Heating-Aided pH Shifting Modifies Hemp Seed Protein Structure, Cross-Linking, and Emulsifying Properties

• DOI: 10.1021/acs.jafc.8b03901
• Publication Date: 2018-09-24T18:21:05Z
• Authors: Qingling Wang; Yan Jin; Youling L. Xiong
• Keywords: Hot Temperature; Protein Conformation; Lysinoalanine; 04 agricultural and veterinary sciences; Hydrogen-Ion Concentration; Cross-Linking Reagents; 0404 agricultural biotechnology; Solubility; Seeds; Emulsions; Amino Acids; Particle Size; Hydrophobic and Hydrophilic Interactions; Cannabis; Plant Proteins

Alkaline pH12 shift treatment performed at varying temperatures (20-80 °C for 1, 5, and 60 min) was applied to structurally modify hemp seed protein isolate (HPI). The solubility of HPI (∼20%) remarkably improved ( p < 0.05) with elevating the temperature prolonging holding time, reaching 97.5% 80 min. treated exhibited a strong tendency forming soluble large aggregates. To limit lysinoalanine (LAL) production, heating methodically controlled 5 min, where LAL content never exceeded 100 mg/100 g loss cysteine lysine also minimal. emulsifying activity by this mild pH shift-heating combination as result dissociation subunits, unraveling tertiary structure, exposure hydrophobic groups. Moreover, emulsion formed maintained superior stability in particle size distribution during storage.