谷氨酰胺转氨酶对荞麦分离蛋白凝胶特性的影响  

Effects of Transglutaminase on Gel Properties of Buckwheat Protein Isolate

作　　者：孙乐常[1,2,3] 王瑜 翁凌 刘明[4] 缪松 刘光明 曹敏杰 SUN Lechang;WANG Yu;WENG Ling;LIU Ming;MIAO Song;LIU Guangming;CAO Minjie(College of Marine Food and Bioengineering,Jimei University,Xiamen 361021,China;Collaborative Innovation Center of Seafood Deep Processing,Dalian Polytechnic University,Dalian 116034,China;National&Local Joint Engineering Research Center of Deep Processing Technology for Aquatic Products,Jimei University,Xiamen 361021,China;Academy of National Food and Strategic Reserves Administration,Beijing 100037,China;Teagasc Food Research Centre,Ministry of Agriculture,Cork 999014,Ireland)

机构地区：[1]集美大学海洋食品与生物工程学院,福建厦门361021 [2]海洋食品精深加工关键技术省部共建协同创新中心,大连工业大学,辽宁大连116034 [3]水产品深加工技术国家地方联合工程研究中心,福建厦门361021 [4]国家粮食和物资储备局科学研究院,北京100037 [5]爱尔兰农业部农业与食品发展局Teagasc食品研究中心,芒斯特科克999014

出　　处：《食品工业科技》2022年第24期112-122,共11页Science and Technology of Food Industry

基　　金：“十三五”国家重点研发计划重点专项(2018YFD0901004)。

摘　　要：以荞麦(Fagopyrum esculentum Moench.)为原料,通过碱溶酸沉法提取荞麦分离蛋白(BPI),分别采用真空冷冻干燥与喷雾干燥制备蛋白粉,研究谷氨酰胺转氨酶(TGase)及不同干燥方式对荞麦分离蛋白理化性质和凝胶特性的影响。结果表明,冷冻干燥荞麦分离蛋白(FBPI)的蛋白组成与BPI类似,而喷雾干燥荞麦分离蛋白(SBPI)的13S球蛋白发生降解。FBPI和SBPI的α-螺旋含量分别为22.10%和20.00%,β-转角含量为19.40%和19.80%,表明喷雾干燥会使蛋白结构更加无序化。SBPI的表面疏水性指数显著(P<0.05)高于FBPI与BPI。与BPI相比,SBPI具有更高的表面疏水性和更均匀的粒径,但溶解度和持水能力较低,而FBPI具有与BPI相似的物理化学性质。加入TGase后,FBPI和SBPI的平均粒径分别由213.01与192.55 nm增加至2289.01与1439.67 nm,表明发生了交联反应。BPI、FBPI和SBPI的电位分别为−15.93、−29.43、−29.35 mV,表明干燥处理能进一步提高蛋白的溶液稳定性。相比于SBPI,BPI和FBPI在升温过程中G'持续下降,表明热处理会破坏BPI和FBPI的蛋白凝胶结构。经加热处理再进行冷却,FBPI的G'显著(P<0.05)高于SBPI与BPI,具有更好的凝胶性。TGase能显著(P<0.05)提高FBPI的储能模量与热稳定性,但对SBPI作用不明显。化学作用力结果显示,疏水相互作用和二硫键是凝胶主要作用力;TGase能有效促进凝胶结构中疏水相互作用和二硫键形成,但会导致蛋白分子间氢键断裂。由此可见,通过冷冻干燥制备的荞麦蛋白能在TGase的作用下形成凝胶性与稳定性较好的凝胶。本研究的结果为荞麦分离蛋白凝胶特性研究及其凝胶类食品的开发与应用提供理论参考。Buckwheat protein isolate(BPI)was extracted from buckwheat(Fagopyrum esculentum Moench.)by alkali solubilization and acidic precipitation,following by spray-drying or vacuum freeze-drying to prepare protein powder.The effects of transglutaminase(TGase)and drying methods on physicochemical and gelling properties of buckwheat protein isolate were investigated.The results showed that the protein components of freeze-dried buckwheat protein isolate(FBPI)were similar to BPI,whereas the degradation of 13S globulin was observed in spray-dried buckwheat protein isolate(SBPI).Theα-helix contents of FBPI and SBPI were 22.10%and 20.00%,with correspondingβ-sheet contents of 19.40%and 19.80%respectively,indicating the transformation of disordered structure in BPI after spray-drying or vacuum freeze-drying.As compared with BPI,SBPI possessed the higher surface hydrophobicity and more uniform particle with a small size,but lower solubility and water holding capacity,while FBPI exhibited similar physicochemical properties to BPI.The average particle sizes of FBPI and SBPI increased from 213.01 and 192.55 nm to 2289.01 and 1439.67 nm after TGase addition respectively,which due to the intermolecular crosslinking reaction.The potentials of BPI,FBPI and SBPI were−15.93,−29.43 and−29.35 mV,respectively,suggesting that drying treatment could further improve the stability of protein solution.Compared with SBPI,G'of BPI and FBPI decreased continuously during the heating process,implied that the gel structures of BPI and FBPI could be destroyed by heating.After pretreatment by heating and then cooling down,FBPI showed a significantly(P<0.05)higher storage module than that of SBPI and BPI,indicating the better gelation.The addition of TGase could significantly(P<0.05)improve the storage modulus and thermal stability of FBPI,but had no significant effect on SBPI.Based on the results of chemical force analysis,it was speculated that the formation of gelation for buckwheat protein isolate was mainly attributed to hydrophobic interact

关 键 词：荞麦 分离蛋白 冷冻干燥 喷雾干燥 谷氨酰胺转氨酶(TGase) 凝胶特性 

分 类 号：TS210.1[轻工技术与工程—粮食、油脂及植物蛋白工程]