LARGE-SCALE PURIFICATION OF RECOMBINANT MONELLIN FROM YEAST

Authors
KIM IH LIM KJ
Citation
Ih. Kim et Kj. Lim, LARGE-SCALE PURIFICATION OF RECOMBINANT MONELLIN FROM YEAST, Journal of fermentation and bioengineering, 82(2), 1996, pp. 180-182
Citations number
13
Categorie Soggetti
Food Science & Tenology","Biothechnology & Applied Migrobiology
Journal title
Journal of fermentation and bioengineering → ACNP
ISSN journal
0922338X
Volume
82
Issue
2
Year of publication
1996
Pages
180 - 182
Database
ISI
SICI code
0922-338X(1996)82:2<180:LPORMF>2.0.ZU;2-T
Abstract
Recombinant sweet-tasting monellin was purified on a large scale (50 g rams) from yeast strain ABI10. The purification yield was 45%, and the purity was as high as 95%, as determined by HPLC gel filtration. Sinc e monellin was proved to be a very basic protein (Cagan, R.: Science, 181, 32-35, 1973), the basicity was utilized as an efficient purificat ion method. Acid treatment for precipitating yeast proteins made prote ins denatured except monellin.