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

Result code in 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>

Alternative codes found

RIV/60162694:G44__/18:43889447

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

<a href="/en/project/LO1211" target="_blank" >LO1211: Materials Research Centre at FCH BUT- Sustainability and Development</a><br>

Continuities

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

Publication year

2018

Confidentiality

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

Name of the periodical

WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY

ISSN

0959-3993

e-ISSN

1573-0972

Volume of the periodical

34

Issue of the periodical within the volume

2

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

14

Pages from-to

1-14

UT code for WoS article

000425095300003

EID of the result in the Scopus database

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