88510-09-2Relevant academic research and scientific papers
Substrate specificity of beta-primeverosidase, a key enzyme in aroma formation during oolong tea and black tea manufacturing.
Ma,Mizutani,Hiratake,Hayashi,Yagi,Watanabe,Sakata
, p. 2719 - 2729 (2007/10/03)
We synthesized nine kinds of diglycosides and a monoglycoside of 2-phenylethanol to investigate the substrate specificity of the purified beta-primeverosidase from fresh leaves of a tea cultivar (Camellia sinensis var. sinensis cv. Yabukita) in comparison with the apparent substrate specificity of the crude enzyme extract from tea leaves. The crude enzyme extract mainly showed beta-primeverosidase activity, although monoglycosidases activity was present to some extent. The purified beta-primeverosidase showed very narrow substrate specificity with respect to the glycon moiety, and especially prominent specificity for the beta-primeverosyl (6-O-beta-D-xylopyranosyl-beta-D-glucopyranosyl) moiety. The enzymes hydrolyzed naturally occurring diglycosides such as beta-primeveroside, beta-vicianoside, beta-acuminoside, beta-gentiobioside and 6-O-alpha-L-arabinofuranosyl-beta-D-glucopyranoside, but were unable to hydrolyze synthetic unnatural diglycosides. The purified enzyme was inactive toward 2-phenylethyl beta-D-glucopyranoside. The enzyme hydrolyzed each of the diglycosides into the corresponding disaccharide and 2-phenylethanol. These results indicate the beta-primeverosidase, a diglycosidase, to be a key enzyme involved in aroma formation during the tea manufacturing process.
Synthesis and n.m.r. spectral properties of grape monoterpenyl glycosides
Voirin, Stephane,Baumes, Raymond,Bayonove, Claude,M'Bairaroua, Oubadjim,Tapiero, Claude
, p. 39 - 56 (2007/10/02)
Several grape 6-O-(6-deoxy-α-L-mannopyranosyl)-β-D-glucopyranosides and 6-O-α-L-arabinofuranosyl-β-D-glucopyranosides having (E)- and (Z)-3,7-dimethyl-2,6-octadien-1-yl, (R,S)-3,7-dimethyl-1,6-octadien-3-yl, (R,S)-1-methyl-1-(4-methyl-3-cyclohexen-1-yl)et
