Selective Complex Coacervation of Pea Whey Proteins with Chitosan To Purify Main 2S Albumins.

Proteins of pea whey were separated by 1-D electrophoresis and 2-D electrophoresis and identified by MALDI-TOF/TOF-MS. In addition to lectin, pea albumin 2 (PA2) and pea albumin 1a (PA1a) were identified as the main 2S albumins. The complex behavior of pea whey proteins with chitosan as a function of pH and protein to polysaccharide ratio was studied by turbidimetric titration, zeta potential, and Tricine-SDS-PAGE. During pH titration, the zeta potential reveals that at maximum turbidity (pH), charge neutrality was fulfilled. The maximal protein recovery was obtained at a mass ratio of 1:1. After coacervation with chitosan, lectin was not involved in the formation of complexes and PA2 transferred into complex preferentially as compared to PA1a. The weak binding affinity and high hydrophilicity of PA1a made it selectively dissolve out from the PA2/PA1a complex at acidic pH conditions. After removal of chitosan and small molar weight peptides, high-purity PA2 and PA1a (>90% by SEC-HPLC) could be obtained. This work provides a novel strategy for the purification of proteins from a multiprotein pea whey system.