Conditions have been created for the isolation of the chimeric protein Alburonl6 (human albumin-interferon-alpha 16) from a culture medium of the yeast Pichia pastoris, under which there is no aggregation of the protein and its biological activity is maintained. The proposed scheme can be used for the isolation and purification of a chimeric protein in laboratory conditions. The obtained results may be useful for improving the purification methods of various recombinant proteins synthesized and secreted by the yeast P. pastoris.