Ultrafiltration to fractionate wheat polypeptides

• Published in: Journal of chromatography. B, Biomedical sciences and applications Vol. 753; no. 1; pp. 29 - 35
• Main Authors: Berot, S, Popineau, Y, Compoint, J.-P, Blassel, C, Chaufer, B
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Amsterdam Elsevier B.V 25.03.2001; Elsevier Science
• Subjects: Analysis; Biological and medical sciences; Chromatography, Gel; General pharmacology; Medical sciences; Peptides - isolation & purification; Pharmacology. Drug treatments; Polypeptides; Spectrophotometry, Ultraviolet; Triticum - chemistry; Ultrafiltration; Ultrafiltration; Polypeptides; Wheat; Gluten; Separation method; Reversed phase chromatography; Foaming; Polypeptide; Gliadin; Ion exchange chromatography
• DOI: 10.1016/S0378-4347(00)00418-7
• ISSN: 0378-4347; 1387-2273

An ultrafiltration process allowing the fractionation of two kinds of polypeptides issued from limited chymotryptic hydrolysis of wheat gliadins was applied to wheat gluten hydrolysates. Hydrophilic and poorly charged polypeptides were well transmitted through an inorganic ZrO 2-based membrane at acidic pH, whereas hydrophobic and positively charged polypeptides were highly retained. By combining reversed-phase and cation-exchange chromatography (CEC), it was proved that the fractionation of the polypeptides was based on electrostatic repulsion of the charged polypeptides by the positively charged membrane. After a continuous diafiltration process, retentates containing 75 to 88% of hydrophobic polypeptide and permeates containing 84 to 90% of hydrophilic polypeptides were recovered, depending on the size of membrane used. Even if the ultrafiltration fractions were less purified than fractions issued from CEC, it was shown that they exhibited very different foaming properties: permeate did not produce nor stabilize foams, whereas retentate was more efficient than the whole hydrolysates and BSA.