Characterization of a long-chain alpha-galactosidase from Papiliotrema flavescens

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26310%2F18%3APU136114" target="_blank" >RIV/00216305:26310/18:PU136114 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60162694:G44__/18:43889447

Výsledek na webu

<a href="https://link.springer.com/article/10.1007/s11274-017-2403-6" target="_blank" >https://link.springer.com/article/10.1007/s11274-017-2403-6</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11274-017-2403-6" target="_blank" >10.1007/s11274-017-2403-6</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Characterization of a long-chain alpha-galactosidase from Papiliotrema flavescens

Popis výsledku v původním jazyce

alpha-Galactosidases are assigned to the class of hydrolases and the subclass of glycoside hydrolases (GHs). They belong to six GH families and include the only characterized alpha-galactosidases from yeasts (GH 27, Saccharomyces cerevisiae). The present study focuses on an investigation of the lactose-inducible alpha-galactosidase produced by Papiliotrema flavescens. The enzyme was present on the surface of cells and in the cytosol. Its temperature optimum was about 60 degrees C and the pH optimum was 4.8; the pH stability ranged from 3.2 to 6.6. This alpha-galactosidase also exhibited transglycosylation activity. The cytosol alpha-galactosidase with a molecular weight about 110 kDa, was purified using a combination of liquid chromatography techniques. Three intramolecular peptides were determined by the partial structural analysis of the sequences of the protein isolated, using MALDI-TOF/TOF mass spectrometry. The data obtained recognized the first yeast alpha-galactosidase, which belongs to the GH 36 family. The bioinformatics analysis and homology modeling of a 210 amino acids long C-terminal sequence (derived from cDNA) confirmed the correctness of these findings. The study was also supplemented by the screening of capsular cryptococcal yeasts, which produce the surface lactose-inducible alpha- and beta-galactosidases. The production of the lactose-inducible alpha-galactosidases was not found to be a general feature within the yeast strains examined and, therefore, the existing hypothesis on the general function of this enzyme in cryptococcal capsule rearrangement cannot be confirmed.

Název v anglickém jazyce

Characterization of a long-chain alpha-galactosidase from Papiliotrema flavescens

Popis výsledku anglicky

alpha-Galactosidases are assigned to the class of hydrolases and the subclass of glycoside hydrolases (GHs). They belong to six GH families and include the only characterized alpha-galactosidases from yeasts (GH 27, Saccharomyces cerevisiae). The present study focuses on an investigation of the lactose-inducible alpha-galactosidase produced by Papiliotrema flavescens. The enzyme was present on the surface of cells and in the cytosol. Its temperature optimum was about 60 degrees C and the pH optimum was 4.8; the pH stability ranged from 3.2 to 6.6. This alpha-galactosidase also exhibited transglycosylation activity. The cytosol alpha-galactosidase with a molecular weight about 110 kDa, was purified using a combination of liquid chromatography techniques. Three intramolecular peptides were determined by the partial structural analysis of the sequences of the protein isolated, using MALDI-TOF/TOF mass spectrometry. The data obtained recognized the first yeast alpha-galactosidase, which belongs to the GH 36 family. The bioinformatics analysis and homology modeling of a 210 amino acids long C-terminal sequence (derived from cDNA) confirmed the correctness of these findings. The study was also supplemented by the screening of capsular cryptococcal yeasts, which produce the surface lactose-inducible alpha- and beta-galactosidases. The production of the lactose-inducible alpha-galactosidases was not found to be a general feature within the yeast strains examined and, therefore, the existing hypothesis on the general function of this enzyme in cryptococcal capsule rearrangement cannot be confirmed.

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/LO1211" target="_blank" >LO1211: Centrum materiálového výzkumu na FCH VUT v Brně - udržitelnost a rozvoj</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY

ISSN

0959-3993

e-ISSN

1573-0972

Svazek periodika

34

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

14

Strana od-do

1-14

Kód UT WoS článku

000425095300003

EID výsledku v databázi Scopus

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