Resolution of DL-amino acids on a native cellulose column and a plausible mechanism for their resolution.

We have studied the resolution of DL-amino acids on a native cellulose column. All the DL-amino acids related to protein and their 16 DNP-DL-amino acids were separated. The resolution capability depends mainly upon the bulkiness of the side group attached to the alpha-carbon, but also on structural and functional interaction of amino acid with cellulose. We propose a plausible resolution mechanism that is thought to be governed by a so-called key and lock relation between an amino acid and cellulose. Then, the affinity of each enantiomer for cellulose was calculated based on the resolution factor, which was known to be some 10(-2) -10(-3) eV.