Abstract
A membrane process for the recovery of ≥ 90 % of the soluble peptides (with antioxidant activity) found in concentrated lecithin-free egg yolk hydrolysates (LFEYH) was established. Hydrolysis of concentrated free lecithin egg yolk protein dispersions (10 and 20 %) was conducted with Alcalase 2.4L, an endoprotease from Bacillus Licheniformis. The obtained hydrolysates were fractionated by ultrafiltration (UF), where the effect of the membrane material and molecular weight cut-off (MWCO) was studied. Two flat sheet regenerated cellulose membranes and three tubular ceramic membranes with different MWCOs (50, 10 and 5kDa) were tested. Different hydrodynamic operating conditions were established in all membranes to work under sustainable flux during UF. The 50kDa ceramic membrane was found to be the most efficient in terms of flux (78.45 and 47.84kgm−2h-1 for 10 and 20 % protein dispersions, respectively) and showed lower fouling. The use of diafiltration (DF), allowed recovering more than 90 % of soluble and heat-stable peptides, which also showed high antioxidant activity, from hydrolysates produced in both concentrated (10 and 20 %) egg yolk protein dispersions.
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