转谷氨酰胺酶对大豆分离蛋白乳状液冻融稳定性的影响
|
摘要
采用转谷氨酰胺酶(transglutaminase,TGase)改性提高大豆分离蛋白(soybean protein isolate,SPI)乳状液冻融稳定性。以出油率和分层系数为稳定性指标,研究TGase交联时间、添加量、冻融循环次数对SPI乳状液冻融稳定性的影响。通过显微结构、热特性分析比较研究由SPI、TGase改性SPI作为乳化剂乳状液的冻融稳定性,利用十二烷基硫酸钠-聚丙烯酰氨凝胶电泳分析酶改性对SPI组成的影响,进而分析与乳状液稳定性的关系。结果表明:经过3次冻融循环后改性SPI制备的乳化剂仍保持较好的冻融稳定性,TGase交联时间3 h、添加量1.5%时稳定性较好,微观结构可看出改性SPI乳状液处于相对稳定状态。乳状液冻融过程中热特性的差异,反映出改性蛋白在冻融过程中乳状液结晶及融化的热行为得到了改变。十二烷基硫酸钠-聚丙烯酰氨凝胶电泳结果表明酶改性使蛋白组成发生改变,从而影响大豆蛋白的冻融稳定性。TGase改性大豆蛋白具有较好的冻融稳定性,为其在冷冻食品中应用提供理论依据。
In this study, transglutaminase(TGase) was used to improve the freeze-thaw stability of oil-in-water emulsion stabilized by soybean protein isolate(SPI). We evaluated the influence of TGase reaction time, enzyme dosage and the number of freeze-thaw cycles on the freeze-thaw stability of SPI-stabilized emulsion as re?ected by oiling off and creaming index. Meanwhile, the microstructure and thermal characteristics of the emulsions containing SPI and TGase-modi?ed SPI as emulsi?er were compared, and the effect of TGase modi?cation on SPI composition was examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE). Furthermore, the relationship between enzymatic modification and emulsion stability was analyzed. The results show that after three freeze-thaw cycles, the emulsion containing TGasemodified SPI maintained good stability. A crosslinking time of 3 h and an enzyme dosage of 1.5% were found to be optimal conditions to obtain better freeze-thaw stability. The emulsion remained stable as indicated by its microstructure.The changes in thermal properties during freeze-thaw showed that the crystallization and melting behavior of the emulsion altered. SDS-PAGE revealed that SPI composition changed after enzymatic modi?cation, thus affecting the freeze-thaw stability of the emulsion. This study provides a theoretical foundation for applying TGase-modi?ed SPI in frozen food.
In this study, transglutaminase(TGase) was used to improve the freeze-thaw stability of oil-in-water emulsion stabilized by soybean protein isolate(SPI). We evaluated the influence of TGase reaction time, enzyme dosage and the number of freeze-thaw cycles on the freeze-thaw stability of SPI-stabilized emulsion as re?ected by oiling off and creaming index. Meanwhile, the microstructure and thermal characteristics of the emulsions containing SPI and TGase-modi?ed SPI as emulsi?er were compared, and the effect of TGase modi?cation on SPI composition was examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE). Furthermore, the relationship between enzymatic modification and emulsion stability was analyzed. The results show that after three freeze-thaw cycles, the emulsion containing TGasemodified SPI maintained good stability. A crosslinking time of 3 h and an enzyme dosage of 1.5% were found to be optimal conditions to obtain better freeze-thaw stability. The emulsion remained stable as indicated by its microstructure.The changes in thermal properties during freeze-thaw showed that the crystallization and melting behavior of the emulsion altered. SDS-PAGE revealed that SPI composition changed after enzymatic modi?cation, thus affecting the freeze-thaw stability of the emulsion. This study provides a theoretical foundation for applying TGase-modi?ed SPI in frozen food.
引文
[1]简俊丽,毛丽娟,刘夫国,等.食品乳状液冻融稳定性的研究进展[J].食品与发酵工业, 2015, 41(4):236-240. DOI:10.13995/j.cnki.11-1802/ts.201504044.
[2]MORENO F L, RAVENTOS M, HEMANDEZ E, et al. Rheological behaviour, freezing curve, and density of coffee solutions at temperatures close to freezing[J]. International Journal of Food Properties, 2015, 18(2):426-438. DOI:10.1080/10942912.2013.833221.
[3]BAMBAJ,CAVEG,BENSOUDAY,etal.Cryoprotectionof emulsionsin freeze-drying:freezing processanalysis[J].Drug Development&Industrial Pharmacy,2008,21(15):1749-1760.DOI:10.3109/03639049509069262.
[4]MCCLEMENTS D J. Protein-stabilized emulsions[J]. Current Opinion inColloid&InterfaceScience,2005,9(5):305-313.DOI:10.1016/j.cocis.2004.09.003.
[5]刘玉兰.现代植物油料油脂加工技术[M].郑州:河南科学技术出版社, 2015.
[6]ABIOSESH,IKUJENLOLAAV,ABODENNFI.Nutritional quality assessment of complementary foods produced from fermented and malted quality protein maize fortified with soy bean flour[J].PolishJournalofFood&NutritionSciences,2015,65(1):49-56.DOI:10.1515/pjfns-2015-0004.
[7]MOLINA E, PAPADOPOULOU A, LEDWARD D A. Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins[J]. Food Hydrocolloids, 2001, 15(3):263-269. DOI:10.1016/S0268-005X(01)00023-6.
[8]THANASUKARN P, PONGSAWATMANIT R, MCCLEMENTS D J.In?uence of emulsi?er type on freeze-thaw stability of hydrogenated palm oil-in-water emulsions[J]. Food Hydrocolloids, 2004, 18(6):1033-1043. DOI:10.1016/j.foodhyd.2004.04.010.
[9]GHOSH S, COUPLAND J N. Factors affecting the freeze-thaw stability of emulsions[J]. Food Hydrocolloids, 2008, 22(1):105-111.DOI:10.1016/j.foodhyd.2007.04.013.
[10]李彦萍,许彬,李斌.食品化学理论与应用研究[M].北京:中国水利水电出版社, 2015.
[11]HUX,RENJY,ZHAOMM,etal.Emulsifyingpropertiesofthe transglutaminase-treated crosslinked product between peanut protein and?sh(Decapterus maruadsi)protein hydrolysates[J]. Journal of the Science of Food&Agriculture, 2011, 91(3):578-585. DOI:10.1002/jsfa.4229.
[12]徐莹.高乳化稳定性大豆蛋白的酶法制备及在冰淇淋中的应用[D].无锡:江南大学, 2013.
[13]黄志良,宁正祥.转谷氨酰胺酶对乳蛋白质的改性作用[J].食品工业科技, 2002, 23(3):77-79. DOI:10.3969/j.issn.1002-0306.2002.03.031.
[14]KIMURAA,FUKUDAT,ZHANGM,etal.Comparisonof physicochemicalpropertiesof7Sand11Sglobulinsfrompea,fava bean, cowpea, and French bean with those of soybean:French bean7S globulin exhibits excellent properties[J]. Journal of Agricultural&Food Chemistry, 2008, 56(21):10273-10279. DOI:10.1021/jf801721b.
[15]PALANUWECH J, POTINENI R, ROBERTS R F, et al. A method to determine free fat in emulsions[J]. Food Hydrocolloids, 2003, 17(1):55-62. DOI:10.1016/S0268-005X(02)00035-8.
[16]NOSHAD M, MOHEBBI M, SHAHIDI F, et al. Freeze-thaw stability of emulsions with soy protein isolate through interfacial engineering[J]. International Journal of Refrigeration, 2015, 58:253-260. DOI:10.1016/j.ijrefrig.2015.05.007.
[17]MAGNUSSON E, ROSéN C, NILSSON L. Freeze-thaw stability of mayonnaise type oil-in-water emulsions[J]. Food Hydrocolloids, 2011,25(4):707-715. DOI:10.1016/j.foodhyd.2010.08.024.
[18]于国萍.食品生物化学实验[M].北京:中国林业出版社, 2012.
[19]PALAZOLO G G, SOBRAL P A, WAGNER J R. Freeze-thaw stability of oil-in-water emulsions prepared with native and thermallydenatured soybean isolates[J]. Food Hydrocolloids, 2011, 25(3):398-409. DOI:10.1016/j.foodhyd.2010.07.008.
[20]WANG Z J, HAN F F, SUI X N, et al. Effect of ultrasound treatment on the wet heating Maillard reaction between mung bean[Vigna radiate(L.)]proteinisolatesandglucoseandonstructuraland physico-chemical properties of conjugates[J]. Journal of the Science of Food&Agriculture, 2016, 96(5):1532-1540. DOI:10.1002/jsfa.7255.
[21]ANURADHASN,PRAKASHV.Alteringfunctionalattributesof proteins through cross linking by transglutaminase:a case study with whey and seed proteins[J]. Food Research International, 2009, 42(9):1259-1265. DOI:10.1016/j.foodres.2009.06.012.
[22]BABIKER E E. Effect of transglutaminase treatment on the functional propertiesofnativeandchymotrypsin-digestedsoyprotein[J].FoodChemistry,2000,70(2):139-145.DOI:10.1016/S0308-8146(99)00231-9.
[23]DEGNER B M, CHUNG C, SCHLEGEL V, et al. Factors in?uencing the freeze-thaw stability of emulsion-based foods[J]. Comprehensive Reviews in Food Science&Food Safety, 2014, 13(2):98-113.DOI:10.1111/1541-4337.12050.
[24]BABIKEREFE,KHANMASN,MATSUDOMIN,etal.Polymerization of protease digests and SCIDhy drolysate of soyprotein by microbial transglutaminase for improvements of the functionalproperties[J].FoodResearchInternational,1996,29(7):627-634. DOI:10.1016/S0963-9969(96)00069-5.
[25]UTSUMIS,MATSUMURAY,MORIT.Foodproteinsandtheir application[M]. New York:Marcel Dekker, 1997:257-291.
[26]THANASUKARNP,PONGSAWATMANITR,MCCLEMENTS DJ.Utilization of layer-by-layerinter facialde position technique to improve freeze-thaw stability of oil-in-water emulsions[J].FoodResearchInternational,2006,39(6):721-729.DOI:10.1016/j.foodres.2006.01.010.
[27]TANGCH,CHENZ,LIL,etal.Effects of trans glutaminase treatment on thet hermalproperties of soyproteinisolates[J].Food Research International,2006,39(6):704-711.DOI:10.1016/j.foodres.2006.01.012.
[28]VANAP ALLISA,PALANUWECH J,COUPLANDJ N.Stability of emulsions to dispersed phase crystallization:effect of oilt ype,dispersed phase volume fraction,and cooling rate[J].Colloids&Surfaces:a Physicochemical&Engineering Aspects,2002,204(1):227-237. DOI:10.1016/S0927-7757(01)01135-9.
[2]MORENO F L, RAVENTOS M, HEMANDEZ E, et al. Rheological behaviour, freezing curve, and density of coffee solutions at temperatures close to freezing[J]. International Journal of Food Properties, 2015, 18(2):426-438. DOI:10.1080/10942912.2013.833221.
[3]BAMBAJ,CAVEG,BENSOUDAY,etal.Cryoprotectionof emulsionsin freeze-drying:freezing processanalysis[J].Drug Development&Industrial Pharmacy,2008,21(15):1749-1760.DOI:10.3109/03639049509069262.
[4]MCCLEMENTS D J. Protein-stabilized emulsions[J]. Current Opinion inColloid&InterfaceScience,2005,9(5):305-313.DOI:10.1016/j.cocis.2004.09.003.
[5]刘玉兰.现代植物油料油脂加工技术[M].郑州:河南科学技术出版社, 2015.
[6]ABIOSESH,IKUJENLOLAAV,ABODENNFI.Nutritional quality assessment of complementary foods produced from fermented and malted quality protein maize fortified with soy bean flour[J].PolishJournalofFood&NutritionSciences,2015,65(1):49-56.DOI:10.1515/pjfns-2015-0004.
[7]MOLINA E, PAPADOPOULOU A, LEDWARD D A. Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins[J]. Food Hydrocolloids, 2001, 15(3):263-269. DOI:10.1016/S0268-005X(01)00023-6.
[8]THANASUKARN P, PONGSAWATMANIT R, MCCLEMENTS D J.In?uence of emulsi?er type on freeze-thaw stability of hydrogenated palm oil-in-water emulsions[J]. Food Hydrocolloids, 2004, 18(6):1033-1043. DOI:10.1016/j.foodhyd.2004.04.010.
[9]GHOSH S, COUPLAND J N. Factors affecting the freeze-thaw stability of emulsions[J]. Food Hydrocolloids, 2008, 22(1):105-111.DOI:10.1016/j.foodhyd.2007.04.013.
[10]李彦萍,许彬,李斌.食品化学理论与应用研究[M].北京:中国水利水电出版社, 2015.
[11]HUX,RENJY,ZHAOMM,etal.Emulsifyingpropertiesofthe transglutaminase-treated crosslinked product between peanut protein and?sh(Decapterus maruadsi)protein hydrolysates[J]. Journal of the Science of Food&Agriculture, 2011, 91(3):578-585. DOI:10.1002/jsfa.4229.
[12]徐莹.高乳化稳定性大豆蛋白的酶法制备及在冰淇淋中的应用[D].无锡:江南大学, 2013.
[13]黄志良,宁正祥.转谷氨酰胺酶对乳蛋白质的改性作用[J].食品工业科技, 2002, 23(3):77-79. DOI:10.3969/j.issn.1002-0306.2002.03.031.
[14]KIMURAA,FUKUDAT,ZHANGM,etal.Comparisonof physicochemicalpropertiesof7Sand11Sglobulinsfrompea,fava bean, cowpea, and French bean with those of soybean:French bean7S globulin exhibits excellent properties[J]. Journal of Agricultural&Food Chemistry, 2008, 56(21):10273-10279. DOI:10.1021/jf801721b.
[15]PALANUWECH J, POTINENI R, ROBERTS R F, et al. A method to determine free fat in emulsions[J]. Food Hydrocolloids, 2003, 17(1):55-62. DOI:10.1016/S0268-005X(02)00035-8.
[16]NOSHAD M, MOHEBBI M, SHAHIDI F, et al. Freeze-thaw stability of emulsions with soy protein isolate through interfacial engineering[J]. International Journal of Refrigeration, 2015, 58:253-260. DOI:10.1016/j.ijrefrig.2015.05.007.
[17]MAGNUSSON E, ROSéN C, NILSSON L. Freeze-thaw stability of mayonnaise type oil-in-water emulsions[J]. Food Hydrocolloids, 2011,25(4):707-715. DOI:10.1016/j.foodhyd.2010.08.024.
[18]于国萍.食品生物化学实验[M].北京:中国林业出版社, 2012.
[19]PALAZOLO G G, SOBRAL P A, WAGNER J R. Freeze-thaw stability of oil-in-water emulsions prepared with native and thermallydenatured soybean isolates[J]. Food Hydrocolloids, 2011, 25(3):398-409. DOI:10.1016/j.foodhyd.2010.07.008.
[20]WANG Z J, HAN F F, SUI X N, et al. Effect of ultrasound treatment on the wet heating Maillard reaction between mung bean[Vigna radiate(L.)]proteinisolatesandglucoseandonstructuraland physico-chemical properties of conjugates[J]. Journal of the Science of Food&Agriculture, 2016, 96(5):1532-1540. DOI:10.1002/jsfa.7255.
[21]ANURADHASN,PRAKASHV.Alteringfunctionalattributesof proteins through cross linking by transglutaminase:a case study with whey and seed proteins[J]. Food Research International, 2009, 42(9):1259-1265. DOI:10.1016/j.foodres.2009.06.012.
[22]BABIKER E E. Effect of transglutaminase treatment on the functional propertiesofnativeandchymotrypsin-digestedsoyprotein[J].FoodChemistry,2000,70(2):139-145.DOI:10.1016/S0308-8146(99)00231-9.
[23]DEGNER B M, CHUNG C, SCHLEGEL V, et al. Factors in?uencing the freeze-thaw stability of emulsion-based foods[J]. Comprehensive Reviews in Food Science&Food Safety, 2014, 13(2):98-113.DOI:10.1111/1541-4337.12050.
[24]BABIKEREFE,KHANMASN,MATSUDOMIN,etal.Polymerization of protease digests and SCIDhy drolysate of soyprotein by microbial transglutaminase for improvements of the functionalproperties[J].FoodResearchInternational,1996,29(7):627-634. DOI:10.1016/S0963-9969(96)00069-5.
[25]UTSUMIS,MATSUMURAY,MORIT.Foodproteinsandtheir application[M]. New York:Marcel Dekker, 1997:257-291.
[26]THANASUKARNP,PONGSAWATMANITR,MCCLEMENTS DJ.Utilization of layer-by-layerinter facialde position technique to improve freeze-thaw stability of oil-in-water emulsions[J].FoodResearchInternational,2006,39(6):721-729.DOI:10.1016/j.foodres.2006.01.010.
[27]TANGCH,CHENZ,LIL,etal.Effects of trans glutaminase treatment on thet hermalproperties of soyproteinisolates[J].Food Research International,2006,39(6):704-711.DOI:10.1016/j.foodres.2006.01.012.
[28]VANAP ALLISA,PALANUWECH J,COUPLANDJ N.Stability of emulsions to dispersed phase crystallization:effect of oilt ype,dispersed phase volume fraction,and cooling rate[J].Colloids&Surfaces:a Physicochemical&Engineering Aspects,2002,204(1):227-237. DOI:10.1016/S0927-7757(01)01135-9.