Characterization of a long-chain α-galactosidase from Papiliotrema flavescens View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-02

AUTHORS

Barbora Stratilová, Jaroslav Klaudiny, Pavel Řehulka, Eva Stratilová, Csilla Mészárosová, Soňa Garajová, Barbora Pavlatovská, Helena Řehulková, Stanislav Kozmon, Sergej Šesták, Zuzana Firáková, Renáta Vadkertiová

ABSTRACT

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. More... »

PAGES

19

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s11274-017-2403-6

DOI

http://dx.doi.org/10.1007/s11274-017-2403-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1100161015

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29302817


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