Heat-Induced Soluble Protein Aggregates from Mixed Pea Globulins and β‑Lactoglobulin

• Published in: Journal of agricultural and food chemistry 2016-04, Vol.64 (13), p.2780-2791
• Main Authors: Chihi, Mohamed-Lazhar, Mession, Jean-luc, Sok, Nicolas, Saurel, Rémi
• Format: Article
• Language: English
• Subjects: Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Food engineering; Globulins - chemistry; Hot Temperature; Hydrophobic and Hydrophilic Interactions; Lactoglobulins - chemistry; Life Sciences; Pisum sativum - chemistry; Protein Aggregates - physiology; Whey Proteins - chemistry
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/acs.jafc.6b00087

The present work investigates the formation of protein aggregates (85 °C, 60 min incubation) upon heat treatment of β-lactoglobulin (βlg)–pea globulins (Glob) mixtures at pH 7.2 and 5 mM NaCl from laboratory-prepared protein isolates. Various βlg/Glob weight ratios were applied, for a total protein concentration of 2 wt % in admixture. Different analytical methods were used to determine the aggregation behavior of “mixed” aggregates, that is, surface hydrophobicity and also sulfhydryl content, protein interactions by means of SDS-PAGE electrophoresis, and molecule size distribution by DLS and gel filtration. The production of “mixed” thermal aggregates would involve both the formation of new disulfide bonds and noncovalent interactions between the denatured βlg and Glob subunits. The majority of “mixed” soluble aggregates displayed higher molecular weight and smaller diameter than those for Glob heated in isolation. The development of pea–whey protein “mixed” aggregates may help to design new ingredients for the control of innovative food textures.