Significados de ipr017853 en inglés

The enzyme showed significant sequence homology with several bacterial beta-N-acetylhexosaminidases which belong to family 20 glycosyl hydrolases.

The predicted amino acid sequence of GlcNAcaseA showed similarity to bacterial beta-N-acetylglucosaminidases belonging to the family 20 glycosyl hydrolases.

Conclusion: This study demonstrated that the presence of suberin in S. scabiei growth medium induced the production of a wide variety of glycosyl hydrolases.

Annotated metagenomic data suggested diverse glycoside hydrolase gene representation within the pooled heavy DNA.

Supernatants from both cultures possessed comparable glycoside hydrolase activities when incubated with artificial biomass substrates.

Bacteria modulate glycoside hydrolase expression in response to the changes in the composition of lignocellulosic biomass.

This enzyme is particularly interesting, because it shows no significant sequence similarity to any known glycoside hydrolase.

A new clan that links glycoside hydrolase families 28 and 49 is suggested.

Conclusions: This work provides the foundation for further comparative and functional analyses of plant glycoside hydrolases.

Sequence analysis reveals approximately 130 predicted glycoside hydrolases that target the major structural and storage plant polysaccharides.

The major advance of our study was the discovery of active-yet-uncultivated soil microorganisms and enrichment of their glycoside hydrolases.

Genes encoding glycoside hydrolases are found in a wide range of organisms, from archea to animals, and are relatively abundant in plant genomes.

Evaluating these enzymes as potential therapeutics, we demonstrate that these glycoside hydrolases selectively target and degrade the exopolysaccharide component of the biofilm matrix.