Cloning of the Thaumatin I cDNA and Characterization of Recombinant Thaumatin I Secreted by Pichia pastoris

他马汀 毕赤酵母 互补DNA 肽序列 核酸序列 生物 生物化学 氨基酸 重组DNA 分子生物学 基因
作者
Nobuyuki Ide,Ryosuke Kaneko,Ritsuko Wada,Alka Mehta,Satoshi Tamaki,Teiji Tsuruta,Yuki Fujita,Tetsuya Masuda,Naofumi Kitabatake
出处
期刊:Biotechnology Progress [Wiley]
被引量:12
标识
DOI:10.1021/bp070072v
摘要

Thaumatin is a sweet-tasting protein comprising a mixture of some variants. The major variants are thaumatins I and II. Although the amino acid sequence of thaumatin I was known and the nucleotide sequence of cDNA of thaumatin II was elucidated, the nucleotide sequence of thaumatin I has been controversial. We have cloned two thaumatin cDNAs from the fruit of Thaumatococcus daniellii Benth. One is the same nucleotide sequence as that of thaumatin II already reported, and the other is a novel nucleotide sequence. The amino acid sequence deduced from the novel cDNA was the same amino acid sequence as that of thaumatin I, the only exception being the residue at position 113 (Asp instead of Asn), indicating that the novel thaumatin cDNA is that for thaumatin I. This thaumatin I cDNA was transformed into Pichia pastoris X-33, and the recombinant thaumatin I expressed was purified and characterized. The threshold value of sweetness of the recombinant thaumatin I was the same as that of the plant thaumatin I, although several unexpected amino acid residues were attached to the N-terminal of the recombinant thaumatin I. These indicate that the N-terminal portion of thaumatin is not critical for the elicitation of sweetness.
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