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谷氨酰胺转氨酶介导的荞麦蛋白-花生蛋白交联及其功能特性研究
引用本文:陈方圆,金建,蓝许诺. 谷氨酰胺转氨酶介导的荞麦蛋白-花生蛋白交联及其功能特性研究[J]. 中国粮油学报, 2024, 39(2): 104-112
作者姓名:陈方圆  金建  蓝许诺
作者单位:西南科技大学,西南科技大学,西南科技大学
基金项目:农业农村部杂粮加工重点实验室开放基金(2018CC14),国家自然科学基金(32001642)
摘    要:该文以谷氨酰胺转氨酶(TGase)为交联酶制剂,对荞麦蛋白与花生蛋白进行交联,通过单因素试验对两种蛋白的比例、总蛋白质浓度、TG酶添加量、交联温度、交联时间和pH进行了参数优化,并研究了最佳交联工艺条件下制备得到的交联产物的功能特性。结果表明,荞麦蛋白与花生蛋白的质量比1:1 (g:g)、总蛋白浓度4%、加酶量1.25%、反应温度40℃、反应时间120 min、pH 8.0时的交联反应效果最佳,交联度为63.1%。功能特性测定结果表明,与未交联的蛋白质相比,交联后的蛋白质的持水性、持油性和乳化稳定性有所提高,但乳化性、起泡性和起泡稳定性降低;在pH 3~12范围,交联蛋白质的溶解度逐渐升高,尤其在pI 4.0处,溶解度提高最为显著。

关 键 词:谷氨酰胺转氨酶;蛋白质交联;功能特性;荞麦蛋白;花生蛋白
收稿时间:2023-01-30
修稿时间:2023-06-03

Buckwheat Protein-peanut Protein Cross-linking induced by Transglutaminase and its Functional Properties
陈方圆,金建 and 蓝许诺. Buckwheat Protein-peanut Protein Cross-linking induced by Transglutaminase and its Functional Properties[J]. Journal of the Chinese Cereals and Oils Association, 2024, 39(2): 104-112
Authors:陈方圆  金建  蓝许诺
Abstract:This paper used glutamine transaminase (TGase) as a cross-linking enzyme preparation to cross-link buckwheat protein with peanut protein, and the parameters of the ratio of the two proteins, total protein concentration, TGase addition, The transglutaminase (TGase) was used to induce the cross-linking between buckwheat protein and peanut protein. Firstly, the parameters of the ratio of the two proteins, total protein concentration, TGasedosage, reaction temperature, cross-linking time, and pH were optimized through a single-factor test. Secondly, the cross-linking product was prepared under the optimum conditions, and its functional properties were studied. The results showed that the optimum cross-linking conditions for the crosslinking between buckwheat protein and peanut protein were a mass ratio of 1:1 (g:g), a total protein concentration of 4%, enzyme dosage of 1.25%, reaction temperature of 40 ℃, the reaction time of 120 min and pH 8.0, under which the degree of cross-linking was 63.1%. The results of functional properties showed that the water-holding capacity, oil-holding capacity, and emulsification stability of the cross-linked proteins were improved, However, the emulsification, foaming, and foaming stability were reduced compared with those of the uncross-linked proteins; the solubility of the cross-linked proteins gradually increased from pH 3 to 12, especially at pI 4.0, where the solubility increased most significantly; when compared with the uncross-linked protein.
Keywords:Glutamine transaminase   Protein cross-linking   Functional properties   Buckwheat protein   Peanut protein
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