超声处理对转谷氨酰胺酶交联乳清分离蛋白的结构特性和凝胶保水性的影响
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摘要
本文研究了超声处理(20 k Hz,400 W,0、10、20、30、40 min)对转谷氨酰胺酶(TGase)交联乳清分离蛋白(WPI)的分子量分布、粒径分布、荧光强度、表面疏水性和凝胶保水性的影响。结果表明,TGase交联WPI后生成了分子量约为120 k Da的大分子聚合物,且聚合物的量随着超声处理时间的增加而逐渐增加; TGase交联WPI后的荧光强度高于未交联的WPI,且荧光强度随着超声处理时间的增加而增大; TGase交联后WPI的表面疏水性增大,且随着超声处理时间的延长,表面疏水性逐渐升高。此外,WPI的粒径随着超声处理而减小,但TGase交联后WPI的粒径明显高于未交联的WPI。TGase交联后WPI的凝胶保水性呈上升趋势,并且随着超声时间的延长而逐渐升高。因此,TGase交联WPI可以改变WPI的结构,增强其凝胶保水性。
The effect of ultrasound treatment(20 kHz,400 W,0,10,20,30,40 min) on the molecular weight distribution,particle size distribution,fluorescence intensity,surface hydrophobicity and water holding capacity(WHC) of TGase-catalyzed WPI were studied.SDS-PAGE indicated that the formation of high molecular aggregates(with a molecular weight about120 kDa) after the reaction of TGase cross-linking,and the amount of aggregates increased with the increase of ultrasound time.The results of fluorescence spectroscopy and surface hydrophobicity analysis showed that TGase-catalyzed WPI had higher fluorescence intensity and surface hydrophobicity than WPI,which increased with the ultrasound time increasing.Besides,the particle size of TGase-catalyzed WPI was significantly higher than that of WPI.In addition,the water holding capacity of WPI increased after TGase cross-linking,which also increased with the increase of ultrasound time.Therefore,TGase-catalyzed cross-linking of WPI could change WPI structure,and enhance its gel water holding capacity.
The effect of ultrasound treatment(20 kHz,400 W,0,10,20,30,40 min) on the molecular weight distribution,particle size distribution,fluorescence intensity,surface hydrophobicity and water holding capacity(WHC) of TGase-catalyzed WPI were studied.SDS-PAGE indicated that the formation of high molecular aggregates(with a molecular weight about120 kDa) after the reaction of TGase cross-linking,and the amount of aggregates increased with the increase of ultrasound time.The results of fluorescence spectroscopy and surface hydrophobicity analysis showed that TGase-catalyzed WPI had higher fluorescence intensity and surface hydrophobicity than WPI,which increased with the ultrasound time increasing.Besides,the particle size of TGase-catalyzed WPI was significantly higher than that of WPI.In addition,the water holding capacity of WPI increased after TGase cross-linking,which also increased with the increase of ultrasound time.Therefore,TGase-catalyzed cross-linking of WPI could change WPI structure,and enhance its gel water holding capacity.
引文
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[26]Zhang P,Hu T,Feng S,et al.Effect of high intensity ultrasound on transglutaminase-catalyzed soy protein isolate cold set gel[J].Ultrasonics Sonochemistry,2016,29:380.
[2]Fu M,Zhao X H.Modified properties of a glycated and crosslinked soy protein isolate by transglutaminase and an oligochitosan of 5 k Da[J].Journal of the Science of Food&Agriculture,2016,97(1):58-64.
[3]Agyare K K,Addo K,Xiong Y L.Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by p H,temperature and salt[J].Food Hydrocolloids,2009,23(1):72-81.
[4]Faergemand M,Otte J,Qvist K B.Enzymatic cross-lining of whey proteins by a Ca2+-independent microbial transglutaminase from Streptomyces lydicus[J].Food Hydrocolloids,1997,11(1):19-25.
[5]Lorenzen,P C(2000).Techno-functional properties of transglutaminase-treated milk proteins[J].Milchwissenschaftmilk Science International,55(12):667-670.
[6]Ahmadi Z,Razavi S M A,Varidi M.Sequential ultrasound and transglutaminase treatments improve functional,rheological,and textural properties of whey protein concentrate[J].Innovative Food Science&Emerging Technologies,2017,43:207-215.
[7]Wang J S,Zhao M M,Yang X Q,et al.Gelation behavior of wheat gluten by heat treatment followed by transglutaminase cross-linking reaction[J].Food Hydrocolloids,2007,21(2):174-179.
[8]Lorenzen P C.Effects of varying time/temperature-conditions of pre-heating and enzymatic cross-linking on techno-functional properties of reconstituted dairy ingredients[J].Food Research International,2007,40(6):700-708.
[9]Chen C C,Hsieh J F.Microwave-assisted cross-linking of milk proteins induced by microbial transglutaminase[J].Scientific Reports,2016,6:39040.
[10]Cando D,Borderías A J,Moreno H M.Combined effect of aminoacids and microbial transglutaminase on gelation of low salt surimi content under high pressure processing[J].Innovative Food Science&Emerging Technologies,2016,36:10-17.
[11]Arzeni C,Pérez O E,Amr P.Functionality of egg white proteins as affected by high intensity ultrasound[J].Food Hydrocolloids,2012,29(2):308-316.
[12]Yuan X,Li X,Zhang X,et al.Effect of ultrasound on structure and functional properties of laccase-catalyzedα-lactalbumin[J].Journal of Food Engineering,2018,223:116-123.
[13]Cura D E,Lantto R,Lille M,et al.Laccase-aided protein modification:Effects on the structural properties of acidified sodium caseinate gels[J].International Dairy Journal,2009,19(12):737-745.
[14]Liu Y,Zhao G,Mouming Zhaoa,et al.Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction[J].Food Chemistry,2012,131(3):901-906.
[15]Chandrapala J,Zisu B,Palmer M,et al.Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate[J].Ultrasonics Sonochemistry,2011,18(5):951-957.
[16]Jiang Z,Yuan X,Yao K,et al.Laccase-aided modification:Effects on structure,gel properties and antioxidant activities ofα-lactalbumin[J].LWT-Food Science and Technology,2017,80.
[17]Hu H,Zhu X,Hu T,et al.Effect of ultrasound pre-treatment on formation of transglutaminase-catalysed soy protein hydrogel as a riboflavin vehicle for functional foods[J].Journal of Functional Foods,2015,19(1):182-193.
[18]Uluko H,Zhang S,Liu L,et al.Effects of thermal,microwave,and ultrasound pretreatments on antioxidative capacity of enzymatic milk protein concentrate hydrolysates[J].Journal of Functional Foods,2014,18:1138-1146.
[19]胡坦,张珮珮,郑婷,等.高场强超声-加热联用增强大豆分离蛋白冷凝胶凝胶特性[J].农业工程学报,2016,32(20):306-314.
[20]Qin X S,Luo S Z,Cai J,et al.Transglutaminase-induced gelation properties of soy protein isolate and wheat gluten mixtures with high intensity ultrasonic pretreatment[J].Ultrasonics Sonochemistry,2016,31:590.
[21]王守业,徐小龙,刘清亮,等.荧光光谱在蛋白质分子构象研究中的应用[J].化学进展,2001,13(4):257-260.
[22]Arzeni C,Martínez K,Zema P,et al.Comparative study of high intensity ultrasound effects on food proteins functionality[J].Journal of Food Engineering,2012,108(3):463-472.
[23]Qiu C,Hu X,Li L,et al.Effect of transglutaminase crosslinking on the conformational and emulsifying properties of peanut arachin and conarachin fractions[J].European Food Research&Technology,2017,243(6):913-920.
[24]涂宗财,包中宇,王辉,等.超声波对大豆分离蛋白结构及其形成谷氨酰胺转氨酶改性凝胶性质的影响[J].食品科学,2015,36(15):15-19.
[25]Hu H,Wu J,Li-Chan E C Y,et al.Effects of ultrasound on structural and physical properties of soy protein isolate(SPI)dispersions[J].Food Hydrocolloids,2013,30(2):647-655.
[26]Zhang P,Hu T,Feng S,et al.Effect of high intensity ultrasound on transglutaminase-catalyzed soy protein isolate cold set gel[J].Ultrasonics Sonochemistry,2016,29:380.