN X, ZHOU Z, et al. Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments[J]. Ultrasonics Sonochemistry, 2013, 20(1):187-195.
[22]MU L, ZHAO M, YANG B, et al. Effect of ultrasonic treatment on the graft reaction between soy protein isolate and gum acacia and on the physicochemical properties of conjugates[J]. Journal of Agri cultural and Food Chemistry, 2010, 58(7):4494-4499.