J Agric Food Chem. 2009 Jun 24;57(12):5148-51.

Single-step purification of native miraculin using immobilized metal-affinity chromatography.

Duhita N, Hiwasa-Tanase K, Yoshida S, Ezura H.

Source

Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki, Japan.

Abstract

Miraculin is a taste-modifying protein that can be isolated from miracle fruit ( Richadella dulcifica ), a shrub native to West Africa. It is able to turn a sour taste into a sweet taste. The commercial exploitation of this sweetness-modifying protein is underway, and a fast and efficient purification method to extract the protein is needed. We succeeded in purifying miraculin from miracle fruit in a single-step purification using immobilized metal-affinity chromatography (IMAC). The purified miraculin exhibited high purity (>95%) in reverse-phase high-performance liquid chromatography. We also demonstrated the necessity of its structure for binding to the nickel-IMAC column.

PMID:: 19469504; [PubMed - indexed for MEDLINE]

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Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit. [J Biol Chem. 1988]
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