Perilla protein isolate exhibits synergistic techno-functionality through modification via sequential dynamic high-pressure microfluidization and enzymatic hydrolysis

Abstract

Modification of proteins derived from plant sources is crucial for enabling their versatile applications in the food industry. In the present study, structural and functional properties of individual treated perilla protein isolate (PPI) through dynamic high-pressure microfluidization (DHPM) and enzymatic hydrolysis (EH) was compared with their sequential (DHPM-EH) treatment. Native PPI thick, sharp-edged blocks transformed into a collapsed structure with wrinkles after sequential (DHPM-EH) treatment. The synergistic effect between DHPM and EH, during sequential (DHPM-EH) treatment caused greater reduction (91.9%) in PPI particle size as compared to DHPM (87.3%), and EH (84.5%), which enhanced PPI solubility, even at low pH. Above treatments altered the conformational structure of PPI as evident from changes in surface hydrophobicity, free –SH groups conversion into –SS bonds, ultraviolet absorption and fluorescence intensities changes, and decreased α-helix, while increased β-sheets. The sequential (DHPM-EH) treated PPI showed enhanced foaming capacity (×3.59), as well as increased thermal and colloidal stability.