Selective Beta-N-acetylhexosaminidase from Aspergillus versicolor—a tool for producing bioactive carbohydrates
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00504360" target="_blank" >RIV/61388963:_____/19:00504360 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/19:00504360
Result on the web
<a href="https://link.springer.com/article/10.1007%2Fs00253-018-9534-z" target="_blank" >https://link.springer.com/article/10.1007%2Fs00253-018-9534-z</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s00253-018-9534-z" target="_blank" >10.1007/s00253-018-9534-z</a>
Alternative languages
Result language
angličtina
Original language name
Selective Beta-N-acetylhexosaminidase from Aspergillus versicolor—a tool for producing bioactive carbohydrates
Original language description
Beta-N-Acetylhexosaminidases (EC 3.2.1.52) are typical of their dual activity encompassing both N-acetylglucosamine and N-acetylgalactosamine substrates. Here we present the isolation and characterization of a selective -N-acetylhexosaminidase from the fungal strain of Aspergillus versicolor. The enzyme was recombinantly expressed in Pichia pastoris KM71H in a high yield and purified in a single step using anion-exchange chromatography. Homologous molecular modeling of this enzyme identified crucial differences in the enzyme active site that may be responsible for its high selectivity for N-acetylglucosamine substrates compared to fungal -N-acetylhexosaminidases from other sources. The enzyme was used in a sequential reaction together with a mutant -N-acetylhexosaminidase from Talaromyces flavus with an enhanced synthetic capability, affording a bioactive disaccharide bearing an azido functional group. The azido function enabled an elegant multivalent presentation of this disaccharide on an aromatic carrier. The resulting model glycoconjugate is applicable as a selective ligand of galectin-3a biomedically attractive human lectin. These results highlight the importance of a general availability of robust and well-defined carbohydrate-active enzymes with tailored catalytic properties for biotechnological and biomedical applications.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - 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
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
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Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Applied Microbiology and Biotechnology
ISSN
0175-7598
e-ISSN
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Volume of the periodical
103
Issue of the periodical within the volume
4
Country of publishing house
US - UNITED STATES
Number of pages
17
Pages from-to
1737-1753
UT code for WoS article
000459250200016
EID of the result in the Scopus database
2-s2.0-85059464051