Amino acid compositions of avenins separated by reversed-phase high-performance liquid chromatography

The prolamins from wheat (gliadin), rye (secalin), barley (hordein) and oats (avenin) were extracted with 70% aqueous ethanol. Reversed-phase high-performance liquid chromatography (RP-HPLC) on C18-silica gel revealed clear differences in elution patterns. Crude avenin from the oat variety Flämingsregent was sepoarated by preparative scale RP-HPLC into thirty components. The amino acid compositions indicate that the first group of minor components (peaks 1–14) comprised non-avenin proteins. The second group (peaks 15–30) was the predominant group and corresponded to avenin proteins. These were classified into three subgroups differing mainly in the content of hydrophobic amino acids (Leu, Ile, Val, Phe). Within these groups, the avenins had similar compositions and differed only in the content of a few amino acids. Avenins appeared not to be related to the prolamins of other cereals on the basis of the amino acid composition data.