Neoculin as a new taste-modifying protein occurring in the fruit of Curculigo latifolia

• Published in: Bioscience, biotechnology, and biochemistry Vol. 68; no. 6; pp. 1403 - 1407
• Main Authors: Shirasuka, Y. (Tokyo Univ. (Japan)), Nakajima, K, Asakura, T, Yamashita, H, Yamamoto, A, Hata, S, Nagata, S, Abo, M, Sorimachi, H, Abe, K
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.06.2004; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: AMINO ACIDS; Base Sequence; Biological and medical sciences; Carbohydrate Sequence; CHEMICAL COMPOSITION; CLONING; Curculigo - chemistry; Curculigo latifolia; curculin; Dimerization; Fruit - chemistry; FRUITS; Fundamental and applied biological sciences. Psychology; Glycosylation; HYPOXIDACEAE; Molecular Sequence Data; neoculin; NUCLEOTIDE SEQUENCE; Plant Proteins - chemistry; Plant Proteins - isolation & purification; Plant Proteins - pharmacology; PROTEINS; SUGARS; SWEETNESS; TASTE (SENSATION); Taste - drug effects; taste modification; Malaysia; curculin; Curculigo latifolia; Fruit; taste modification; sweetness; Taste; neoculin; Protein
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.68.1403

A unique taste-modifying activity that converts the sense of sourness to the sense of sweetness occurs in the fruit of the plant Curculigo latifolia, intrinsic to West Malaysia. The active component, known as curculin, is a protein consisting of two identical subunits. We have found a new taste-modifying protein, named neoculin, of the same origin. Both chemical analysis and cDNA cloning characterized neoculin as a heterodimeric protein consisting of an acidic, glycosylated subunit of 113 amino acid residues and a basic subunit that is the monomeric curculin itself.