The flavonoid degrading fungus Acremonium sp. DSM 24697 produces two diglycosidases with different specificities

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F19%3A00518268" target="_blank" >RIV/61388971:_____/19:00518268 - isvavai.cz</a>

Výsledek na webu

<a href="https://link.springer.com/article/10.1007%2Fs00253-019-10180-y" target="_blank" >https://link.springer.com/article/10.1007%2Fs00253-019-10180-y</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00253-019-10180-y" target="_blank" >10.1007/s00253-019-10180-y</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The flavonoid degrading fungus Acremonium sp. DSM 24697 produces two diglycosidases with different specificities

Popis výsledku v původním jazyce

Diglycosidases hydrolyze the heterosidic linkage of diglycoconjugates, releasing the disaccharide and the aglycone. Usually, these enzymes do not hydrolyze or present only low activities towards monoglycosylated compounds. The flavonoid degrading fungus Acremonium sp. DSM 24697 produced two diglycosidases, which were termed 6-O-alpha-rhamnosyl-beta-glucosidase I and II (alpha R beta G I and II) because of their function of releasing the disaccharide rutinose (6-O-alpha-L-rhamnosyl-beta-D-glucose) from the diglycoconjugates hesperidin or rutin. In this work, the genome of Acremonium sp. DSM 24697 was sequenced and assembled with a size of similar to 27 Mb. The genes encoding alpha R beta G I and II were expressed in Pichia pastoris KM71 and the protein products were purified with apparent molecular masses of 42 and 82 kDa, respectively. A phylogenetic analysis showed that alpha R beta G I grouped in glycoside hydrolase family 5, subfamily 23 (GH5), together with other fungal diglycosidases whose substrate specificities had been reported to be different from alpha R beta G I. On the other hand, alpha R beta G II grouped in glycoside hydrolase family 3 (GH3) and thus is the first GH3 member that hydrolyzes the heterosidic linkage of rutinosylated compounds. The substrate scopes of the enzymes were different: alpha R beta G I showed exclusive specificity toward 7-O-beta-rutinosyl flavonoids, whereas alpha R beta G II hydrolyzed both 7-O-beta-rutinosyl- and 3-O-beta-rutinosyl- flavonoids. None of the enzymes displayed activity toward 7-O-beta-neohesperidosyl- flavonoids. The recombinant enzymes also exhibited transglycosylation activities, transferring rutinose from hesperidin or rutin onto various alcoholic acceptors. The different substrate scopes of alpha R beta G I and II may be part of an optimized strategy of the original microorganism to utilize different carbon sources.

Název v anglickém jazyce

The flavonoid degrading fungus Acremonium sp. DSM 24697 produces two diglycosidases with different specificities

Popis výsledku anglicky

Diglycosidases hydrolyze the heterosidic linkage of diglycoconjugates, releasing the disaccharide and the aglycone. Usually, these enzymes do not hydrolyze or present only low activities towards monoglycosylated compounds. The flavonoid degrading fungus Acremonium sp. DSM 24697 produced two diglycosidases, which were termed 6-O-alpha-rhamnosyl-beta-glucosidase I and II (alpha R beta G I and II) because of their function of releasing the disaccharide rutinose (6-O-alpha-L-rhamnosyl-beta-D-glucose) from the diglycoconjugates hesperidin or rutin. In this work, the genome of Acremonium sp. DSM 24697 was sequenced and assembled with a size of similar to 27 Mb. The genes encoding alpha R beta G I and II were expressed in Pichia pastoris KM71 and the protein products were purified with apparent molecular masses of 42 and 82 kDa, respectively. A phylogenetic analysis showed that alpha R beta G I grouped in glycoside hydrolase family 5, subfamily 23 (GH5), together with other fungal diglycosidases whose substrate specificities had been reported to be different from alpha R beta G I. On the other hand, alpha R beta G II grouped in glycoside hydrolase family 3 (GH3) and thus is the first GH3 member that hydrolyzes the heterosidic linkage of rutinosylated compounds. The substrate scopes of the enzymes were different: alpha R beta G I showed exclusive specificity toward 7-O-beta-rutinosyl flavonoids, whereas alpha R beta G II hydrolyzed both 7-O-beta-rutinosyl- and 3-O-beta-rutinosyl- flavonoids. None of the enzymes displayed activity toward 7-O-beta-neohesperidosyl- flavonoids. The recombinant enzymes also exhibited transglycosylation activities, transferring rutinose from hesperidin or rutin onto various alcoholic acceptors. The different substrate scopes of alpha R beta G I and II may be part of an optimized strategy of the original microorganism to utilize different carbon sources.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA19-00091S" target="_blank" >GA19-00091S: Prozkoumání α-L-rhamnosyl-β-D-glukosidas — enzymů rozvíjejících se v potravinářství</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Applied Microbiology and Biotechnology

ISSN

0175-7598

e-ISSN

—

Svazek periodika

103

Číslo periodika v rámci svazku

23-24

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

9493-9504

Kód UT WoS článku

000495237400001

EID výsledku v databázi Scopus

2-s2.0-85075018338