Towards absolute quantification of protein genetic variants in Pisum sativum extracts

Effect of Pea Legumin-to-Vicilin Ratio on the Protein Emulsifying Properties: Explanation in Terms of Protein Molecular and Interfacial Properties

“…Protein Isolation from Yellow Pea. PPC was prepared by alkaline extraction followed by iso-electric precipitation, as described by Vreeke et al 8 Whole frozen peas (Alimex) were broken with a pin mill (LV 15M Condux-Werk, Wolfgang bei Hanau, Germany) and subsequently milled (ZPS50 impact mill, Hosokawa-Alpine, Augsburg, Germany). The pea flour (10%, w/w) was suspended in Milli-Q water (MQ).…”

“…Fractionation from PPC. The PPC −20 was further fractionated to obtain PLF and PVF, as described by Vreeke et al 8 Defrosted PPC −20 was adjusted to pH 8.0 with NaOH and stirred for 1 h at 4 °C. The solution was subsequently diluted 1:1 with a McIlvaine buffer of pH 4.8, to a final concentration of 200 mM disodium phosphate and 100 mM citric acid containing 200 mM NaCl.…”

“…The emulsifying activity indices (EAI) determined for pea protein isolates (PPI), obtained with similar isolation methods and measured under similar conditions, range from 25 to 117 m 2 g –1 . − Can these differences be explained by the pea protein composition? The ratio between the main globular proteins in pea, legumin, and vicilin is known to vary from 66:33 to 10:90 (w/w) depending on the cultivar. − This study aims to determine the effect of the legumin-to-vicilin (L:V) ratio on the emulsifying properties by studying the emulsion droplet size ( d 3,2 ) as a function of protein concentration ( C p ) at pH 7.0. The experimental results were used to test if the recently developed model to predict the d 3,2 could be used to describe the emulsifying properties of the pea protein mixtures.…”