Title of article
Refolding the sweet-tasting protein thaumatin II from insoluble inclusion bodies synthesised in Escherichia coli
Author/Authors
Daniell، نويسنده , , Sarah and Mellits، نويسنده , , Kennneth H and Faus، نويسنده , , Ignacio and Connerton، نويسنده , , Ian، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2000
Pages
6
From page
105
To page
110
Abstract
A synthetic gene encoding the amino acid sequence of the strongly sweet-tasting protein thaumatin II has been expressed in Escherichia coli. The recombinant protein has been renatured from inclusion bodies using a reduced/oxidized glutathione system to yield a purified protein preparation that is indistinguishable from native thaumatin with respect to its biochemical, spectroscopic and organoleptic properties.
Keywords
protein refolding , Thiol/disulfide redox , Thaumatin , Sweet taste
Journal title
Food Chemistry
Serial Year
2000
Journal title
Food Chemistry
Record number
1949022
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