Any feedback?
Information on EC 3.2.1.206 - oleuropein beta-glucosidase
for references in articles please use BRENDA:EC3.2.1.206Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.206 oleuropein beta-glucosidaseIUBMB Comments
Oleuropein is a glycosylated secoiridoid exclusively biosynthesized by members of the Oleaceae plant family where it is part of a defence system againt herbivores. The enzyme also hydrolyses ligstroside and demethyloleuropein.
Specify your search results
Word Map
- 3.2.1.206
-
gaucher
-
secoiridoids
- olive
-
planta
- europaea
- beta-d-fucosidase
-
deglycosylated
- taurocholate
- glucosylceramide
- triton
-
two-component
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
oeglu, soluble beta-glucosidase, oleuropein-specific beta-glucosidase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GLU
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oleuropein + H2O = oleuropein aglycone + D-glucopyranose
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
oleuropein 2-beta-D-glucohydrolase
Oleuropein is a glycosylated secoiridoid exclusively biosynthesized by members of the Oleaceae plant family where it is part of a defence system againt herbivores. The enzyme also hydrolyses ligstroside and demethyloleuropein.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
the enzyme is 200fold less active against 4-nitrophenyl-beta-D-glucopyranoside than oleuropein
-
-
?
5-bromo-4-chloro-3-indolyl beta-D-glucopyranoside + H2O
5-bromo-4-chloro-3-indolol + D-glucose
-
-
-
-
?
5-bromo-4-chloro-3-indolyl-beta-D-glucopyranoside + H2O
5-bromo-4-chloro-1H-indol-3-ol + D-glucopyranose
apigenin 7-O-beta-D-glucopyranoside + H2O
apigenin + D-glucose
-
1% activity compared to oleuropein
-
-
?
demethyloleuropein + H2O
(2R,3E,4S)-4-[2-[2-(3,4-dihydroxyphenyl)ethoxy]-2-oxoethyl]-3-ethylidene-2-hydroxy-3,4-dihydro-2H-pyran-5-carboxylic acid + D-glucose
-
21% activity compared to oleuropein
-
-
?
demethyloleuropein + H2O
?
15.6% activity compared to oleuropein
-
-
?
demethyloleuropein + H2O
demethyloleuropein aglycone + D-glucopyranose
-
-
-
-
?
ligstroside + H2O
ligstroside aglycone + D-glucopyranose
25.6% activity compared to oleuropein
-
-
?
ligstroside + H2O
methyl (2R,3E,4S)-3-ethylidene-2-hydroxy-4-[2-[2-(4-hydroxyphenyl)ethoxy]-2-oxoethyl]-3,4-dihydro-2H-pyran-5-carboxylate + D-glucose
-
65.4% activity compared to oleuropein
-
-
?
luteolin 7-O-beta-D-glucopyranoside + H2O
luteolin + D-glucose
-
0.2% activity compared to oleuropein
-
-
?
oleuropein + H2O
aldehydic forms of oleuropein aglycone + beta-D-glucose
-
-
-
-
?
oleuropein + H2O
oleuropein agylcone + D-glucopyranose
-
-
products are monoaldehydic forms of oleuropein aglycone, hydroxytyrosol, elenolic acid, and D-glucopyranose. The mix of diastereomers of the monoaldehydic form of oleuropein aglycone, is identified as (5S,8R,9S)-, (5S,8S,9S)- and (5S,8R,9R)
-
?
5-bromo-4-chloro-3-indolyl-beta-D-glucopyranoside + H2O
5-bromo-4-chloro-1H-indol-3-ol + D-glucopyranose
-
-
-
-
?
5-bromo-4-chloro-3-indolyl-beta-D-glucopyranoside + H2O
5-bromo-4-chloro-1H-indol-3-ol + D-glucopyranose
-
-
-
-
?
5-bromo-4-chloro-3-indolyl-beta-D-glucopyranoside + H2O
5-bromo-4-chloro-1H-indol-3-ol + D-glucopyranose
-
-
-
-
?
5-bromo-4-chloro-3-indolyl-beta-D-glucopyranoside + H2O
5-bromo-4-chloro-1H-indol-3-ol + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + beta-D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + beta-D-glucopyranose
-
-
byproductas are elenolic acid, and hydroxytyrosol
-
?
oleuropein + H2O
oleuropein aglycone + beta-D-glucopyranose
-
i.e. (4S,5E,6S)-4-[2-[2-(3,4-dihydroxyphenyl)ethoxy]-2-oxoethyl]-5-ethylidene-6-[[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)-2-tetrahydropyranyl]oxy]-4H-pyran-3-carboxylic acid methyl ester. The biotransformation produces unstable aglycone species formed by oleuropein hydrolysis that gives rise to the formation of hydroxytyrosol, at the operative temperatures of the bioreactor. The results of the biotransformation at 70°C showed that the main products are hydroxytyrosol, and glucose, being the oleuropein aglycone present in lowamount at the end of reaction
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
82.5% of oleuropein is deglycosylated after 1 h at 40°C
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
100% activity
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
100% activity
-
-
?
additional information
?
-
-
the enzyme is not active on verbascoside and rutin
-
-
?
additional information
?
-
catalytic mechanism is initiated as residue Glu353 nucleophilically attacks the anomeric carbon of the beta-D-glucosyl residue, displacing the oleuropein aglycone in an SN2 fashion. Glu164 works as an acid/base conduit, protonating the leaving group (oleuropein aglycone) and subsequently deprotonating a water molecule, creating a hydroxide nucleophile that displaces Glu353 and releases beta-D-glucose with retention of stereochemistry. Tyr295 orients the nucleophilic Glu353 to preorganize the active site for attack
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oleuropein + H2O
aldehydic forms of oleuropein aglycone + beta-D-glucose
-
-
-
-
?
oleuropein + H2O
oleuropein agylcone + D-glucopyranose
-
-
products are monoaldehydic forms of oleuropein aglycone, hydroxytyrosol, elenolic acid, and D-glucopyranose. The mix of diastereomers of the monoaldehydic form of oleuropein aglycone, is identified as (5S,8R,9S)-, (5S,8S,9S)- and (5S,8R,9R)
-
?
oleuropein + H2O
oleuropein aglycone + beta-D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + beta-D-glucopyranose
-
-
byproductas are elenolic acid, and hydroxytyrosol
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
82.5% of oleuropein is deglycosylated after 1 h at 40°C
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
oleuropein + H2O
oleuropein aglycone + D-glucopyranose
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucose
-
the presence of 2% D-glucose in the medium inhibits the enzyme activity by 40 to 50%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is not activated by D-glucose, trehalose, or delta-gluconolactone
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.86
oleuropein
wild-type, pH not specified in the publication, temperature not specified in the publication
3.8
oleuropein
-
polysulfone capillary membrane-immobilized enzyme, at pH 6.5 and 25°C
3.8
oleuropein
-
enzyme immobilized on polysulfone capillary membranes, at pH 6.5 and 25°C
8.59
oleuropein
mutant C181A, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0107
oleuropein
mutant C181A, pH not specified in the publication, temperature not specified in the publication
0.033
oleuropein
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
oleuropein
mutant C181A, pH not specified in the publication, temperature not specified in the publication
0.0018
oleuropein
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6
4 - 6
-
about 60% activity at pH 4.0, about 80% activity at pH 5.0, 100% activity at pH 5.5, about 40% activity at pH 6.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme plays a key role in the defense response against insect (Bactrocera oleae) injuries of olive fruits
physiological function
-
the enzyme plays a critical role in shaping the phenolic profile of virgin olive oil
physiological function
-
the enzyme plays a key role in the defence response against insect injuries
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BGLC_OLEEU
551
0
62894
Swiss-Prot
other Location (Reliability: 5)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C181A
kcat is improved by 3.2fold with the mutant, Km is increased by 4.6fold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
the enzyme is stable for about 1 h at up to 40°C with a dramatic decrease of activity above this temperature
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
18.2% of the enzyme is inactivated in the immobilisation process on lyophilised chitosan matrix
-
the stability of the bioreactor at the operative temperatures shows a t1/2 of 30 days at 70°C and a t1/2 of 56 days at 60°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Hitrap Q column chromatography, and HiTrap butyl Sepharose column chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in fruits harvested in October, the enzyme activity is significantly enhanced in uninfected fruits when compared to the Bactrocera oleae-infected fruits
-
in the fruits, the enzyme activity increases considerably during the first phase of ripening
-
within 20 min after the injury, which simulates Bactrocera oleae punctures, a strong enzyme activ ity can be observed in the damaged tissues
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
high yield production of hydroxytyrosol from a commercially available oleuropein by using the immobilised recombinant EcSbgly from the hyperthermophilic archaeon Sulfolobus solfataricus on chitosan support
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mazzuca, S.; Spadafora, A.; Innocenti, A.M.
Cell and tissue localization of ?-glucosidase during the ripening of olive fruit (Olea europaea) by in situ activity assay
Plant Sci.
171
726-733
2006
Olea europaea
brenda
Mazzei, R.; Giorno, L.; Piacentini, E.; Mazzuca, S.; Drioli, E.
Kinetic study of a biocatalytic membrane reactor containing immobilized beta-glucosidase for the hydrolysis of oleuropein
J. Membr. Sci.
339
215-223
2009
Prunus dulcis
-
brenda
Briante, R.; La Cara, F.; Febbraio, F.; Barone, R.; Piccialli, G.; Carolla, R.; Mainolfi, P.; De Napoli, L.; Patumi, M.; Fontanazza, G.; Nucci, R.
Hydrolysis of oleuropein by recombinant beta-glycosidase from hyperthermophilic archaeon Sulfolobus solfataricus immobilised on chitosan matrix
J. Biotechnol.
77
275-286
2000
Saccharolobus solfataricus
brenda
Spadafora, A.; Mazzuca, S.; Chiappetta, F.; Parise, A.; Perri, E.; Innocenti, A.
Oleuropein-specific-beta-glucosidase activity marks the early response of olive fruits (Olea europaea) to mimed insect attack
Agric. Sci. China
7
703-712
2008
Olea europaea
-
brenda
Capasso, R.; Evidente, A.; Visca, C.; Gianfreda, L.; Maremonti, M.; Greco Jr., G.
Production of glucose and bioactive aglycone by chemical and enzymatic hydrolysis of purified oleuropein from Olea europea
Appl. Biochem. Biotechnol.
61
365-377
1996
Olea europaea
-
brenda
Ciafardini, G.; Marsilio, V.; Lanza, B.; Pozzi, N.
Hydrolysis of oleuropein by Lactobacillus plantarum strains associated with olive fermentation
Appl. Environ. Microbiol.
60
4142-4147
1994
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum B21, Lactiplantibacillus plantarum B20, Lactiplantibacillus plantarum B17
brenda
Mazzei, R.; Giorno, L.; Mazzuca, S.; Spadafora, A.; Drioli, E.
beta-Glucosidase separation from Olea europaea fruit and its use in membrane bioreactors for hydrolysis of oleuropein
Desalination
200
483-484
2006
Olea europaea
-
brenda
De Leonardis, A.; Macciola, V.; Cuomo, F.; Lopez, F.
Evidence of oleuropein degradation by olive leaf protein extract
Food Chem.
175
568-574
2015
Olea europaea
brenda
Ramirez, E.; Brenes, M.; Garcia, P.; Medina, E.; Romero, C.
Oleuropein hydrolysis in natural green olives: Importance of the endogenous enzymes
Food Chem.
206
204-209
2016
Olea europaea
brenda
Delgado-Povedano, M.D.; Priego-Capote, F.; Luque de Castro, M.D.
Selective ultrasound-enhanced enzymatic hydrolysis of oleuropein to its aglycon in olive (Olea europaea L.) leaf extracts
Food Chem.
220
282-288
2017
Aspergillus niger
brenda
Romero-Segura, C.; Sanz, C.; Perez, A.G.
Purification and characterization of an olive fruit beta-glucosidase involved in the biosynthesis of virgin olive oil phenolics
J. Agric. Food Chem.
57
7983-7988
2009
Olea europaea
brenda
Gutierrez-Rosales, F.; Romero, M.P.; Casanovas, M.; Motilva, M.J.; Minguez-Mosquera, M.I.
Metabolites involved in oleuropein accumulation and degradation in fruits of Olea europaea L.: Hojiblanca and Arbequina varieties
J. Agric. Food Chem.
58
12924-12933
2010
Olea europaea
brenda
Gutierrez-Rosales, F.; Romero, M.P.; Casanovas, M.; Motilva, M.J.; Minguez-Mosquera, M.I.
beta-Glucosidase involvement in the formation and transformation of oleuropein during the growth and development of olive fruits (Olea europaea L. cv. Arbequina) grown under different farming practices
J. Agric. Food Chem.
60
4348-4358
2012
Olea europaea
brenda
Ramirez, E.; Medina, E.; Brenes, M.; Romero, C.
Endogenous enzymes involved in the transformation of oleuropein in Spanish table olive varieties
J. Agric. Food Chem.
62
9569-9575
2014
Olea europaea
brenda
Nikolaivits, E.; Termentzi, A.; Skaltsounis, A.L.; Fokialakis, N.; Topakas, E.
Enzymatic tailoring of oleuropein from Olea europaea leaves and product identification by HRMS/MS spectrometry
J. Biotechnol.
253
48-54
2017
Thermothelomyces thermophilus
brenda
Koudounas, K.; Banilas, G.; Michaelidis, C.; Demoliou, C.; Rigas, S.; Hatzopoulos, P.
A defence-related Olea europaea beta-glucosidase hydrolyses and activates oleuropein into a potent protein cross-linking agent
J. Exp. Bot.
66
2093-2106
2015
Olea europaea (Q8GVD0), Olea europaea
brenda
Palmeri, R.; Restuccia, C.; Monteleone, J.I.; Sperlinga, E.; Siracusa, L.; Serafini, M.; Finamore, A.; Spagna, G.
Bioactivity improvement of Olea europaea leaf extract biotransformed by Wickerhamomyces anomalus enzymes
Plant Foods Hum. Nutr.
72
211-218
2017
Prunus dulcis
brenda
Koudounas, K.; Thomopoulou, M.; Michaelidis, C.; Zevgiti, E.; Papakostas, G.; Tserou, P.; Daras, G.; Hatzopoulos, P.
The C-domain of oleuropein beta-glucosidase assists in protein folding and sequesters the enzyme in nucleus
Plant Physiol.
174
1371-1383
2017
Olea europaea
brenda
Briante, R.; Patumi, M.; Limongelli, S.; Febbraio, F.; Vaccaro, C.; Di Salle, A.; La Cara, F.; Nucci, R.
Changes in phenolic and enzymatic activities content during fruit ripening in two Italian cultivars of Olea europaea L.
Plant Sci.
162
791-798
2002
Olea europaea
-
brenda
Spadafora, A.; Mazzuca, S.; Chiappetta, F.; Parise, A.; Perri, E.; Innocenti, A.
Oleuropein-specific-beta-glucosidase activity marks the early response of olive fruits (Olea europaea) to mimed insect attack
Agric. Sci. China
7
703-712
2008
Olea europaea
-
brenda
Sivakumar, G.; Bati, C.; Uccella, N.
Demethyloleuropein and beta-glucosidase activity in olive fruits
Biotechnol. J.
2
381-385
2007
Olea europaea
brenda
Romero-Segura, C.; Garcia-Rodrguez, R.; Sanchez-Ortiz, A.; Sanz, C.; Perez, A.
The role of olive beta-glucosidase in shaping the phenolic profile of virgin olive oil
Food Res. Int.
45
191-196
2012
Olea europaea
-
brenda
Velazquez-Palmero, D.; Romero-Segura, C.; Garcia-Rodriguez, R.; Hernandez, M.L.; Vaistij, F.E.; Graham, I.A.; Perez, A.G.; Martinez-Rivas, J.M.
An oleuropein beta-glucosidase from olive fruit is involved in determining the phenolic composition of virgin olive oil
Front. Plant Sci.
8
1902
2017
Olea europaea (A0A2H4ER88)
brenda
Cirilli, M.; Caruso, G.; Gennai, C.; Urbani, S.; Frioni, E.; Ruzzi, M.; Servili, M.; Gucci, R.; Poerio, E.; Muleo, R.
The role of polyphenoloxidase, peroxidase, and beta-glucosidase in phenolics accumulation in Olea europaea L. fruits under different water regimes
Front. Plant Sci.
8
717
2017
Olea europaea
brenda
Mazzei, R.; Giorno, L.; Piacentini, E.; Mazzuca, S.; Drioli, E.
Kinetic study of a biocatalytic membrane reactor containing immobilized beta-glucosidase for the hydrolysis of oleuropein
J. Membr. Sci.
339
215-223
2009
Prunus dulcis
-
brenda
Boudabbous, M.; Saibi, W.; Bouallagui, Z.; Dardouri, M.; Sayadi, S.; Belghith, H.; Mechichi, T.; Gargouri, A.
Fast activated charcoal prepurification of Fusarium solani beta-glucosidase for an efficient oleuropein bioconversion
Prep. Biochem. Biotechnol.
47
185-191
2017
Fusarium solani
brenda
Guggenheim, K.G.; Crawford, L.M.; Paradisi, F.; Wang, S.C.; Siegel, J.B.
beta-Glucosidase discovery and design for the degradation of oleuropein
ACS Omega
3
15754-15762
2018
Streptomyces sp. (Q59976)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.2.1.206)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
