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sordariales - enzymology (152) 152
index medicus (119) 119
enzymes (67) 67
biotechnology & applied microbiology (58) 58
sordariales - genetics (52) 52
fungal proteins - metabolism (48) 48
fungal proteins - chemistry (45) 45
kinetics (44) 44
biochemistry & molecular biology (43) 43
microbiology (41) 41
substrate specificity (37) 37
enzyme stability (35) 35
hydrogen-ion concentration (35) 35
fungal proteins - genetics (34) 34
fungi (31) 31
amino acid sequence (30) 30
hydrolysis (30) 30
analysis (29) 29
purification (28) 28
biotechnology (26) 26
molecular sequence data (26) 26
temperature (26) 26
catalysis (25) 25
laccase (23) 23
life sciences (23) 23
models, molecular (23) 23
oxidases (23) 23
expression (22) 22
cellulose (21) 21
myceliophthora thermophila (21) 21
pichia-pastoris (21) 21
recombinant proteins - metabolism (21) 21
laccase - metabolism (20) 20
protein conformation (19) 19
cloning (18) 18
proteins (18) 18
cloning, molecular (17) 17
gene (17) 17
gene expression (17) 17
laccase - chemistry (17) 17
molecular weight (17) 17
recombinant proteins - chemistry (16) 16
recombinant proteins - genetics (16) 16
trichoderma-reesei (16) 16
biocatalysis (15) 15
crystal-structure (15) 15
glucose (15) 15
lignin (15) 15
oxidation (15) 15
oxidation-reduction (15) 15
physiological aspects (15) 15
pichia - genetics (15) 15
pichia pastoris (15) 15
biomass (14) 14
chemistry, applied (14) 14
degradation (14) 14
protein (14) 14
cellulase (13) 13
fermentation (13) 13
hot temperature (13) 13
research (13) 13
saccharomyces-cerevisiae (13) 13
stability (13) 13
binding sites (12) 12
biophysics (12) 12
cellulase - metabolism (12) 12
cellulose 1,4-beta-cellobiosidase - metabolism (12) 12
food science & technology (12) 12
microbial genetics and genomics (12) 12
sordariales - chemistry (12) 12
sordariales - metabolism (12) 12
animals (11) 11
catalytic domain (11) 11
cellobiose dehydrogenase (11) 11
cellulose - metabolism (11) 11
chemistry (11) 11
crystallography, x-ray (11) 11
enzymes, immobilized - chemistry (11) 11
hydrolases (11) 11
hydrolyse (11) 11
sequence alignment (11) 11
biochemical research methods (10) 10
carboxylic ester hydrolases - metabolism (10) 10
cellulose 1,4-beta-cellobiosidase - chemistry (10) 10
chemical properties (10) 10
electrodes (10) 10
enzymatic-hydrolysis (10) 10
genetic aspects (10) 10
hydrolase (10) 10
lignin - metabolism (10) 10
lignocellulose (10) 10
polymers (10) 10
recombinant proteins - isolation & purification (10) 10
studies (10) 10
thermophiler pilz (10) 10
thermophilic-fungi (10) 10
xylanase (10) 10
binding (9) 9
biochemistry, general (9) 9
carbohydrate dehydrogenases - chemistry (9) 9
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1. Full Text Production of d-glucuronic acid from myo-inositol using Escherichia coli whole-cell biocatalyst overexpressing a novel myo-inositol oxygenase from Thermothelomyces thermophile
by Teng, Fei and You, Ran and Hu, Meirong and Liu, Weifeng and Wang, Lei and Tao, Yong
Enzyme and Microbial Technology, ISSN 0141-0229, 08/2019, Volume 127, pp. 70 - 74
D-glucuronic acid (GlcUA) is an important intermediate with numerous applications in the food, cosmetics, and pharmaceutical industries. Its biological... 
Myo-inositol oxygenase | Whole-cell biocatalyst | Thermothelomyces thermophile | D-glucuronic acid | Recombinant Proteins - metabolism | Gene Expression | Arabidopsis - enzymology | Cryptococcus neoformans - enzymology | Inositol - metabolism | Cryptococcus neoformans - genetics | Glucuronic Acid - metabolism | Chaetomium - enzymology | Recombinant Proteins - genetics | Chaetomium - genetics | Arabidopsis - genetics | Animals | Escherichia coli - genetics | Inositol Oxygenase - metabolism | Biotransformation | Escherichia coli - metabolism | Inositol Oxygenase - genetics | Mice | Sordariales - enzymology | Sordariales - genetics | Arabidopsis thaliana | Enzymes | Inositol | Escherichia coli | Genomics | Production processes | Organic acids | Cosmetics industry
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2. Full Text Molecular and catalytic properties of fungal extracellular cellobiose dehydrogenase produced in prokaryotic and eukaryotic expression systems
by Ma, Su and Preims, Marita and Piumi, François and Kappel, Lisa and Seiboth, Bernhard and Record, Eric and Kracher, Daniel and Ludwig, Roland
Microbial Cell Factories, ISSN 1475-2859, 02/2017, Volume 16, Issue 1, p. 37
Background: Cellobiose dehydrogenase (CDH) is an extracellular enzyme produced by lignocellulolytic fungi. cdh gene expression is high in cellulose containing... 
Glycoforms | Cellobiose dehydrogenase | Aspergillus niger | Escherichia coli | Cofactor loading | Pichia pastoris | Trichoderma reesei | Heterologous expression | ASPERGILLUS-NIGER | SACCHARIFICATION | TRANSFORMATION SYSTEM | CELLULOSE DEGRADATION | CLONING | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PURIFICATION | PICHIA-PASTORIS | PROTEINS | NEUROSPORA-CRASSA | Recombinant Proteins - metabolism | Gene Expression | Temperature | Escherichia coli - enzymology | Carbohydrate Dehydrogenases - isolation & purification | Enzyme Stability | Aspergillus niger - enzymology | Glycosylation | Trichoderma - genetics | Trichoderma - enzymology | Pichia - enzymology | Aspergillus niger - genetics | Escherichia coli - genetics | Pichia - genetics | Catalysis | Kinetics | Culture Media - chemistry | Sordariales - enzymology | Carbohydrate Dehydrogenases - genetics | Carbohydrate Dehydrogenases - metabolism | Life Sciences | Food and Nutrition
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3. Full Text BcNoxD, a putative ER protein, is a new component of the NADPH oxidase complex in Botrytis cinerea
by Siegmund, Ulrike and Marschall, Robert and Tudzynski, Paul
Molecular Microbiology, ISSN 0950-382X, 03/2015, Volume 95, Issue 6, pp. 988 - 1005
Summary NADPH oxidases (Nox) are major enzymatic producer of reactive oxygen species (ROS). In fungi these multi‐enzyme complexes are involved in sexual... 
P22(PHOX) SUBUNIT | DISULFIDE-ISOMERASE | OXIDATIVE STRESS | NOX-FAMILY | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MICROBIOLOGY | ASCOSPORE GERMINATION | CELL-DIFFERENTIATION | SEXUAL DEVELOPMENT | PLANT INFECTION | GRAY MOLD FUNGUS | Endoplasmic Reticulum - enzymology | Gene Expression Regulation, Fungal | NADPH Oxidases - chemistry | Sequence Deletion | Reactive Oxygen Species - metabolism | NADPH Oxidases - metabolism | Multienzyme Complexes - metabolism | Botrytis - enzymology | Multienzyme Complexes - genetics | Phylogeny | Botrytis - genetics | Botrytis - physiology | Spores, Fungal - physiology | Phenotype | Hyphae - metabolism | Spores, Fungal - ultrastructure | Base Sequence | NADPH Oxidases - genetics | Cell Membrane - metabolism | Sordariales - enzymology | Sordariales - genetics | Fungal Proteins - metabolism | Oxidases
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4. Full Text Carbonic anhydrases in fungi
by Elleuche, Skander and Poggeler, Stefanie
Microbiology, ISSN 1350-0872, 01/2010, Volume 156, Issue 1, pp. 23 - 29
Institute of Microbiology and Genetics, Department of Genetics of Eukaryotic Microorganisms, Georg-August University, Göttingen, Germany Carbonic anhydrases... 
ANTIOXIDANT ACTIVITY | FRUITING BODY DEVELOPMENT | ACTIVE-SITE | ADENYLYL-CYCLASE | ESCHERICHIA-COLI | MICROBIOLOGY | SORDARIA-MACROSPORA | CRYPTOCOCCUS-NEOFORMANS | GENE NCE103 | SACCHAROMYCES-CEREVISIAE | BETA-CLASS | Candida albicans - genetics | Cryptococcus neoformans - enzymology | Carbonic Anhydrases - genetics | Cryptococcus neoformans - genetics | Bicarbonates - metabolism | Fruiting Bodies, Fungal - growth & development | Sordariales - enzymology | Sordariales - genetics | Candida albicans - enzymology | Carbonic Anhydrases - metabolism
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5. Full Text Enzymatic Synthesis of Lignin‐Based Concrete Dispersing Agents
by Jankowska, Dagmara and Heck, Tobias and Schubert, Mark and Yerlikaya, Alpaslan and Weymuth, Christophe and Rentsch, Daniel and Schober, Irene and Richter, Michael
ChemBioChem, ISSN 1439-4227, 07/2018, Volume 19, Issue 13, pp. 1365 - 1369
Lignin is the most abundant aromatic biopolymer, functioning as an integral component of woody materials. In its unmodified form it shows limited water... 
oxidoreductases | dispersing agents | green chemistry | lignins | biocatalysis | Green chemistry | Biocatalysis | Oxidoreductases | Dispersing agents | Lignins | CHEMISTRY, MEDICINAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | LACCASES | KRAFT LIGNIN | Fungal Proteins - chemistry | Lignin - chemical synthesis | 4-Aminobenzoic Acid - chemistry | Silicon Dioxide - chemistry | Bacterial Proteins - chemistry | Solubility | Sulfanilic Acids - chemistry | Laccase - chemistry | Trametes - enzymology | Calcium Carbonate - chemistry | Construction Materials | Green Chemistry Technology - methods | Lignin - analogs & derivatives | Water - chemistry | Streptomyces coelicolor - enzymology | Bacillus pumilus - enzymology | Sordariales - enzymology | Enzymes | Lignin | Usage | Green technology | Catalysis | Paper industry | Enzymatic synthesis | Concrete additives | Additives | Transformation | Paper mills | Foaming agents | pH effects | Biopolymers | Dispersion | Pulp | Pulp and paper industry | Lignosulfonates | Synthesis | Sulfanilic acid | Acids | Reagents | Sulfonation | Concrete | Polymers | Mortars (material)
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6. Full Text Structural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substrates
by Simmons, T.J and Frandsen, K.E.H and Ciano, L and Tryfona, T and Lenfant, N and Poulsen, J.C and Wilson, L.F.L and Tandrup, T and Tovborg, M and Schnorr, K and Johansen, K.S and Henrissat, B and Walton, P.H and Lo Leggio, L and Dupree, P
Nature Communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 1064 - 12
Lytic polysaccharide monooxygenases (LPMOs) are industrially important copper-dependent enzymes that oxidatively cleave polysaccharides. Here we present a... 
LIGNOCELLULOSIC BIOMASS | SPECIFICITY | MULTIDISCIPLINARY SCIENCES | AA9 | ACTIVE ENZYMES | CLEAVAGE | OXIDATIVE-DEGRADATION | CELLULOSE | DISCOVERY | FAMILY | METALLOENZYME | Fungal Proteins - chemistry | Catalytic Domain | Electron Spin Resonance Spectroscopy | Models, Molecular | Substrate Specificity | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Polysaccharides - metabolism | Copper - chemistry | Polysaccharides - chemistry | Polyporaceae - enzymology | Sordariales - enzymology | Fungal Proteins - metabolism | Binding | Carbohydrates | Ordination | Cellulose | Xylan | Oligosaccharides | Monooxygenase | Substrates | Fungi | Glucan | Xyloglucan | Polysaccharides | Glucans | Determinants | Catalysis | Copper | Saccharides | Structural analysis | Structure-function relationships | Biotechnology | Polyporaceae | Neurons and Cognition | Neurobiology | Innate immunity | Emerging diseases | Mixed Function Oxygenases | Life Sciences | Immunology | Biomolecules | Pharmaceutical sciences | Sordariales | Quantitative Methods | Biochemistry, Molecular Biology | Fungal Proteins | Pharmacology | Bacteriology | Virology | Human health and pathology | Microbiology and Parasitology | Infectious diseases
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7. Full Text Cellulase–lignin interactions—The role of carbohydrate-binding module and pH in non-productive binding
by Rahikainen, Jenni Liisa and Evans, James David and Mikander, Saara and Kalliola, Anna and Puranen, Terhi and Tamminen, Tarja and Marjamaa, Kaisa and Kruus, Kristiina
Enzyme and Microbial Technology, ISSN 0141-0229, 10/2013, Volume 53, Issue 5, pp. 315 - 321
Non-productive cellulase adsorption onto lignin is a major inhibitory mechanism preventing enzymatic hydrolysis of lignocellulosic feedstocks. Therefore,... 
Lignin | Non-productive binding | Lignocellulose | Cellulase | Electrostatic interaction | CBM | REESEI CELLOBIOHYDROLASE-I | STEAM PRETREATED SOFTWOOD | TRICHODERMA-REESEI | ENZYMATIC-HYDROLYSIS | ADSORPTION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ENZYMES | MELANOCARPUS-ALBOMYCES | PROTEINS | DOMAINS | CRYSTALLINE CELLULOSE | Cellulase - chemistry | Recombinant Proteins - metabolism | Mutagenesis, Site-Directed | Cellulase - genetics | Catalytic Domain - genetics | Lignin - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Trichoderma - genetics | Trichoderma - enzymology | Static Electricity | Hydrolysis | Cellulase - metabolism | Lignin - metabolism | Adsorption | Hydrophobic and Hydrophilic Interactions | Sordariales - enzymology | Sordariales - genetics | Cellulose - metabolism | Hydrogen-Ion Concentration | Chemical properties | Hydrogen-ion concentration | Cellulose
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8. Full Text Functional Expression of a Fungal Laccase in Saccharomyces cerevisiae by Directed Evolution
by Thomas Bulter and Miguel Alcalde and Volker Sieber and Peter Meinhold and Christian Schlachtbauer and Frances H. Arnold
Applied and Environmental Microbiology, ISSN 0099-2240, 02/2003, Volume 69, Issue 2, pp. 987 - 995
ERRATUM ( vol. 69 , p. 5037 ) Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg... 
NONPHENOLIC LIGNIN | TRAMETES-VERSICOLOR | BILIRUBIN OXIDASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | MOLECULAR EVOLUTION | RHUS-VERNICIFERA LACCASE | GENE-EXPRESSION | PICHIA-PASTORIS | MICROBIOLOGY | 4-ELECTRON REDUCTION | HETEROLOGOUS EXPRESSION | HORSERADISH-PEROXIDASE | Oxidoreductases - metabolism | Oxidoreductases - genetics | Saccharomyces cerevisiae - genetics | Models, Molecular | Substrate Specificity | Directed Molecular Evolution | Glycosylation | Hydrazones - metabolism | Oxidoreductases - chemistry | Sulfonic Acids - metabolism | Recombination, Genetic | Saccharomyces cerevisiae - enzymology | Sordariales - enzymology | Sordariales - genetics | Benzothiazoles | Laccase | Fungi | Physiological aspects | Catalysis | Gene expression | Analysis | Enzymology and Protein Engineering
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9. Full Text Development of tailor-made synergistic cellulolytic enzyme system for saccharification of steam exploded sugarcane bagasse
by Bunterngsook, Benjarat and Laothanachareon, Thanaporn and Chotirotsukon, Chayanon and Inoue, Hiroyuki and Fujii, Tatsuya and Hoshino, Tamotsu and Roongsawang, Niran and Kuboon, Sanchai and Kraithong, Wasawat and Techanan, Wikanda and Kraikul, Natthakorn and Champreda, Verawat
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 04/2018, Volume 125, Issue 4, pp. 390 - 396
Designing a tailor-made synergistic system is a promising strategy for developing an effective enzyme for saccharification of lignocellulosic materials. In... 
Glycosyl hydrolase | Biorefinery | Synergy | Lignocellulose | Mixture design | LIGNOCELLULOSIC BIOMASS | FOOD SCIENCE & TECHNOLOGY | IDENTIFICATION | ETHANOL FERMENTATION | CELLULASE | PRETREATMENT | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | RICE STRAW | EFFICIENT HYDROLYSIS | WALL DEGRADING ENZYMES | ACREMONIUM-CELLULOLYTICUS | GLYCOSYL HYDROLASES | Endo-1,4-beta Xylanases - metabolism | Saccharum - chemistry | Xylose - metabolism | Talaromyces - enzymology | Biomass | Hydrolysis | Cellulose - chemistry | Cellulose 1,4-beta-Cellobiosidase - metabolism | Steam | Glucose - metabolism | beta-Glucosidase - metabolism | Aspergillus - enzymology | Sordariales - enzymology | Cellulose - metabolism | Enzymes | Green technology | Genetically modified organisms | Genetic engineering | Glucose | Biotechnological microorganisms | Sugarcane | Microbial biotechnology | Nanotechnology | Dextrose
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10. Full Text Improvement in thermostability of an Achaetomium sp. strain Xz8 endopolygalacturonase via the optimization of charge-charge interactions
by Tu, Tao and Luo, Huiying and Meng, Kun and Cheng, Yanli and Ma, Rui and Shi, Pengjun and Huang, Huoqing and Bai, Yingguo and Wang, Yaru and Zhang, Lujia and Yao, Bin
Applied and Environmental Microbiology, ISSN 0099-2240, 2015, Volume 81, Issue 19, pp. 6938 - 6944
Improving enzyme thermostability is of importance for widening the spectrum of application of enzymes. In this study, a structure-based rational design... 
THERMAL-STABILITY | ASPERGILLUS-NIGER | XYLANASE | PROTEIN STABILITY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | CRYSTAL-STRUCTURE | POLYGALACTURONASE | PURIFICATION | EQUATIONS | MICROBIOLOGY | ELECTROSTATICS | TITRATION CURVES | Fungal Proteins - chemistry | Mutagenesis, Site-Directed | Polygalacturonase - chemistry | Enzyme Stability | Fungal Proteins - genetics | Hot Temperature | Polygalacturonase - metabolism | Sordariales - chemistry | Protein Engineering | Polygalacturonase - genetics | Protein Conformation | Kinetics | Sordariales - enzymology | Sordariales - genetics | Fungal Proteins - metabolism | Hydrogen-Ion Concentration | Fungi | Proteins | Genetic aspects | Research | Conformation | Enzymology and Protein Engineering
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11. Full Text Engineered thermostable fungal Cel6A and Cel7A cellobiohydrolases hydrolyze cellulose efficiently at elevated temperatures
by Wu, Indira and Arnold, Frances H
Biotechnology and Bioengineering, ISSN 0006-3592, 07/2013, Volume 110, Issue 7, pp. 1874 - 1883
Thermostability is an important feature in industrial enzymes: it increases biocatalyst lifetime and enables reactions at higher temperatures, where faster... 
proline substitutions | enzyme thermostability | cellulase synergy | biofuel | fungal cellulase | CBHII | Enzyme thermostability | Fungal cellulase | Proline substitutions | Biofuel | Cellulase synergy | STRUCTURE-GUIDED RECOMBINATION | PROTEIN STABILITY | TRICHODERMA-REESEI | ETHANOL-PRODUCTION | CELLULASES | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ENZYMES | REDUCES RECALCITRANCE | HYPOCREA-JECORINA | DEGRADATION | HUMICOLA-INSOLENS | Recombinant Proteins - metabolism | Directed Molecular Evolution - methods | Temperature | Hypocrea - enzymology | Cellulose 1,4-beta-Cellobiosidase - genetics | Enzyme Stability | Models, Molecular | Recombinant Proteins - chemistry | Crystallography, X-Ray | Recombinant Proteins - genetics | Hydrolysis | Cellulose 1,4-beta-Cellobiosidase - chemistry | Cellulose 1,4-beta-Cellobiosidase - metabolism | Mutagenesis | Recombination, Genetic | Hypocrea - genetics | Protein Conformation | Kinetics | Sordariales - enzymology | Sordariales - genetics | Cellulose - metabolism | Proline | Enzymes | Biomass energy | Cellulose | Index Medicus
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12. Full Text Activation of bacterial lytic polysaccharide monooxygenases with cellobiose dehydrogenase
by Loose, Jennifer S. M and Forsberg, Zarah and Kracher, Daniel and Scheiblbrandner, Stefan and Ludwig, Roland and Eijsink, Vincent G. H and Vaaje‐Kolstad, Gustav
Protein Science, ISSN 0961-8368, 12/2016, Volume 25, Issue 12, pp. 2175 - 2186
Lytic polysaccharide monooxygenases (LPMOs) represent a recent addition to the carbohydrate‐active enzymes and are classified as auxiliary activity (AA)... 
electron transfer | cellulose | electron donor | hydrogen peroxide | lytic polysaccharide monooxygenase | enzyme kinetics | cellobiose dehydrogenase | chitin | PROTEIN | BROWN-ROT FUNGUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | OXIDATIVE CELLULOSE DEGRADATION | PHANEROCHAETE-CHRYSOSPORIUM | ELECTRON-TRANSFER | OXIDASE | STRUCTURAL BASIS | PICHIA-PASTORIS | NEUROSPORA-CRASSA | FLAVOCYTOCHROME | Fungal Proteins - chemistry | Oxidation-Reduction | Bacterial Proteins - chemistry | Bacteria - enzymology | Chitin - chemistry | Lactose - chemistry | Mixed Function Oxygenases - chemistry | Sordariales - enzymology | Carbohydrate Dehydrogenases - chemistry | Lactose | Chitin | Hydrogen peroxide | Oxidoreductases | Enzyme kinetics | Cellulose | Enzymes | Biodegradation | Carbohydrates | Cellobiose dehydrogenase | Oxygen | Correlation | Ascorbic acid | Electron transfer | Activation | Dehydrogenase | Chemical compounds | Degradation | Fungi | Polysaccharides | Cellobiose | Chemical bonds | Bacteria | Oxidation | Catalysis | Copper | Saccharides
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13. Full Text Discovery of a xylooligosaccharide oxidase from Myceliophthora thermophila C1
by Ferrari, Alessano R and Rozeboom, Henriëtte J and Dobruchowska, Justyna M and van Leeuwen, Sander S and Vugts, Aniek S C and Koetsier, Martijn J and Visser, Jaap and Fraaije, Marco W
The Journal of Biological Chemistry, ISSN 0021-9258, 11/2016, Volume 291, Issue 45, pp. 23709 - 23718
By inspection of the predicted proteome of the fungus Myceliophthora thermophila C1 for VAO-type flavoprotein oxidases, a putative oligosaccharide oxidase was... 
To be checked by Faculty | oxidase | OXIDATION | GLUCOOLIGOSACCHARIDE OXIDASE | flavin adenine dinucleotide (FAD) | CAZy | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHITOOLIGOSACCHARIDE OXIDASE | carbohydrate processing | ACCEPTOR OXIDOREDUCTASE | LACTOBIONIC ACID | xylan | carbohydrate | oligosaccharide | CELLOBIOSE DEHYDROGENASE | xylose | PURIFICATION | crystal structure | FUSARIUM-GRAMINEARUM | Amino Acid Sequence | Xylans - metabolism | Oxidation-Reduction | Oxidoreductases - metabolism | Disaccharides - metabolism | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Glucuronates - metabolism | Oligosaccharides - metabolism | Sordariales - metabolism | Oxidoreductases - chemistry | Sordariales - chemistry | Flavin-Adenine Dinucleotide - metabolism | Sequence Alignment | Protein Conformation | Sordariales - enzymology | Enzymology
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14. Full Text Engineered Humicola insolens cutinase for efficient cellulose acetate deacetylation
by Shirke, Abhijit N and Butterfoss, Glenn L and Saikia, Rakhi and Basu, Aditya and Maria, Leonardo and Svendsen, Allan and Gross, Richard A
Biotechnology Journal, ISSN 1860-6768, 08/2017, Volume 12, Issue 8, pp. 1700188 - n/a
Cutinases comprise a family of esterases with broad hydrolytic activity for chain and pendant ester groups. This work aimed to identify and improve an... 
Cutinase | Substrate docking | Enzyme kinetics | Cellulose acetate deacetylation | MOLECULAR-WEIGHT | CARBOHYDRATE-BINDING MODULE | DEPOLYMERASE | BIOCHEMICAL RESEARCH METHODS | SURFACE MODIFICATION | OPPORTUNITIES | FIBERS | ACETYLXYLAN ESTERASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | DEGRADATION | SUBSTITUENT DISTRIBUTION | POLYETHYLENE TEREPHTHALATE | Carboxylic Ester Hydrolases - chemistry | Structure-Activity Relationship | Amino Acid Sequence - genetics | Fusarium - enzymology | Sordariales - metabolism | Hydrolysis | Cellulose - chemistry | Aspergillus oryzae - genetics | Cellulose - genetics | Aspergillus oryzae - enzymology | Protein Conformation | Carboxylic Ester Hydrolases - genetics | Acetylation | Catalysis | Kinetics | Sordariales - enzymology | Binding Sites | Circular Dichroism | Fusarium - genetics | Carboxylic Ester Hydrolases - metabolism | Cellulose - analogs & derivatives | Cellulose - metabolism | Enzymes | Gene mutations | Hydrogen | Analysis | Cellulose | Green technology | Green chemistry
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