An in vitro study was conducted to investigate the sensitivity of lactose-b
eta-lactoglobulin conjugates to beta-galactosidase from Kluyveromyces lacti
s. The hydrolysis was monitored by ion exchange chromatography. Compared to
free lactose or lactulose, which were rapidly hydrolysed, protein-bound la
ctose was not hydrolysed by beta-galactosidase even after an extended hydro
lysis time. Tryptic digestion of the conjugates before addition of beta-gal
actosidase improved the substrate accessibility and led to the release of a
bout 50% of the linked lactose. The results strongly suggest that the resis
tance of protein bound lactose is linked to the globular and compact struct
ure of lactose-beta-lactoglobulin conjugates. (C) 2000 Elsevier Science Ltd
. All rights reserved.