PDF(Pubmed)
Abstract：
Plant-based protein is considered a sustainable protein source and has increased in demand recently. However, products containing plant-based proteins require further modification to achieve the desired functionalities akin to those present in animal protein products. This study aimed to investigate the effects of enzymes as cross-linking reagents on the physicochemical and functional properties of hybrid plant- and animal-based proteins in which lupin and whey proteins were chosen as representatives, respectively. They were hybridised through enzymatic cross-linking using two laccases (laccase R, derived from Rhus vernicifera and laccase T, derived from Trametes versicolor) and transglutaminase (TG). The cross-linking experiments were conducted by mixing aqueous solutions of lupin flour and whey protein concentrate powder in a ratio of 1:1 of protein content under the conditions of pH 7, 40 °C for 20 h and in the presence of laccase T, laccase R, or TG. The cross-linked mixtures were freeze-dried, and the powders obtained were assessed for their cross-linking pattern, colour, charge distribution (ζ-potential), particle size, thermal stability, morphology, solubility, foaming and emulsifying properties, and total amino acid content. The findings showed that cross-linking with laccase R significantly improved the protein solubility, emulsion stability and foaming ability of the mixture, whereas these functionalities were lower in the TG-treated mixture due to extensive cross-linking. Furthermore, the mixture treated with laccase T turned brownish in colour and showed a decrease in total amino acid content which could be due to the enzyme\'s oxidative cross-linking mechanism. Also, the occurrence of cross-linking in the lupin and whey mixture was indicated by changes in other investigated parameters such as particle size, ζ-potential, etc., as compared to the control samples. The obtained results suggested that enzymatic cross-linking, depending on the type of enzyme used, could impact the physicochemical and functional properties of hybrid plant- and animal-based proteins, potentially influencing their applications in food.
摘要：
基于植物的蛋白质被认为是可持续的蛋白质来源并且最近需求增加。然而,含有基于植物的蛋白质的产品需要进一步修饰以实现与动物蛋白质产品中存在的那些类似的所需功能。本研究旨在研究酶作为交联剂对以羽扇豆和乳清蛋白为代表的基于植物和动物的杂种蛋白的物理化学和功能特性的影响。分别。使用两种漆酶（漆酶R，来源于白菊和漆酶T，源自杂色Trametes）和转谷氨酰胺酶（TG）。交联实验是通过在pH7，40°C的条件下以1：1的蛋白质含量比例混合羽扇豆粉和乳清蛋白浓缩物粉末的水溶液进行的。在漆酶T的存在下，漆酶R,或TG。将交联的混合物冷冻干燥,并评估获得的粉末的交联模式，颜色,电荷分布(ζ电位)，颗粒大小,热稳定性，形态学,溶解度，发泡和乳化性能，和总氨基酸含量。结果表明，与漆酶R交联显著提高了蛋白质的溶解度，混合物的乳化稳定性和起泡能力，而这些官能团在TG处理的混合物中由于广泛的交联而较低。此外，用漆酶T处理的混合物变成褐色，总氨基酸含量下降，这可能是由于酶的氧化交联机制。此外，羽扇豆和乳清混合物中交联的发生通过其他研究参数的变化表明，如粒径，ζ-电位,等。,与对照样品相比。获得的结果表明，酶交联，根据使用的酶的类型，可能会影响基于植物和动物的杂种蛋白质的物理化学和功能特性，有可能影响它们在食品中的应用。
