A5103019567- Enzyme Production and Characterization
- Biofuel production and bioconversion
- Enzyme Structure and Function
- Polysaccharides and Plant Cell Walls
- Microbial Metabolic Engineering and Bioproduction
- Glycosylation and Glycoproteins Research
- Enzyme Catalysis and Immobilization
- Phytochemistry and Biological Activities
- Enzyme-mediated dye degradation
- Microbial Metabolites in Food Biotechnology
- Bacterial Genetics and Biotechnology
- X-ray Diffraction in Crystallography
- Polysaccharides Composition and Applications
- Photosynthetic Processes and Mechanisms
- Fungal Biology and Applications
- Carbohydrate Chemistry and Synthesis
- Biochemical and Molecular Research
- Protein Structure and Dynamics
- HIV/AIDS drug development and treatment
- Bacteriophages and microbial interactions
- Erythrocyte Function and Pathophysiology
- Probiotics and Fermented Foods
- DNA and Nucleic Acid Chemistry
- Flavonoids in Medical Research
- Toxin Mechanisms and Immunotoxins
University of Copenhagen
2014-2024
University of Gothenburg
2012
University of Hong Kong
2011
Aarhus University
2011
University of Siena
2011
Synchrotron soleil
2008
Enkam (Denmark)
2008
Institut Néel
2005
Tokyo Institute of Technology
2003-2004
Utrecht University
2002
The enzymatic degradation of recalcitrant plant biomass is one the key industrial challenges 21st century. Accordingly, there a continuing drive to discover new routes promote polysaccharide degradation. Perhaps most promising approach involves application “cellulase-enhancing factors,” such as those from glycoside hydrolase (CAZy) GH61 family. Here we show that enzymes are unique family copper-dependent oxidases. We demonstrate copper needed for maximal activity and formation cellodextrin...
Currently, the relatively high cost of enzymes such as glycoside hydrolases that catalyze cellulose hydrolysis represents a barrier to commercialization biorefinery capable producing renewable transportable fuels ethanol from abundant lignocellulosic biomass. Among many families and hemicellulose hydrolysis, few are more enigmatic than family 61 (GH61), originally classified based on measurement very weak endo-1,4-beta-d-glucanase activity in one member. Here we show certain GH61 proteins...
Lytic polysaccharide monooxygenases (LPMOs) are recently discovered enzymes that oxidatively deconstruct polysaccharides. LPMOs fundamental in the effective utilization of these substrates by bacteria and fungi; moreover, have significant industrial importance. We report here activity, spectroscopy three-dimensional structure a starch-active LPMO, representative new CAZy AA13 family. demonstrate generate aldonic acid-terminated malto-oligosaccharides from retrograded starch boost...
Lytic polysaccharide monooxygenases (LPMOs) are industrially important copper-dependent enzymes that oxidatively cleave polysaccharides. Here we present a functional and structural characterization of two closely related AA9-family LPMOs from Lentinus similis (LsAA9A) Collariella virescens (CvAA9A). LsAA9A CvAA9A range polysaccharides, including cellulose, xyloglucan, mixed-linkage glucan glucomannan. additionally cleaves isolated xylan substrates. The structures bound to cellulosic...
The corpuscular elements of the peripheral blod and morphology chromosome constitution bone marrow cells have been studied in patients before during lithium therapy as well who had received for a substantial period. Lithium produced elevated total white cell, granulocyte, eosinophil thrombocyte counts lymphocytopenia, whereas no effect was seen on erythrocyte reticulocyte counts. There were morphological or cytogenetic changes aspirates. Neither toxic doses able to produce abnormalities rats.
Isomaltooligosaccharides (IMO) have been suggested as promising prebiotics that stimulate the growth of probiotic bacteria. Genomes lactobacilli from acidophilus group, represented by Lactobacillus NCFM, encode α-1,6 glucosidases family GH13_31 (glycoside hydrolase 13 subfamily 31) confer degradation IMO. These genes reside frequently within maltooligosaccharide utilization operons, which include an ATP-binding cassette transporter and α-glucan active enzymes, e.g., maltogenic amylases...
Lignocellulose is a renewable but complex material exhibiting high recalcitrance to enzymatic hydrolysis, which attributed, in part, the presence of covalent linkages between lignin and polysaccharides plant cell wall. Glucuronoyl esterases from carbohydrate esterase family 15 (CE15) have been proposed as an aid reducing this by cleaving ester bonds found glucuronoxylan. In Bacteroidota phylum, some species organize genes related metabolism polysaccharide utilization loci (PULs) encode all...
Orotidine 5'-monophosphate decarboxylase (ODCase) catalyzes the decarboxylation of orotidine 5'-monophosphate, last step in de novo synthesis uridine 5'-monophosphate. ODCase is a very proficient enzyme [Radzicka, A., and Wolfenden, R. (1995) Science 267, 90−93], enhancing reaction rate by factor 1017. This proficiency has been enigmatic, since it achieved without metal ions or cofactors. Here we present 2.5 Å resolution structure complexed with inhibitor...
Lignocellulose is highly recalcitrant to enzymatic deconstruction, where the recalcitrance primarily results from chemical linkages between lignin and carbohydrates. Glucuronoyl esterases (GEs) carbohydrate esterase family 15 (CE15) have been suggested play key roles in reducing lignocellulose by cleaving covalent ester bonds found glucuronoxylan. However, only a limited number of GEs biochemically characterized structurally determined date, limiting our understanding these enzymes their...
Glucuronoyl esterases (GEs) catalyze the cleavage of ester linkages between lignin and glucuronic acid moieties on glucuronoxylan in plant biomass. As such, GEs represent promising biochemical tools industrial processing these recalcitrant resources. However, details how interact degradation their natural substrates are sparse, calling for thorough enzyme structure-function studies. Presented here is a structural mechanistic investigation bacterial GE OtCE15A. belong to carbohydrate esterase...
Rhamnogalacturonan lyase (RG‐lyase) specifically recognizes and cleaves α‐1,4 glycosidic bonds between l ‐rhamnose d ‐galacturonic acids in the backbone of rhamnogalacturonan‐I, a major component plant cell wall polysaccharide, pectin. The three‐dimensional structure RG‐lyase from Aspergillus aculeatus has been determined to 1.5 Å resolution representing first known polysaccharide family 4 an enzyme with this catalytic specificity. 508‐amino acid polypeptide displays unique arrangement three...
Advances in automation have facilitated the widespread adoption of high-throughput vapour-diffusion methods for initial crystallization screening. However, many proteins, screening thousands conditions fails to yield crystals sufficient quality structural characterization. Here, rates crystal identification thaumatin, catalase and myoglobin using microfluidic Crystal Former devices sitting-drop plates are compared. It is shown that results a greater number identified compared with vapour...
<italic>N</italic>-alkylated analogues of 1-deoxynojirimycin inhibit β-glucosidase from white rot fungus. The amino group in the β-glucosidase–iminosugar complex is unprotonated when bound, while an active site carboxylate protonated.
In plant cell walls, covalent bonds between polysaccharides and lignin increase recalcitrance to degradation. Ester are known exist glucuronic acid moieties on glucuronoxylan lignin, these can be cleaved by glucuronoyl esterases (GEs) from carbohydrate esterase family 15 (CE15). GEs found in both bacteria fungi, some microorganisms also encode multiple GEs, although the reason for this is still not fully clear. The fungus Lentithecium fluviatile encodes three CE15 enzymes, of which two have...
The use of retaining glycoside hydrolases as synthetic tools for glycochemistry is highly topical and the focus considerable research. However, due to incomplete identification molecular determinants transglycosylation/hydrolysis partition (t/h), rational engineering create transglycosylases remains challenging. Therefore, understand better factors that underpin transglycosylation in a GH51 α-l-arabinofuranosidase from Thermobacillus xylanilyticus, investigation this enzyme's active site was...