Purification and characterization of beta-glucosidase involved in the emission of 2-phenylethanol from rose flowers.
Beta-glucosidase was partially purified from Rosa 'Hoh-Jun' petals. The enzyme was highly specific for such beta-D-glucopyranosides as 2-phenylethyl beta-D-glucopyranoside. The optimal activity was observed at pH 6.0 and 35 degrees C. The enzymes were composed with two proteins (160 and 155 kDa) by blue native-PAGE, and were classified in a family 1 glucosidase based on LC-MS/MS analyses.
Sakai
Miwa
M
The United Graduate School of Agricultural Science, Gifu University (Shizuoka University), Ohya, Shizuoka, Japan.
Tomita
Saori
S
Hirata
Hiroshi
H
Asai
Tatsuo
T
Dohra
Hideo
H
Hara
Masakazu
M
Watanabe
Naoharu
N
D035264:Flowers / Q000201:enzymology*; D006001:Glycoconjugates / Q000378:metabolism; D007700:Kinetics; D010626:Phenylethyl Alcohol / Q000378:metabolism*; D010940:Plant Proteins / Q000302:isolation & purification / Q000378:metabolism; D027826:Rosa / Q000201:enzymology*; D013379:Substrate Specificity; D001617:beta-Glucosidase / Q000302:isolation & purification / Q000378:metabolism*
D006001:Glycoconjugates; D010940:Plant Proteins; D001617:beta-Glucosidase; D010626:Phenylethyl Alcohol