Two fungal flavonoid-specific glucosidases/rutinosidases for rutin hydrolysis and rutinoside synthesis under homogeneous and heterogeneous reaction conditions
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F21%3A00547402" target="_blank" >RIV/61388971:_____/21:00547402 - isvavai.cz</a>
Alternative codes found
RIV/60461373:22330/21:43926402
Result on the web
<a href="https://amb-express.springeropen.com/articles/10.1186/s13568-021-01298-2" target="_blank" >https://amb-express.springeropen.com/articles/10.1186/s13568-021-01298-2</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1186/s13568-021-01298-2" target="_blank" >10.1186/s13568-021-01298-2</a>
Alternative languages
Result language
angličtina
Original language name
Two fungal flavonoid-specific glucosidases/rutinosidases for rutin hydrolysis and rutinoside synthesis under homogeneous and heterogeneous reaction conditions
Original language description
The glycosidases within GH5-23 cleave the glycosidic bond of beta-glucosylated or rutinosylated flavonoids. Moreover, by virtue of their transglycosylation activity, glycoconjugates with glucosyl and rutinosyl moieties are accessible. Here we report the biochemical characterization and biotechnological assessment of two heterologously expressed members of GH5-23-McGlc from Mucor circinelloides and PcGlc from Penicillium chrysogenum. Both enzymes exhibited the highest hydrolytic activities with quercetin-3-beta-O-glucopyranoside, whereas lower specificity constants were determined with the rutinosides narcissin, rutin and hesperidin. High stabilities against thermal, ethanol and dimethyl sulfoxide-induced inactivation, a very limited secondary hydrolysis of the formed transglycosylation products, and no detectable product inhibition were additional features appropriate for biotechnological applications. The enzymes were compared in their efficiencies to hydrolyze rutin and to synthesize 2-phenylethyl rutinoside under homogeneous and heterogeneous reaction conditions using high rutin concentrations of 100 and 300 mM. Highest transglycosylation efficiencies were achieved with fully dissolved rutin in reaction mixtures containing 25% dimethyl sulfoxide. Molecular docking and multiple sequence alignments suggest that the hydrophobic environment of aromatic residues within the + 1 subsite of GH5-23 glycosidases is very important for the binding of flavonoid glucosides and rutinosides.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
20902 - Bioprocessing technologies (industrial processes relying on biological agents to drive the process) biocatalysis, fermentation
Result continuities
Project
<a href="/en/project/GA19-00091S" target="_blank" >GA19-00091S: Exploring α-L-rhamnosyl-β-D-glucosidases — emerging enzymes in food chemistry</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
AMB Express
ISSN
2191-0855
e-ISSN
2191-0855
Volume of the periodical
11
Issue of the periodical within the volume
1
Country of publishing house
DE - GERMANY
Number of pages
11
Pages from-to
136
UT code for WoS article
000708473800002
EID of the result in the Scopus database
2-s2.0-85117450028