Purification of glycomacropeptide from non-dialyzable fraction of sweet whey by anion-exchange chromatography

Authors
Nakano, T Ozimek, L
Citation
T. Nakano et L. Ozimek, Purification of glycomacropeptide from non-dialyzable fraction of sweet whey by anion-exchange chromatography, BIOTECH TEC, 13(11), 1999, pp. 739-742
Citations number
11
Categorie Soggetti
Biotecnology & Applied Microbiology
Journal title
BIOTECHNOLOGY TECHNIQUES
ISSN journal
0951208X → ACNP
Volume
13
Issue
11
Year of publication
1999
Pages
739 - 742
Database
ISI
SICI code
0951-208X(199911)13:11<739:POGFNF>2.0.ZU;2-L
Abstract
Glycomacropeptide (GMP) was purified from non-dialyzable fraction of sweet whey by anion-exchange chromatography on DEAE-Sephacel at two pHs 6.4 and 3 .0. Chromatography at pH 3.0 (but not pH 6.4) gave a GMP fraction of high p urity with its yield (1 g from every litre of whey) being approximately 100 times higher than that shown in the previous report. It was concluded that DEAE-Sephacel chromatography at pH 3.0 is a simple useful method to separa te GMP from most whey proteins. It may be applicable to a large scale produ ction of GMP.