Adsorption at the air-water interface and emulsification properties of grain legume protein derivatives from pea and broad bean.
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.
Tsoukala
A
A
Laboratory of Food Chemistry and Technology, School of Chemistry, Aristotle University of Thessaloniki, GR-54124 Thessaloniki, Greece.
Papalamprou
E
E
Makri
E
E
Doxastakis
G
G
Braudo
E E
EE
D000327:Adsorption; D000388:Air; D001329:Autolysis; D004655:Emulsions; D031297:Lupinus / Q000737:chemistry*; D018532:Pisum sativum / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D031307:Vicia faba / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D004655:Emulsions; D010940:Plant Proteins; D014867:Water