Improving the functionality of pea protein with laccase-catalyzed crosslinking mediated by chlorogenic acid.

The influences of laccase-catalyzed crosslinking on the structural, emulsifying and gelling properties of pea protein with chlorogenic acid were intensively probed. Molecular weight analysis illustrated the formation of pea protein aggregates by laccase-induced polymerization in the presence of chlorogenic acid and the increase of incubation time facilitated the aggregation. Particle size of pea protein-laccase-chlorogenic acid progressively enhanced increasing incubation time. Laccase-induced polymerization possessed remarkable impacts on the secondary and tertiary structure of pea protein, confirmed by circular dichroism, and fluorescence spectroscopy. Surface hydrophobicity of pea protein appreciably enhanced with laccase-induced crosslinking due to the exposure of interior hydrophobic amino acid residues. Emulsifying activity, emulsifying capacity, gel strength, and water-holding capacity of pea protein can be considerably enhanced with laccase-catalyzed crosslinking with chlorogenic acid, suggesting excellent functionalities for pea protein were accomplished after being modified by laccase with chlorogenic acid. The obtained information will widen pea protein's application in food systems.