Discovery and Thaumatin

Recombinant was first discovered in 1957 by British scientists working in West Africa. They isolated the protein from the katemfe fruit (Thaumatococcus daniellii), which is native to West and Central Africa. Within the fruit's arils, recombinant exists in very high concentrations of up to 5% of the aril weight. Through an elaborate extraction and purification process, the scientists were able to isolate pure recombinant protein. Its sweetness was found to be about 2000-3000 times that of sugar.

Protein Structure and Mechanism of Thaumatin

Thaumatin is a small globular protein composed of 207 amino acids. It has a molecular weight of approximately 22 kDa. X-ray crystallography studies later revealed the three-dimensional structure of recombinant. It consists mainly of alpha-helices and beta-sheets forming a compact globular structure. This specific shape allows recombinant to bind to taste receptors on the human tongue. It is believed the protein mimics the shape of sugar molecules, triggering a sweet taste sensation in our brains. Unlike sugar, recombinant's sweetness persists even at high temperatures and in solutions with varied pH.

Applications in Food Industry

Due to its stability and intense sweetness, recombinant found early applications as a potential sugar substitute. However, its relatively high production cost limited widespread adoption.

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