about
P688
The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharidesA new black Aspergillus species, A. vadensis, is a promising host for homologous and heterologous protein production.Construction of engineered bifunctional enzymes and their overproduction in Aspergillus niger for improved enzymatic tools to degrade agricultural by-products.Synthesis of highly water-soluble feruloyl diglycerols by esterification of an Aspergillus niger feruloyl esterase.Multiple amino acid substitutions significantly improve the thermostability of feruloyl esterase A from Aspergillus niger.Uncovering the genome-wide transcriptional responses of the filamentous fungus Aspergillus niger to lignocellulose using RNA sequencingTranscriptome analysis of Aspergillus niger grown on sugarcane bagasse.Design and production in Aspergillus niger of a chimeric protein associating a fungal feruloyl esterase and a clostridial dockerin domain.RNA-sequencing reveals the complexities of the transcriptional response to lignocellulosic biofuel substrates in Aspergillus niger.Regulation of the feruloyl esterase (faeA) gene from Aspergillus niger.An Aspergillus niger esterase (ferulic acid esterase III) and a recombinant Pseudomonas fluorescens subsp. cellulosa esterase (Xy1D) release a 5-5' ferulic dehydrodimer (diferulic acid) from barley and wheat cell walls.The intra- and extracellular proteome of Aspergillus niger growing on defined medium with xylose or maltose as carbon substrated-Xylose concentration-dependent hydrolase expression profiles and the function of CreA and XlnR in Aspergillus niger.The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds.Spatial differentiation in the vegetative mycelium of Aspergillus niger.Altering the activation mechanism in Thermomyces lanuginosus lipase.Targeting expression of a fungal ferulic acid esterase to the apoplast, endoplasmic reticulum or golgi can disrupt feruloylation of the growing cell wall and increase the biodegradability of tall fescue (Festuca arundinacea).Heterologous production of the Piromyces equi cinnamoyl esterase in Trichoderma reesei for biotechnological applications.Study of new feruloyl esterases to understand lipase evolution: the case of Bacillus flexus.Heterogenic expression of genes encoding secreted proteins at the periphery of Aspergillus niger colonies.Expression profiling of pectinolytic genes from Aspergillus niger.Deletion of flbA results in increased secretome complexity and reduced secretion heterogeneity in colonies of Aspergillus niger.High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris.Overproduction of the Aspergillus niger feruloyl esterase for pulp bleaching application.Mutational analysis of a feruloyl esterase from Aspergillus awamori involved in substrate discrimination and pH dependence.Release of ferulic acid from wheat bran by a ferulic acid esterase (FAE-III) from Aspergillus niger.Overexpression of Aspergillus tubingensis faeA in protease-deficient Aspergillus niger enables ferulic acid production from plant material.AFM studies of water-soluble wheat arabinoxylans--effects of esterase treatment.Identification of active site residues in a ferulic acid esterase (FAE-III) from Aspergillus niger.Chemical and thermal stability of ferulic acid esterase-III from Aspergillus niger.Expression of a fungal ferulic acid esterase increases cell wall digestibility of tall fescue (Festuca arundinacea).Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger.Exploration of members of Aspergillus sections Nigri, Flavi, and Terrei for feruloyl esterase production.Identification of amino acid residues responsible for increased thermostability of feruloyl esterase A from Aspergillus niger using the PoPMuSiC algorithm.Expression in Escherichia coli, refolding and crystallization of Aspergillus niger feruloyl esterase A using a serial factorial approach.Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A.Spatially Resolving the Secretome within the Mycelium of the Cell Factory Aspergillus nigerCreA modulates the XlnR-induced expression on xylose of Aspergillus niger genes involved in xylan degradationEsterification of ferulic acid with polyols using a ferulic acid esterase from Aspergillus nigerFeruloyl esterases as a tool for the release of phenolic compounds from agro-industrial by-products
P921
Q24673395-C02FA156-2BBA-4D2F-B36D-9F3BB4BBE933Q30941809-77D1E70D-9164-44FB-81C0-30A821D2E1A0Q34232451-4B68C4AE-22EB-4D3B-8845-C039E38B2825Q34242784-FA45A929-30C9-4707-845E-A16BAF5F44DAQ34276399-D5C246D6-9F07-4AB8-9724-F4C088385CC2Q34388528-9AF11630-C262-49F5-B124-6B2C4AE25AD7Q35560051-8A4EAA2C-B66D-4619-98E4-F8FA194213A7Q37701854-378C426A-2D0E-46C2-BDFF-D3AA01A0E95CQ38954496-BE8F4080-2C17-4331-B4FC-DA78051C95BEQ39484262-E46902DB-D811-44D2-8335-8DDFA7EB7662Q39801374-79290D15-33EF-42BE-845A-1908844F34C8Q40687205-14032695-4217-498A-8D34-E4CDEE37C6C5Q41771971-FB1BA415-0EAB-451F-B408-EE3383D8C65EQ41957115-94329327-8DB1-482C-867C-029013E594ACQ42150085-382CA2D6-C253-4FD3-B9C6-0CA01A17328CQ42662775-C24A76BD-67CB-4232-A1DF-109A38C7FFCCQ43183860-B097B8B0-B79A-4F6C-9951-B68DDAFA5ECCQ43271367-6C7005E7-D410-4B64-8698-4BF68B4F321FQ43657722-C9829CD7-447D-45B0-9B80-CFC94580680AQ44019957-4396B79C-8ADB-40B1-964B-DB73163846A7Q44185052-81D65BBB-7B16-4CA8-8AF7-9AC069601DEBQ44376031-5479B122-9842-4D77-99D9-8552B58BEF3BQ44408172-641EE3F6-904A-49B0-B392-A8A212200D1CQ44438967-E6B81282-642D-4BB2-9B2F-3B0ECD38FB0EQ45269606-A2B63382-E977-4AAA-889B-C18CF0D54591Q46377741-C83A0064-E895-4CE6-86E3-363F214B8DF7Q46452449-1584F9B1-B8F6-4245-A598-148DD68A2779Q46580143-02217AC0-F90D-4458-8CFC-87325A1CF3E1Q46718397-9BC1B86B-EE2B-4749-A2C3-1524D7C48A01Q46802407-E385FE74-9F1E-475D-AE51-D692C115DA78Q46845828-B86883B0-2982-42B8-A128-82173D14EDE3Q46988372-6466D3B0-47AE-468B-96F8-0402D66BA204Q51103214-54D8DC41-5EB2-4A2A-A0A9-89D506439CCEQ51666140-71715FBF-C159-452A-87CB-49EF4A8BD597Q54440667-94C302FC-CAB7-40A5-8495-BBAE0AAF7C80Q54454190-1F92CB23-A250-4D17-8BF4-6EA10E774729Q57666112-C6C6ABCB-6D07-4C7A-8C7E-3D1378711285Q61485917-869D1983-62DA-4192-8FC7-795C20943C33Q61551517-044DADBA-EEE3-4631-AC95-DBB04A644585Q61551523-6EB3B1B1-314B-4CB2-81CF-822D0B16C61E
P921
description
protein
@id
proteïne in An09g00120-T
@nl
protèin
@ace
name
An09g00120-T
@nl
Feruloyl esterase
@en
type
label
An09g00120-T
@nl
Feruloyl esterase
@en
prefLabel
An09g00120-T
@nl
Feruloyl esterase
@en
P279
P31
P3382
An09g00120-T