Genetic evidence indicates that only the beta-anomer of galactose is transported to Kluyveromyces lactis cells by galactose/glucose transporter Hgt1p, and that aldose-1-epimerase encoded by GAL10 is a prerequisite for growth on galactose. Minor aldose-1-epimerases other than Gal10p also exist in K. lactis. Using a mutant defective in both aldose-1-epimerases, we show by solid-state nuclear magnetic resonance spectroscopy that only beta-anomer is transported in the cell and stays without or with a slow rate of conversion to alpha-anomer. Signals due to intracellular beta-galactose appeared at two positions, both of which were shifted towards higher magnetic fields than that of beta-galactose in aqueous solution, suggesting that incorporated galactose binds to cellular components, probably proteins.