Functional properties of enzymatically modified high-protein sesame meal extracts as a natural food emulsifier
Jung-Min Noh, Shin‐Joung Rho, Yong‐Ro Kim
Abstract
This study investigated the potential of enzymatically high-protein sesame meal extracts (SME) as natural emulsifiers. SME, extracted from sesame meal pellets (SMP), was enzymatically treated with papain (PP), a hydrolyzing enzyme, and transglutaminase (TG), a cross-linking enzyme, to produce enzyme-modified SME (SME-PP and SME-TG). SME-PP had reduced particle size and enhanced SDS-PAGE band intensity below 17 kDa, while SME-TG exhibited increased particle size with new high-molecular-weight bands. Among enzyme-treated samples, SME-PP1 (30 U/mg PP) demonstrated a 3.56-fold and 1.73-fold increase in emulsifying activity index (EAI), and 1.69- and 2.30-fold increases in emulsion stability index (ESI) compared to SME and WPI control, respectively, which could be related to increases in solubility and surface hydrophobicity. Also, SME-TG2 (20 U/g TG) showed 2.96- and 1.43-fold increases in EAI compared to SME and WPI, respectively, possibly due to improved interfacial activity induced by protein cross-linking. Oil-in-water nanoemulsions prepared using SME-PP1 and SME-TG2 showed creaming index (CI) values similar to WPI over 28 days. After 28 days of storage, SME-PP1- and SME-TG2-stabilized emulsions maintained significantly smaller droplet sizes (261.50 d nm and 290.33 d nm, respectively) compared to WPI (309.57 d nm). Overall, SME-PP1 and SME-TG2 demonstrated excellent performance in terms of emulsifying activity and emulsion stability comparable to WPI, suggesting that enzyme-modified SME could be a promising plant-based emulsifier, providing sustainable and eco-friendly options for food applications. • Enzyme-treated high-protein sesame meal extracts (SME) was produced. • Surface hydrophobicity and solubility of SME increased with papain treatment. • Transglutaminase treatment improved the emulsifying properties of SME. • Enzyme-modified SME showed emulsion stability comparable to that of WPI.