Engineered Glycosidases for the Synthesis of Analogs of Human Milk Oligosaccharides

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F22%3A00557244" target="_blank" >RIV/61388971:_____/22:00557244 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/22:10443847

Result on the web

<a href="https://www.mdpi.com/1422-0067/23/8/4106" target="_blank" >https://www.mdpi.com/1422-0067/23/8/4106</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/ijms23084106" target="_blank" >10.3390/ijms23084106</a>

Result language

angličtina

Original language name

Engineered Glycosidases for the Synthesis of Analogs of Human Milk Oligosaccharides

Original language description

Enzymatic synthesis is an elegant biocompatible approach to complex compounds such as human milk oligosaccharides (HMOs). These compounds are vital for healthy neonatal development with a positive impact on the immune system. Although HMOs may be prepared by glycosyltransferases, this pathway is often complicated by the high price of sugar nucleotides, stringent substrate specificity, and low enzyme stability. Engineered glycosidases (EC 3.2.1) represent a good synthetic alternative, especially if variations in the substrate structure are desired. Site-directed mutagenesis can improve the synthetic process with higher yields and/or increased reaction selectivity. So far, the synthesis of human milk oligosaccharides by glycosidases has mostly been limited to analytical reactions with mass spectrometry detection. The present work reveals the potential of a library of engineered glycosidases in the preparative synthesis of three tetrasaccharides derived from lacto-N-tetraose (Gal beta 4GlcNAc beta 3Gal beta 4Glc), employing sequential cascade reactions catalyzed by beta 3-N-acetylhexosaminidase BbhI from Bifidobacterium bifidum, beta 4-galactosidase BgaD-B from Bacillus circulans, beta 4-N-acetylgalactosaminidase from Talaromyces flavus, and beta 3-galactosynthase BgaC from B. circulans. The reaction products were isolated and structurally characterized. This work expands the insight into the multi-step catalysis by glycosidases and shows the path to modified derivatives of complex carbohydrates that cannot be prepared by standard glycosyltransferase methods.

Czech name

—

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

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2022

Confidentiality

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

Name of the periodical

International Journal of Molecular Sciences

ISSN

1422-0067

e-ISSN

1422-0067

Volume of the periodical

23

Issue of the periodical within the volume

8

Country of publishing house

CH - SWITZERLAND

Number of pages

13

Pages from-to

4106

UT code for WoS article

000786916300001

EID of the result in the Scopus database

2-s2.0-85127578440