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Published on December 5, 2002; 10.1104/pp.102.011023

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Received July 16, 2002
Returned for revision August 27, 2002
Accepted September 19, 2002

Cloning of {beta}-Primeverosidase from Tea Leaves, a Key Enzyme in Tea Aroma Formation

Masaharu Mizutani *, Hidemitsu Nakanishi , Jun-ichi Ema , Seung-Jin Ma , Etsuko Noguchi , Misa Inohara-Ochiai , Masako Fukuchi-Mizutani , Masahiro Nakao , and Kanzo Sakata

Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan (M.M., H.N., J.-i.E., S.-J.M., E.N., K.S.); and Institute of Fundamental Research, Research Center, Suntory Ltd., Shimamoto-cho, Mishima-gun, Osaka 618-8503, Japan (M.I.-O., M.F.-M., M.N.)

* Corresponding author; email: mizutani{at}scl.kyoto-u.ac.jp.

A {beta}-primeverosidase from tea (Camellia sinensis) plants is a unique disaccharide-specific glycosidase, which hydrolyzes aroma precursors of {beta}-primeverosides (6-O-{beta}-D-xylopyranosyl-{beta}-D-glucopyranosides) to liberate various aroma compounds, and the enzyme is deeply concerned with the floral aroma formation in oolong tea and black tea during the manufacturing process. The {beta}-primeverosidase was purified from fresh leaves of a cultivar for green tea (C. sinensis var sinensis cv Yabukita), and its partial amino acid sequences were determined. The {beta}-primeverosidase cDNA has been isolated from a cDNA library of cv Yabukita using degenerate oligonucleotide primers. The cDNA insert encodes a polypeptide consisting of an N-terminal signal peptide of 28 amino acid residues and a 479-amino acid mature protein. The {beta}-primeverosidase protein sequence was 50% to 60% identical to {beta}-glucosidases from various plants and was classified in a family 1 glycosyl hydrolase. The mature form of the {beta}-primeverosidase expressed in Escherichia coli was able to hydrolyze {beta}-primeverosides to liberate a primeverose unit and aglycons, but did not act on 2-phenylethyl {beta}-D-glucopyranoside. These results indicate that the {beta}-primeverosidase selectively recognizes the {beta}-primeverosides as substrates and specifically hydrolyzes the {beta}-glycosidic bond between the disaccharide and the aglycons. The stereochemistry for enzymatic hydrolysis of 2-phenylethyl {beta}-primeveroside by the {beta}-primeverosidase was followed by 1H-nuclear magnetic resonance spectroscopy, revealing that the enzyme hydrolyzes the {beta}-primeveroside by a retaining mechanism. The roles of the {beta}-primeverosidase in the defense mechanism in tea plants and the floral aroma formation during tea manufacturing process are also discussed.




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