不同比例酪蛋白与牛明胶酶促交联产物的功能性质
|
摘要
将酪蛋白和明胶以2∶1、4∶1和6∶1的质量比混合,并利用转谷氨酰胺酶进行酶促反应,制备酪蛋白-明胶交联复合物,通过对交联复合物功能性质的测定,研究明胶比例不同对复合物功能性质的影响,以发新型蛋白质配料。在5%(w/v)底物浓度下,每克蛋白质添加转谷氨酰胺酶10 U,45℃反应4 h,等电点沉淀除去游离明胶和交联明胶,得到4-羟脯氨酸含量分别为51.37、33.38、25.97 g/kg蛋白质的3个复合物。复合物在pH 4.5或更低时溶解性优于酪蛋白,但在中性或弱碱性时则低于酪蛋白。与酪蛋白相比,复合物的吸水性、吸油性均有显著提高,明胶含量高的复合物其吸油性较高,而吸水性相应较低。不过,复合物的体外消化能力低于酪蛋白,并且随着明胶含量的增加其体外消化能力降低。
Casein and bovine gelatin were mixed in three ratios of 2:1,4:1,6:1( w /w),respectively,and treated by transglutaminase to prepare three casein-gelatin composites,which were then evaluated for their functional properties to reveal whether the addition levels of bovine gelatin had impacts on the evaluated properties and if the composites were potential as new protein ingredients for food processing.Under the selected reaction conditions such as transglutaminase addition of 10 U/g protein,reaction temperature of 45℃ and reaction time of 4 h,together with an isoelectric precipitation procedure for the prepared composites to remove the free and cross-linked gelatin,three composites thus obtained had 4-hydroxyproline content of 51.27,33.38,25.97 g/kg protein,respectively.The composites had better solubility than casein at pH 4.5 or lower pH,but showed lower solubility than casein at neutral or alkaline conditions.Compared to casein,the composites had better water holding capacity and oil absorption capacity.The composite containing more gelatin also exhibited higher water holding capacity but lower oil absorption capacity.The composites showed lower in-vitro digestibility compared with casein,especially if more gelatin was crosslinked into the composite.
Casein and bovine gelatin were mixed in three ratios of 2:1,4:1,6:1( w /w),respectively,and treated by transglutaminase to prepare three casein-gelatin composites,which were then evaluated for their functional properties to reveal whether the addition levels of bovine gelatin had impacts on the evaluated properties and if the composites were potential as new protein ingredients for food processing.Under the selected reaction conditions such as transglutaminase addition of 10 U/g protein,reaction temperature of 45℃ and reaction time of 4 h,together with an isoelectric precipitation procedure for the prepared composites to remove the free and cross-linked gelatin,three composites thus obtained had 4-hydroxyproline content of 51.27,33.38,25.97 g/kg protein,respectively.The composites had better solubility than casein at pH 4.5 or lower pH,but showed lower solubility than casein at neutral or alkaline conditions.Compared to casein,the composites had better water holding capacity and oil absorption capacity.The composite containing more gelatin also exhibited higher water holding capacity but lower oil absorption capacity.The composites showed lower in-vitro digestibility compared with casein,especially if more gelatin was crosslinked into the composite.
引文
[1]Dichinson E.Enzymic cross-linking as a tool for food colloid rheology control and interfacial stabilization[J].Trends in Food Science and Technology,1997,8(10):334-339.
[2]Motok M,Seguro K.Transglutaminase and its use for food processing[J].Trends in Food Science and Technology,1998,9(5):204-210.
[3]De Jong G A H,Koppelman S J.Transglutaminase catalyzed reactions:impact on food applications[J].Journal of Food Science,2002,67(8):2 798-2 806.
[4]Liu M,Damodaran S.Effect of transglutaminase-catalyzed polymerization ofβ-casein on its emulsifying properties[J].Journal of Agricultural and Food Chemistry,1999,47(4):1 514-1 519.
[5]Domagala J,Wszolek M,Tamime A Y,et al.The effect of transglutaminase concentration on the texture,syneresis and microstructure of set-type goat’s milk yoghurt during the storage period[J].Small Ruminant Research,2013,112(1-3):154-161.
[6]Damodaran S,Agyare K K.Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate[J].Food Hydrocolloids,2013,30(1):12-18.
[7]Mhd Sarbon N,Badii F,Howell N K.Preparation and characterization of chicken skin gelatin as an alternative to mammalian gelatin[J].Food Hydrocolloids,2013,30(1):143-151.
[8]张伊宁,赵新淮.酪蛋白与明胶的酶促交联与产物的流变学性质[J].中国乳品工业,2011,39(3):20-23.
[9]Syk I,gren M S,Adawi D,et al.Inhibition of matrix metalloproteinases enhances breaking strength of colonic anastomoses in an experimental model[J].British Journal of Surgery,2001,88(2):228-234.
[10]Bera M B,Mukherjee R K.Solubility,emulsifying,and foaming properties of rice bran protein concentrates[J].Journal of Food Science,1989,54(1):142-145.
[11]Yin S W,Tang C H,Wen Q B,et al.Functional properties and in vitro trypsin digestibility of red kidney bean(Phaseolus vulgaris L.)protein isolate:Effect of highpressure treatment[J].Food Chemistry,2008,110(4):938-945.
[12]Saetae D,Kleekayai T,Jayasena V,et al.Functional properties of protein isolate obtained from physic nut(Jatropha curcas L.)seed cake[J].Food Science and Biotechnology,2011,20(1):29-37.
[13]Lin M J Y,Humbert E S,Sosulski F W.Certain functional properties of sunflower meal products[J].Journal of Food Science,1974,39(2):368-370.
[14]Lin Y K,Kuan C Y.Development of 4-hydroxyproline analysis kit and its application to collagen quantification[J].Food Chemistry,2010,119(3):1 271-1 277.
[15]Agyare K K,Xiong Y L,Addo K.Influence of salt and pH on the solubility and structural characteristics of transglutaminase-treated wheat gluten hydrolysate[J].Food Chemistry,2008,107(3):1 131-1 137.
[16]Souissi N,Bougatef A,Triki-Ellouz Y,et al.Biochemical and functional properties of sardinella(Sardinella aurita)by-product hydrolysates[J].Food Technology and Biotechnology,2007,45(2):187-194.
[17]Roos N,Lorenzen P C,Sick H,et al.Cross-linking by transglutaminase changes neither the in vitro proteolysis nor the in vivo digestibility of caseinate[J].Kieler Milchwirtschaftliche Forschungsberichte,2003,55(4):261-276.
[18]Kishimura H,Tokuda Y,Yabe M,et al.Trypsins from the pyloric ceca of jacopever(Sebastes schlegelii)and elkhorn sculpin(Alcichthys alcicornis):Isolation and characterization[J].Food Chemistry,2007,100(4):1 490-1 495.
[19]Schrieber R,Gareis H.Gelatin handbook:theory and industrial practice[M].Darmstadt,Germany:John Wiely&Sons,2007:60.
[20]Imm J Y,Lian P,Lee C M.Gelation and water binding properties of transglutaminase-treated skim milk powder[J].Journal of Food Science,2000,65(2):200-205.
[21]Lorenzen P C.Techno-functional properties of transglutaminase-treated milk proteins[J].Milchwissenschaft,2000,55(12):667-670.
[22]Kinsella J E.Functional properties of proteins in foods:a survey[J].Critical Reciews in Food Science and Nutrition,1976,7(3):219-280.
[2]Motok M,Seguro K.Transglutaminase and its use for food processing[J].Trends in Food Science and Technology,1998,9(5):204-210.
[3]De Jong G A H,Koppelman S J.Transglutaminase catalyzed reactions:impact on food applications[J].Journal of Food Science,2002,67(8):2 798-2 806.
[4]Liu M,Damodaran S.Effect of transglutaminase-catalyzed polymerization ofβ-casein on its emulsifying properties[J].Journal of Agricultural and Food Chemistry,1999,47(4):1 514-1 519.
[5]Domagala J,Wszolek M,Tamime A Y,et al.The effect of transglutaminase concentration on the texture,syneresis and microstructure of set-type goat’s milk yoghurt during the storage period[J].Small Ruminant Research,2013,112(1-3):154-161.
[6]Damodaran S,Agyare K K.Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate[J].Food Hydrocolloids,2013,30(1):12-18.
[7]Mhd Sarbon N,Badii F,Howell N K.Preparation and characterization of chicken skin gelatin as an alternative to mammalian gelatin[J].Food Hydrocolloids,2013,30(1):143-151.
[8]张伊宁,赵新淮.酪蛋白与明胶的酶促交联与产物的流变学性质[J].中国乳品工业,2011,39(3):20-23.
[9]Syk I,gren M S,Adawi D,et al.Inhibition of matrix metalloproteinases enhances breaking strength of colonic anastomoses in an experimental model[J].British Journal of Surgery,2001,88(2):228-234.
[10]Bera M B,Mukherjee R K.Solubility,emulsifying,and foaming properties of rice bran protein concentrates[J].Journal of Food Science,1989,54(1):142-145.
[11]Yin S W,Tang C H,Wen Q B,et al.Functional properties and in vitro trypsin digestibility of red kidney bean(Phaseolus vulgaris L.)protein isolate:Effect of highpressure treatment[J].Food Chemistry,2008,110(4):938-945.
[12]Saetae D,Kleekayai T,Jayasena V,et al.Functional properties of protein isolate obtained from physic nut(Jatropha curcas L.)seed cake[J].Food Science and Biotechnology,2011,20(1):29-37.
[13]Lin M J Y,Humbert E S,Sosulski F W.Certain functional properties of sunflower meal products[J].Journal of Food Science,1974,39(2):368-370.
[14]Lin Y K,Kuan C Y.Development of 4-hydroxyproline analysis kit and its application to collagen quantification[J].Food Chemistry,2010,119(3):1 271-1 277.
[15]Agyare K K,Xiong Y L,Addo K.Influence of salt and pH on the solubility and structural characteristics of transglutaminase-treated wheat gluten hydrolysate[J].Food Chemistry,2008,107(3):1 131-1 137.
[16]Souissi N,Bougatef A,Triki-Ellouz Y,et al.Biochemical and functional properties of sardinella(Sardinella aurita)by-product hydrolysates[J].Food Technology and Biotechnology,2007,45(2):187-194.
[17]Roos N,Lorenzen P C,Sick H,et al.Cross-linking by transglutaminase changes neither the in vitro proteolysis nor the in vivo digestibility of caseinate[J].Kieler Milchwirtschaftliche Forschungsberichte,2003,55(4):261-276.
[18]Kishimura H,Tokuda Y,Yabe M,et al.Trypsins from the pyloric ceca of jacopever(Sebastes schlegelii)and elkhorn sculpin(Alcichthys alcicornis):Isolation and characterization[J].Food Chemistry,2007,100(4):1 490-1 495.
[19]Schrieber R,Gareis H.Gelatin handbook:theory and industrial practice[M].Darmstadt,Germany:John Wiely&Sons,2007:60.
[20]Imm J Y,Lian P,Lee C M.Gelation and water binding properties of transglutaminase-treated skim milk powder[J].Journal of Food Science,2000,65(2):200-205.
[21]Lorenzen P C.Techno-functional properties of transglutaminase-treated milk proteins[J].Milchwissenschaft,2000,55(12):667-670.
[22]Kinsella J E.Functional properties of proteins in foods:a survey[J].Critical Reciews in Food Science and Nutrition,1976,7(3):219-280.
© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号 地址：北京市海淀区学院路29号 邮编：100083 电话：办公室：(+86 10)66554848；文献借阅、咨询服务、科技查新：66554700 |