3.2.1.168: hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase
This is an abbreviated version!
For detailed information about hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.168
-
3.2.1.168
-
diglycosidase
-
flavonoid
-
transglycosylation
-
glycoside
-
rutinose
-
hydrolyse
-
juice
-
aglycone
-
acremonium
-
citrus
-
sinensis
-
mandatory
-
orange
-
food industry
-
quercetin
-
deglycosylation
-
fagopyrum
-
niger
-
rutinosides
-
utilises
-
biotechnology
- 3.2.1.168
-
diglycosidase
- flavonoid
-
transglycosylation
- glycoside
- rutinose
-
hydrolyse
- juice
-
aglycone
- acremonium
-
citrus
-
sinensis
-
mandatory
- orange
- food industry
- quercetin
-
deglycosylation
- fagopyrum
- niger
- rutinosides
-
utilises
- biotechnology
Reaction
Synonyms
6-O-alpha-rhamnosyl-beta-glucosidase, alpha-rhamnosyl-beta-glucosidase, alphaRbetaG, AMIS_8220, hesperidin deglycosylase, rutinase, rutinoside transferase
ECTree
Advanced search results
Application
Application on EC 3.2.1.168 - hesperidin 6-O-alpha-L-rhamnosyl-beta-D-glucosidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
biotechnology
-
bulk biotransformations, the hydrolytic and transglycosidic activity of alpha-rhamnosyl-beta-glucosidase has potential use for industrial processing of plant-based food and the products of the transglycosylation products could play a role as starting materials for the development of new drugs. The immobilization allows the kinetic control of the process
food industry
additional information
-
herperidin occurs in lemons and oranges in high concentrations and contributes to juice clouding. Enzymatic hydrolysis via the diglycosidase is useful to remove the unpleasant taste or for juice clarification, a deglycosylation (hydrolysis and transglycosylation) in a single step
food industry
-
potential use of the enzyme for biotechnoligical applications, e.g. in aroma modulation of fermented foods
rutinose-containing glycoconjugates are resistant to hydrolysis in human tissues because of the absence of rutinoside-attacking glycosidases such as rhamnosidases or alpha-L-rhamnosyl-beta-D-glucosidases. Thus, rutinose-capped HQ may offer an additional advantage over other hydroquinone (HQ)-containing glycoconjugates in that it may be less prone to enzymatic degradation than, for example, glucosylated HQ when applied to human skin. Moreover, rutinosides have potential applications as food additives and antiviral agents
additional information
-
rutinose-containing glycoconjugates of phenolics might have antiviral activity and by useful as therapeutics/antiviral agents