Refolding the sweet-tasting protein thaumatin II from insoluble inclusion bodies synthesised in Escherichia coli

Authors
Daniell, S Mellits, KH Faus, I Connerton, I
Citation
S. Daniell et al., Refolding the sweet-tasting protein thaumatin II from insoluble inclusion bodies synthesised in Escherichia coli, FOOD CHEM, 71(1), 2000, pp. 105-110
Citations number
23
Categorie Soggetti
Food Science/Nutrition
Journal title
FOOD CHEMISTRY
ISSN journal
03088146 → ACNP
Volume
71
Issue
1
Year of publication
2000
Pages
105 - 110
Database
ISI
SICI code
0308-8146(200010)71:1<105:RTSPTI>2.0.ZU;2-R
Abstract
A synthetic gene encoding the amino acid sequence of the strongly sweet-tas ting protein thaumatin II has been expressed in Escherichia coli. The recom binant protein has been renatured from inclusion bodies using a reduced/oxi dized glutathione system to yield a purified protein preparation that is in distinguishable from native thaumatin with respect to its biochemical, spec troscopic and organoleptic properties. (C) 2000 Elsevier Science Ltd. All r ights reserved.