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@article{1472761,
author = {Stratilová, Barbora and Klaudiny, Jaroslav and Řehulka, Jaroslav and Stratilová, Eva and Mészárosová, Csilla and Garajová, Soňa and Pavlatovská, Barbora and Řehulková, Helena and Kozmon, Stanislav and Šesták, Sergej and Firáková, Zuzana and Vadkertiová, Renáta},
article_location = {Netherlands},
article_number = {19},
keywords = {α-Galactosidase, Cryptococcus flavescens, GH 36 family, Lactose-inducible, Long-chain, Papiliotrema flavescens},
language = {eng},
issn = {0959-3993},
journal = {World Journal of Microbiology and Biotechnology},
title = {Characterization of a long-chain α-galactosidase from Papiliotrema flavescens},
url = {https://link.springer.com/article/10.1007/s11274-017-2403-6#enumeration},
volume = {34},
year = {2018}
}
TY - JOUR
ID - 1472761
AU - Stratilová, Barbora - Klaudiny, Jaroslav - Řehulka, Jaroslav - Stratilová, Eva - Mészárosová, Csilla - Garajová, Soňa - Pavlatovská, Barbora - Řehulková, Helena - Kozmon, Stanislav - Šesták, Sergej - Firáková, Zuzana - Vadkertiová, Renáta
PY - 2018
TI - Characterization of a long-chain α-galactosidase from Papiliotrema flavescens
JF - World Journal of Microbiology and Biotechnology
VL - 34
IS - 19
PB - Springer Netherlands
SN - 09593993
KW - α-Galactosidase, Cryptococcus flavescens, GH 36 family, Lactose-inducible, Long-chain, Papiliotrema flavescens
UR - https://link.springer.com/article/10.1007/s11274-017-2403-6#enumeration
N2 - α-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 α-galactosidases from yeasts (GH 27, Saccharomyces cerevisiae). The present study focuses on an investigation of the lactose-inducible α-galactosidase produced by Papiliotrema flavescens. The enzyme was present on the surface of cells and in the cytosol. Its temperature optimum was about 60 °C and the pH optimum was 4.8; the pH stability ranged from 3.2 to 6.6. This α-galactosidase also exhibited transglycosylation activity. The cytosol α-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 α-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 α- and β-galactosidases. The production of the lactose-inducible α-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.
ER -
STRATILOVÁ, Barbora, Jaroslav KLAUDINY, Jaroslav ŘEHULKA, Eva STRATILOVÁ, Csilla MÉSZÁROSOVÁ, Soňa GARAJOVÁ, Barbora PAVLATOVSKÁ, Helena ŘEHULKOVÁ, Stanislav KOZMON, Sergej ŠESTÁK, Zuzana FIRÁKOVÁ a Renáta VADKERTIOVÁ. Characterization of a long-chain α-galactosidase from Papiliotrema flavescens. \textit{World Journal of Microbiology and Biotechnology}. Netherlands: Springer Netherlands, 2018, roč.~34, č.~19. ISSN~0959-3993.
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