Tsoukala A, Papalamprou E, Makri E, Doxastakis G, Braudo E E
Laboratory of Food Chemistry and Technology, School of Chemistry, Aristotle University of Thessaloniki, GR-54124 Thessaloniki, Greece.
Colloids Surf B Biointerfaces. 2006 Dec 1;53(2):203-8. doi: 10.1016/j.colsurfb.2006.08.019. Epub 2006 Sep 3.
Functional properties of native and modified (through induced autolysis) pea (Pisum sativum L.) and broad bean (Vicia faba L.) protein derivatives are studied. In specific, protein solubility and behavior at the air-water interface through surface pressure measurements are investigated. Furthermore the ability of the protein products to act as emulsifying agents and to stabilize emulsions is studied through oil droplet size distribution measurements and by the protein adsorbed at the oil-water interface. The data reveal that the ability of the proteins to act as surfactants and build up a rigid film around the oil droplets, mainly depends on their suitable molecular configuration and structure. Hydrolysis did not promote the functionality of the legume proteins. Broad bean exhibited better functionality than pea, before and after hydrolysis. Some comparisons were also made with lupin (Lupinus albus L.) protein isolate.
研究了天然和改性（通过诱导自溶）豌豆（Pisum sativum L.）和蚕豆（Vicia faba L.）蛋白质衍生物的功能特性。具体而言，通过表面压力测量研究了蛋白质在空气-水界面的溶解性和行为。此外，通过油滴尺寸分布测量以及吸附在油水界面的蛋白质，研究了蛋白质产品作为乳化剂和稳定乳液的能力。数据表明，蛋白质作为表面活性剂并在油滴周围形成刚性膜的能力，主要取决于其合适的分子构型和结构。水解并未促进豆类蛋白质的功能。水解前后，蚕豆的功能均优于豌豆。还与羽扇豆（Lupinus albus L.）分离蛋白进行了一些比较。
