Resistance of beta-lactoglobulin-bound lactose to the hydrolysis by beta-galactosidase

Citation
F. Morgan et al., Resistance of beta-lactoglobulin-bound lactose to the hydrolysis by beta-galactosidase, INT DAIRY J, 9(11), 1999, pp. 813-816
Citations number
10
Categorie Soggetti
Food Science/Nutrition
Journal title
INTERNATIONAL DAIRY JOURNAL
ISSN journal
09586946 → ACNP
Volume
9
Issue
11
Year of publication
1999
Pages
813 - 816
Database
ISI
SICI code
0958-6946(1999)9:11<813:ROBLTT>2.0.ZU;2-8
Abstract
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.