Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin |
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| Authors: | S Theerasilp H Hitotsuya S Nakajo K Nakaya Y Nakamura Y Kurihara |
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| Affiliation: | Department of Chemistry, Faculty of Education, Yokohama National University, Japan. |
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| Abstract: | The taste-modifying protein, miraculin, has the unusual property of modifying sour taste into sweet taste. The complete amino acid sequence of miraculin purified from miracle fruits by a newly developed method (Theerasilp, S., and Kurihara, Y. (1988) J. Biol. Chem. 263, 11536-11539) was determined by an automatic Edman degradation method. Miraculin was a single polypeptide with 191 amino acid residues. The calculated molecular weight based on the amino acid sequence and the carbohydrate content (13.9%) was 24,600. Asn-42 and Asn-186 were linked N-glycosidically to carbohydrate chains. High homology was found between the amino acid sequences of miraculin and soybean trypsin inhibitor. |
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