双频超声场下花生和荞麦蛋白质在转谷氨酰胺酶介导下的交联:功能属性研究

Xuan Zhang , Yu Chen , Yu Hu , Jian Jin , Hui lin Shen , Chibuike C. Udenigwe
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摘要

开发了双频超声(DFU)场下转谷氨酰胺酶(TGase)交联的花生蛋白(PP)/荞麦蛋白(BWP)混合物,并对其结构和功能特性进行了表征。结果表明,PP-BWP 交联的最佳双频超声参数为 25 kHz/40 kHz 双频超声工作时间比 10:10(s/s)、温度 45°C、超声功率密度 125 W/L、持续时间 30 min,交联度(DC)为 37.7%,比对照组高 125%。与不使用超声波的蛋白质聚合体(TG-PP-BWP)相比,蛋白质聚合体(在双频超声波下用 TGase 交联的花生蛋白-荞麦蛋白,U-TG-PP-BWP)在 pH 7.0 下的溶解度、持油能力和乳化能力显著提高(P<0.05),但乳液稳定性、发泡能力和形态稳定性有所下降。二级结构分析表明,未交联蛋白质与 U-TG-PP-BWP 之间无明显差异。与 TG-PP-BWP 相比,超声处理后 U-TG-PP-BWP 的 α-螺旋减少了 11.2%,β-片、β-匝和无规线圈分别增加了 7.7%、3.4% 和 4.7%。微观结构显示,U-TG-PP-BWP 形成了具有许多微孔的层状结构,而 TG-PP-BWP 则聚集成紧密的大块。SDS-PAGE 分析表明,与 PP 和 BWP 相比,交联的 TG-PP-BWP 和 U-TG-PP-BWP 的亚基条带在 14.4-116 kDa 处发生了变化,生成的蛋白质大于 116 kDa,表明这两种蛋白质发生了共价交联。总之,DFU 可以促进蛋白质的酶促交联,为开发新型植物蛋白提供了一种新方法。
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Transglutaminase mediated cross-linking of peanut and buckwheat proteins under dual-frequency ultrasound field: Functional attributes study

Peanut protein (PP)/buckwheat protein (BWP) mixture crosslinked by transglutaminase (TGase) under dual-frequency ultrasound (DFU) field was developed and its structural and functional properties were characterized. The results showed that the optimal DFU parameters for PP-BWP crosslinking were 25 kHz/40 kHz dual-frequency ultrasound working time ratio of 10:10 (s/s), a temperature of 45°C, ultrasonic power density of 125 W/L and time duration of 30 min, resulting in the degree of crosslinking (DC) of 37.7 %, which is 125 % higher than that of the control. The solubility at pH 7.0, oil-holding capacity, and emulsifying capacity of the protein aggregate (peanut protein-buckwheat protein crosslinked by TGase under dual-frequency ultrasound, U-TG-PP-BWP) was significantly (P<0.05) improved compared with protein aggregates formed without ultrasound (TG-PP-BWP); however, the emulsion stability, foaming capacity and form stability decreased. Secondary structure analysis indicated no apparent difference between un-crosslinked protein and U-TG-PP-BWP. After ultrasound treatment, the α-helix decreased by 11.2 % and the β-sheet, β-turn and random coil increased by 7.7 %, 3.4 % and 4.7 %, respectively, in U-TG-PP-BWP compared to TG-PP-BWP. The microstructures showed that U-TG-PP-BWP formed a lamellar structure with many micropores while TG-PP-BWP aggregated into large and tight blocks. SDS-PAGE analysis showed that, compared to PP and BWP, the subunit bands of cross-linked TG-PP-BWP and U-TG-PP-BWP were altered at 14.4–116 kDa, yielding proteins larger than 116 kDa, suggesting covalent cross-linking of the two proteins. In conclusion, the enzymatic cross-linking of proteins can be promoted by DFU, providing a new approach to developing novel plant proteins.

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