Purification and characterization of beta-glucosidase involved in the emission of 2-phenylethanol from rose flowers

Miwa Sakai; Saori Tomita; Hiroshi Hirata; Tatsuo Asai; Hideo Dohra; Masakazu Hara; Naoharu Watanabe

doi:10.1271/bbb.70404

Purification and characterization of beta-glucosidase involved in the emission of 2-phenylethanol from rose flowers

Biosci Biotechnol Biochem. 2008 Jan;72(1):219-21. doi: 10.1271/bbb.70404. Epub 2008 Jan 7.

Authors

Miwa Sakai¹, Saori Tomita, Hiroshi Hirata, Tatsuo Asai, Hideo Dohra, Masakazu Hara, Naoharu Watanabe

Affiliation

¹ The United Graduate School of Agricultural Science, Gifu University (Shizuoka University), Ohya, Shizuoka, Japan.

PMID: 18175907
DOI: 10.1271/bbb.70404

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Flowers / enzymology*
Glycoconjugates / metabolism
Kinetics
Phenylethyl Alcohol / metabolism*
Plant Proteins / isolation & purification
Plant Proteins / metabolism
Rosa / enzymology*
Substrate Specificity
beta-Glucosidase / isolation & purification
beta-Glucosidase / metabolism*

Substances

Glycoconjugates
Plant Proteins
beta-Glucosidase
Phenylethyl Alcohol