Structural and rheology properties of pea protein isolate-stabilised emulsion gel: Effect of crosslinking with transglutaminase
Structural and rheology properties of pea protein isolate-stabilised emulsion gel: Effect of crosslinking with transglutaminase
复制标题
豌豆分离蛋白稳定乳液凝胶的结构和流变特性：转谷氨酰胺酶交联的影响
DOI：
10.1111/ijfs.15446
复制
发表时间：
--
影响因子：
3.3
通讯作者：
Chen Yijie
中科院分区：
文献类型：
--
作者：
Zhan Fuchao;Tang Xiaomin;Sobhy Remah;Li Bin;Chen Yijie
研究了不同含油率（φ，20%~50%）的转谷氨酰胺酶（TGase）法制备豌豆分离蛋白（PPI）乳状液凝胶的微观结构和特性（持水性和流变性）。结果表明，PPI乳液凝胶的保水性和凝胶强度（储能模量）随φ的增大而增大。同时，由于酶处理，网络中包埋的蛋白质逐渐增加，导致乳液凝胶的内部结构更加紧密。在高油重量分数（例如50%）下，乳液的网络本质上是粗颗粒链，主要形成“紧密结合”的油滴。因此，凝胶化机理与体系中蛋白质的状态有关，分为吸附在界面上的蛋白质和未吸附的蛋白质。这一结果对理解凝胶化过程和酶固定蛋白质乳液凝胶的理论有重要的帮助。
The microstructures and characteristics (water holding capacity (WHC) and rheological properties) of pea protein isolate (PPI) emulsion gels produced via transglutaminase (TGase) with different oil‐weight fractions (φ, 20%~50%) were studied in the present work. The results showed that the WHC and gel strength (storage modulus) of PPI emulsion gel were raised with increasing of φ. Simultaneously, the proteins entrapped within the network gradually increase due to the enzymatic treatment, which resulted in a tighter internal structure of emulsion gel. At high oil‐weight fractions (e.g. 50%), the network of the emulsion was essentially a coarse chain of particulate, mainly forming a ‘close‐knit’ oil droplet. Therefore, the gelation mechanism is related to the state of proteins in the system, which are divided into proteins adsorbed and unadsorbed on the interface. The results will be of significant assistance in comprehending the theories of the gelation process and the protein emulsion gels immobilisation by the enzyme.