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| Content Provider | PubMed Central |
|---|---|
| Author | Mizutani, Masaharu Nakanishi, Hidemitsu Ema, Jun-ichi Ma, Seung-jin Noguchi, Etsuko Misa, Inohara-ochiai Masako, Fukuchi-mizutani Nakao, Masahiro Sakata, Kanzo |
| Copyright Year | 2002 |
| Abstract | A β-primeverosidase from tea (Camellia sinensis) plants is a unique disaccharide-specific glycosidase, which hydrolyzes aroma precursors of β-primeverosides (6-O-β-d-xylopyranosyl-β-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 β-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 β-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 β-primeverosidase protein sequence was 50% to 60% identical to β-glucosidases from various plants and was classified in a family 1 glycosyl hydrolase. The mature form of the β-primeverosidase expressed in Escherichia coli was able to hydrolyze β-primeverosides to liberate a primeverose unit and aglycons, but did not act on 2-phenylethyl β-d-glucopyranoside. These results indicate that the β-primeverosidase selectively recognizes the β-primeverosides as substrates and specifically hydrolyzes the β-glycosidic bond between the disaccharide and the aglycons. The stereochemistry for enzymatic hydrolysis of 2-phenylethyl β-primeveroside by the β-primeverosidase was followed by 1H-nuclear magnetic resonance spectroscopy, revealing that the enzyme hydrolyzes the β-primeveroside by a retaining mechanism. The roles of the β-primeverosidase in the defense mechanism in tea plants and the floral aroma formation during tea manufacturing process are also discussed. |
| Related Links | http://dx.doi.org/10.1104/pp.102.011023 |
| Ending Page | 2176 |
| Page Count | 13 |
| Starting Page | 2164 |
| File Format | |
| ISSN | 00320889 |
| e-ISSN | 15322548 |
| Journal | Plant Physiology |
| Issue Number | 4 |
| Volume Number | 130 |
| Language | English |
| Publisher | American Society of Plant Biologists |
| Publisher Date | 2002-12-01 |
| Access Restriction | Open |
| Rights Holder | American Society of Plant Biologists |
| Subject Keyword | Plant Science Genetics Physiology Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Physiology Plant Science |
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