Results 221 to 230 of about 511,400 (248)
Some of the next articles are maybe not open access.

Enzymatic acylation of flavonoid glycosides by a carbohydrate esterase of family 16

Biotechnology Letters, 2014
The acetyl esterase of Trichoderma reesei belonging to carbohydrate esterase (CE) family 16 catalyzes transacylations to carbohydrate moieties of flavonoid glycosides, esculin and rutin. The enzyme recognizes as acyl donors vinyl esters of short carboxylic acids.
P. Biely   +3 more
semanticscholar   +3 more sources

Structural annotation of the conserved carbohydrate esterase vb_24B_21 from Shiga toxin-encoding bacteriophage Φ24B.

Journal of Structural Biology, 2020
Shiga toxin-encoding bacteriophages transfer Shiga toxin genes to Escherichia coli and are responsible for the emergence of pathogenic bacterial strains that cause severe foodborne human diseases.
B. Franke   +5 more
semanticscholar   +1 more source

Microbial carbohydrate esterases in cold adapted environments

Gene, 2008
Psychrophiles produce cold-evolved enzymes that display a high catalytic efficiency, associated with a low thermal stability. In recent years, these enzymes have attracted the attention of scientists because of their peculiar properties that render them particularly useful in investigating the relationship existing between enzyme stability and ...
Aurilia V, Parracino A, D'Auria S
openaire   +4 more sources

Carbohydrate Esterases: An Overview

2018
Carbohydrate esterases are a group of enzymes which release acyl or alkyl groups attached by ester linkage to carbohydrates. The CAZy database, which classifies enzymes that assemble, modify, and break down carbohydrates and glycoconjugates, classifies all carbohydrate esterases into 16 families.
Mariana, Armendáriz-Ruiz   +3 more
openaire   +2 more sources

Microbial Xylanolytic Carbohydrate Esterases

2007
The plant cell wall represents the most abundant reservoir of organic carbon in the biosphere with 1011 tons synthesized annually. The degradation of this macromolecular structure by microbial enzymes is a key biological process that is central to the carbon cycle, herbivore nutrition and host invasion by phytopathogenic fungi and bacteria.
Evangelos Topakas, Christakopoulos Paul
openaire   +1 more source

Significance of a family-6 carbohydrate-binding module in a modular feruloyl esterase for removing ferulic acid from insoluble wheat arabinoxylan.

Enzyme and Microbial Technology, 2020
Ruminiclostridium josui Fae1A is a modular enzyme consisting of an N-terminal signal peptide, family-1 carbohydrate esterase module (CE1), family-6 carbohydrate-binding module (CBM6), and dockerin module in that order.
Ai Mamiya   +7 more
semanticscholar   +1 more source

Structural and functional profile of the carbohydrate esterase gene complement in Phytophthora infestans

Current Genetics, 2010
The plant cell cuticle is the first obstacle for penetration of the host by plant pathogens. To breach this barrier, most pathogenic fungi employ a complex assortment of cell wall-degrading enzymes including carbohydrate esterases, glycoside hydrolases, and polysaccharide lyases.
M. Ospina-Giraldo   +2 more
semanticscholar   +3 more sources

Transacetylations to carbohydrates catalyzed by acetylxylan esterase in the presence of organic solvent

Biochimica et Biophysica Acta (BBA) - General Subjects, 2003
Various conditions were applied to test the ability of acetylxylan esterase (AcXE) from Schizophyllum commune to catalyze acetyl group transfer to methyl beta-D-xylopyranoside (Me-beta-Xylp) and other carbohydrates. The best performance of the enzyme was observed in an n-hexane-vinyl acetate-sodium dioctylsulfosuccinate (DOSS)-water microemulsion at a ...
Peter, Biely   +3 more
openaire   +2 more sources

Comparison of Catalytic Properties of Acetyl Xylan Esterases from Three Carbohydrate Esterase Families

2003
Most natural hemicelluloses are acetylated. Some xylans carryalso esterified phenolic acid side groups. Carbohydrate-actingesterases (CE) have been recently classified according tostructural similarities into several CE families. However, thisclassification does not necessarily predict the substrate specificity of these enzymes.
Tenkanen, Maija   +4 more
openaire   +4 more sources

Home - About - Disclaimer - Privacy