Journal
FOOD SCIENCE AND TECHNOLOGY RESEARCH
Volume 16, Issue 6, Pages 585-592Publisher
KARGER
DOI: 10.3136/fstr.16.585
Keywords
thaumatin; sweet-tasting protein; sweetness; Pichia pastoris; pre-sequence; fermenter
Categories
Funding
- Japan Society for Promotion of Science [19780074]
- Japan Food Chemical Research Foundation
- Grants-in-Aid for Scientific Research [19780074, 22580105] Funding Source: KAKEN
Ask authors/readers for more resources
Thaumatin, an intensely sweet-tasting protein used as a sweetener, was secreted by the methylotrophic yeast Pichia pastoris. Approximately 100 mg L-1 of recombinant thaumatin I was obtained using an expression vector which possesses three copies of the thaumatin gene containing the 22-amino acid pre-sequence. Expression yield was about three-fold higher than when the a-factor secretion signal from Saccharomyces cerevisiae was used. The circular dichroism and tryptophan fluorescence spectra for recombinant thaumatin I were almost the same as those for plant thaumatin. Large amounts of homogeneous recombinant thaumatin allowed for preparation of high-quality crystals in the presence of cryoprotective glycerol used in high-resolution x-ray structural analysis to help further understand the perception of the sweet taste of thaumatin.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available