Dyadic Netherlands

Wageningen, Netherlands

Dyadic Netherlands

Wageningen, Netherlands

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Visser H.,Dyadic Netherlands | Joosten V.,Dyadic Netherlands | Punt P.J.,TNO | Punt P.J.,Leiden University | And 9 more authors.
Industrial Biotechnology | Year: 2011

The filamentous fungus C1 was developed into an expression platform for screening and production of diverse industrial enzymes. C1 shows a lowviscosity morphology in submerged culture, enabling the use of complex growth and production media. This morphology furthermore allowed C1 to be used as a host for high-throughput robotic screening of gene libraries. A C1-genetic toolbox was developed, which enabled the generation of a large collection of dedicated C1 host strains and gene-expression strategies. The 38 Mbp genome was sequenced and found to be rich in biomass-hydrolyzing-enzyme-encoding genes. C1 production strains have been developed that produce large quantities of these enzyme mixtures (up to 100 g/L total protein). Recombinant C1 strains were constructed that produce single enzymes in a relatively pure form, facilitating enzyme purification and characterization, as well as for commercial applications. Molecular phylogenetic studies revealed that C1, previously classified as Chrysosporium lucknowense based on morphological characteristics, is actually a Myceliophthora thermophila isolate. In addition, C1 has proven to be a source of novel industrial enzymes, and the C1-technology platform developed has been applied as a tool for research on and production of industrial enzymes for various industrial applications, such as biofuels and biorefineries. © 2011 Mary Ann Liebert, Inc.


News Article | November 8, 2016
Site: www.newsmaker.com.au

This report studies Dextranase in Global market, especially in North America, Europe, China, Japan, Southeast Asia and India, focuses on top manufacturers in global market, with capacity, production, price, revenue and market share for each manufacturer, covering  Novozymes  Amano  Specialty Enzymes  Aumgene Biosciences  Dyadic Netherlands  EN Group  SunHY  Sunson  Vland Biotech Group  Shandong Longda Bio-Products  Yangshao Bo-Chemical  Shandong Jienuo Enzyme  Hunan Hong Ying Xiang Biochemistry  Shandong Sukahan Bio-Technology  Hunan Lerkam Blology  Youtell Biotechnology  Market Segment by Regions, this report splits Global into several key Regions, with production, consumption, revenue, market share and growth rate of Dextranase in these regions, from 2011 to 2021 (forecast), like  North America  Europe  China  Japan  Southeast Asia  India For more information or any query mail at [email protected] Split by product type, with production, revenue, price, market share and growth rate of each type, can be divided into  Type I  Type II  Type III  Split by application, this report focuses on consumption, market share and growth rate of Dextranase in each application, can be divided into  Application 1  Application 2  Application 3 Global Dextranase Market Research Report 2016  1 Dextranase Market Overview  1.1 Product Overview and Scope of Dextranase  1.2 Dextranase Segment by Type  1.2.1 Global Production Market Share of Dextranase by Type in 2015  1.2.2 Type I  1.2.3 Type II  1.2.4 Type III  1.3 Dextranase Segment by Application  1.3.1 Dextranase Consumption Market Share by Application in 2015  1.3.2 Application 1  1.3.3 Application 2  1.3.4 Application 3  1.4 Dextranase Market by Region  1.4.1 North America Status and Prospect (2011-2021)  1.4.2 Europe Status and Prospect (2011-2021)  1.4.3 China Status and Prospect (2011-2021)  1.4.4 Japan Status and Prospect (2011-2021)  1.4.5 Southeast Asia Status and Prospect (2011-2021)  1.4.6 India Status and Prospect (2011-2021)  1.5 Global Market Size (Value) of Dextranase (2011-2021) 2 Global Dextranase Market Competition by Manufacturers  2.1 Global Dextranase Capacity, Production and Share by Manufacturers (2015 and 2016)  2.2 Global Dextranase Revenue and Share by Manufacturers (2015 and 2016)  2.3 Global Dextranase Average Price by Manufacturers (2015 and 2016)  2.4 Manufacturers Dextranase Manufacturing Base Distribution, Sales Area and Product Type  2.5 Dextranase Market Competitive Situation and Trends  2.5.1 Dextranase Market Concentration Rate  2.5.2 Dextranase Market Share of Top 3 and Top 5 Manufacturers  2.5.3 Mergers & Acquisitions, Expansion 3 Global Dextranase Capacity, Production, Revenue (Value) by Region (2011-2016)  3.1 Global Dextranase Capacity and Market Share by Region (2011-2016)  3.2 Global Dextranase Production and Market Share by Region (2011-2016)  3.3 Global Dextranase Revenue (Value) and Market Share by Region (2011-2016)  3.4 Global Dextranase Capacity, Production, Revenue, Price and Gross Margin (2011-2016)  3.5 North America Dextranase Capacity, Production, Revenue, Price and Gross Margin (2011-2016)  3.6 Europe Dextranase Capacity, Production, Revenue, Price and Gross Margin (2011-2016)  3.7 China Dextranase Capacity, Production, Revenue, Price and Gross Margin (2011-2016)  3.8 Japan Dextranase Capacity, Production, Revenue, Price and Gross Margin (2011-2016)  3.9 Southeast Asia Dextranase Capacity, Production, Revenue, Price and Gross Margin (2011-2016)  3.10 India Dextranase Capacity, Production, Revenue, Price and Gross Margin (2011-2016) 4 Global Dextranase Supply (Production), Consumption, Export, Import by Regions (2011-2016)  4.1 Global Dextranase Consumption by Regions (2011-2016)  4.2 North America Dextranase Production, Consumption, Export, Import by Regions (2011-2016)  4.3 Europe Dextranase Production, Consumption, Export, Import by Regions (2011-2016)  4.4 China Dextranase Production, Consumption, Export, Import by Regions (2011-2016)  4.5 Japan Dextranase Production, Consumption, Export, Import by Regions (2011-2016)  4.6 Southeast Asia Dextranase Production, Consumption, Export, Import by Regions (2011-2016)  4.7 India Dextranase Production, Consumption, Export, Import by Regions (2011-2016) 5 Global Dextranase Production, Revenue (Value), Price Trend by Type  5.1 Global Dextranase Production and Market Share by Type (2011-2016)  5.2 Global Dextranase Revenue and Market Share by Type (2011-2016)  5.3 Global Dextranase Price by Type (2011-2016)  5.4 Global Dextranase Production Growth by Type (2011-2016) For more information or any query mail at [email protected] Wise Guy Reports is part of the Wise Guy Consultants Pvt. Ltd. and offers premium progressive statistical surveying, market research reports, analysis & forecast data for industries and governments around the globe. Wise Guy Reports features an exhaustive list of market research reports from hundreds of publishers worldwide. We boast a database spanning virtually every market category and an even more comprehensive collection of market research reports under these categories and sub-categories.


Frommhagen M.,Wageningen University | Sforza S.,Wageningen University | Sforza S.,University of Parma | Westphal A.H.,Wageningen University | And 6 more authors.
Biotechnology for Biofuels | Year: 2015

Background: Many agricultural and industrial food by-products are rich in cellulose and xylan. Their enzymatic degradation into monosaccharides is seen as a basis for the production of biofuels and bio-based chemicals. Lytic polysaccharide monooxygenases (LPMOs) constitute a group of recently discovered enzymes, classified as the auxiliary activity subgroups AA9, AA10, AA11 and AA13 in the CAZy database. LPMOs cleave cellulose, chitin, starch and β-(1 → 4)-linked substituted and non-substituted glucosyl units of hemicellulose under formation of oxidized gluco-oligosaccharides. Results: Here, we demonstrate a new LPMO, obtained from Myceliophthora thermophila C1 (MtLPMO9A). This enzyme cleaves β-(1 → 4)-xylosyl bonds in xylan under formation of oxidized xylo-oligosaccharides, while it simultaneously cleaves β-(1 → 4)-glucosyl bonds in cellulose under formation of oxidized gluco-oligosaccharides. In particular, MtLPMO9A benefits from the strong interaction between low substituted linear xylan and cellulose. MtLPMO9A shows a strong synergistic effect with endoglucanase I (EGI) with a 16-fold higher release of detected oligosaccharides, compared to the oligosaccharides release of MtLPMO9A and EGI alone. Conclusion: Now, for the first time, we demonstrate the activity of a lytic polysaccharide monooxygenase (MtLPMO9A) that shows oxidative cleavage of xylan in addition to cellulose. The ability of MtLPMO9A to cleave these rigid regions provides a new paradigm in the understanding of the degradation of xylan-coated cellulose. In addition, MtLPMO9A acts in strong synergism with endoglucanase I. The mode of action of MtLPMO9A is considered to be important for loosening the rigid xylan-cellulose polysaccharide matrix in plant biomass, enabling increased accessibility to the matrix for hydrolytic enzymes. This discovery provides new insights into how to boost plant biomass degradation by enzyme cocktails for biorefinery applications. © 2015 Frommhagen et al.


Kuhnel S.,Wageningen University | Westphal Y.,Wageningen University | Hinz S.W.A.,Dyadic Netherlands | Schols H.A.,Wageningen University | Gruppen H.,Wageningen University
Bioresource Technology | Year: 2011

The mode of action of four Chrysosporium lucknowense C1 α- l-arabinohydrolases was determined to enable controlled and effective degradation of arabinan. The active site of endoarabinanase Abn1 has at least six subsites, of which the subsites -1 to +2 have to be occupied for hydrolysis. Abn1 was able to hydrolyze a branched arabinohexaose with a double substituted arabinose at subsite -2. The exo acting enzymes Abn2, Abn4 and Abf3 release arabinobiose (Abn2) and arabinose (Abn4 and Abf3) from the non-reducing end of reduced arabinose oligomers. Abn2 binds the two arabinose units only at the subsites -1 and -2. Abf3 prefers small oligomers over large oligomers. It is able to hydrolyze all linkages present in beet arabinan, including the linkages of double substituted residues. Abn4 is more active towards polymeric substrate and releases arabinose monomers from single substituted arabinose residues. Depending on the combination of the enzymes, the C1 arabinohydrolases can be used to effectively release branched arabinose oligomers and/or arabinose monomers. © 2010 Elsevier Ltd.


Kool M.M.,Wageningen University | Schols H.A.,Wageningen University | Wagenknecht M.,University of Munster | Hinz S.W.A.,Dyadic Netherlands | And 2 more authors.
Carbohydrate Polymers | Year: 2014

Screening of eight carbohydrate acetyl esterases for their activity towards xanthan resulted in the recognition of one active esterase. AXE3, a CAZy family CE1 acetyl xylan esterase originating from Myceliophthora thermophila C1, removed 31% of all acetyl groups present in xanthan after a 48 h incubation. AXE3 activity towards xanthan was only observed when xanthan molecules were in the disordered conformation. Optimal performance towards xanthan was observed at 53 °C in the complete absence of salt, a condition favouring the disordered conformation. AXE3-deacetylated xanthan was hydrolyzed using cellulases and analyzed for its repeating units using UPLC-HILIC-ELSD/ESI-MS. This showed that AXE3 specifically removes the acetyl groups positioned on the inner mannose and that acetyl groups positioned on the outer mannose are not removed at all. After a prolonged incubation at optimal conditions, 57% of all acetyl groups, representing 70% of all acetyl groups on the inner mannose units, were hydrolyzed. © 2014 Elsevier Ltd.


Kuhnel S.,Wageningen University | Pouvreau L.,NIZO Food Research | Appeldoorn M.M.,Wageningen University | Hinz S.W.A.,Dyadic Netherlands | And 2 more authors.
Enzyme and Microbial Technology | Year: 2012

Three ferulic acid esterases from the filamentous fungus Chrysosporium lucknowense C1 were purified and characterized. The enzymes were most active at neutral pH and temperatures up to 45°C. All enzymes released ferulic acid and p-coumaric acid from a soluble corn fibre fraction. Ferulic acid esterases FaeA1 and FaeA2 could also release complex dehydrodiferulic acids and dehydrotriferulic acids from corn fibre oligomers, but released only 20% of all ferulic acid present in sugar beet pectin oligomers. Ferulic acid esterase FaeB2 released almost no complex ferulic acid oligomers from corn fibre oligomers, but 60% of all ferulic acid from sugar beet pectin oligomers. The ferulic acid esterases were classified based on both, sequence similarity and their activities toward synthetic substrates. The type A ferulic acid esterases FaeA1 and FaeA2 are the first members of the phylogenetic subfamily 5 to be biochemically characterized. Type B ferulic acid esterase FaeB2 is a member of subfamily 6. © 2011 Elsevier Inc.


Van Den Brink J.,Fungal Biodiversity Center | Van Muiswinkel G.C.J.,Dyadic Netherlands | Theelen B.,Fungal Biodiversity Center | Hinz S.W.A.,Dyadic Netherlands | De Vries R.P.,Fungal Biodiversity Center
Applied and Environmental Microbiology | Year: 2013

Rapid and efficient enzymatic degradation of plant biomass into fermentable sugars is a major challenge for the sustainable production of biochemicals and biofuels. Enzymes that are more thermostable (up to 70°C) use shorter reaction times for the complete saccharification of plant polysaccharides compared to hydrolytic enzymes of mesophilic fungi such as Trichoderma and Aspergillus species. The genus Myceliophthora contains four thermophilic fungi producing industrially relevant thermostable enzymes. Within this genus, isolates belonging to M. heterothallica were recently separated from the well-described species M. thermophila. We evaluate here the potential of M. heterothallica isolates to produce efficient enzyme mixtures for biomass degradation. Compared to the other thermophilic Myceliophthora species, isolates belonging to M. heterothallica and M. thermophila grew faster on pretreated spruce, wheat straw, and giant reed. According to their protein profiles and in vitro assays after growth on wheat straw, (hemi-)cellulolytic activities differed strongly between M. thermophila and M. heterothallica isolates. Compared to M. thermophila, M. heterothallica isolates were better in releasing sugars from mildly pretreated wheat straw (with 5% HCl) with a high content of xylan. The high levels of residual xylobiose revealed that enzyme mixtures of Myceliophthora species lack sufficient β-xylosidase activity. Sexual crossing of two M. heterothallica showed that progenies had a large genetic and physiological diversity. In the future, this will allow further improvement of the plant biomass-degrading enzyme mixtures of M. heterothallica. © 2013, American Society for Microbiology.


Westphal Y.,Wageningen University | Kuhnel S.,Wageningen University | de Waard P.,Wageningen Center | Hinz S.W.A.,Dyadic Netherlands | And 3 more authors.
Carbohydrate Research | Year: 2010

Sugar beet arabinan consists of an α-(1,5)-linked backbone of l-arabinosyl residues, which can be either single or double substituted with α-(1,2)- and/or α-(1,3)-linked l-arabinosyl residues. Neutral branched arabino-oligosaccharides were isolated from sugar beet arabinan by enzymatic degradation with mixtures of pure and well-defined arabinohydrolases from Chrysosporium lucknowense followed by fractionation based on size and analysis by MALDI-TOF MS and HPAEC. Using NMR analysis, two main series of branched arabino-oligosaccharides have been identified, both having an α-(1,5)-linked backbone of l-arabinosyl residues. One series carries single substituted α-(1,3)-linked l-arabinosyl residues at the backbone, whereas the other series consists of a double substituted α-(1,2,3,5)-linked arabinan structure within the molecule. The structures of eight such branched arabino-oligosaccharides were established. © 2010 Elsevier Ltd. All rights reserved.


Frommhagen M.,Wageningen University | Sforza S.,University of Parma | Westphal A.H.,Wageningen University | Visser J.,Dyadic Netherlands | And 5 more authors.
Biotechnology for Biofuels | Year: 2015

Background: Many agricultural and industrial food by-products are rich in cellulose and xylan. Their enzymatic degradation into monosaccharides is seen as a basis for the production of biofuels and bio-based chemicals. Lytic polysaccharide monooxygenases (LPMOs) constitute a group of recently discovered enzymes, classified as the auxiliary activity subgroups AA9, AA10, AA11 and AA13 in the CAZy database. LPMOs cleave cellulose, chitin, starch and β-(1 → 4)-linked substituted and non-substituted glucosyl units of hemicellulose under formation of oxidized gluco-oligosaccharides. Results: Here, we demonstrate a new LPMO, obtained from Myceliophthora thermophila C1 (MtLPMO9A). This enzyme cleaves β-(1 → 4)-xylosyl bonds in xylan under formation of oxidized xylo-oligosaccharides, while it simultaneously cleaves β-(1 → 4)-glucosyl bonds in cellulose under formation of oxidized gluco-oligosaccharides. In particular, MtLPMO9A benefits from the strong interaction between low substituted linear xylan and cellulose. MtLPMO9A shows a strong synergistic effect with endoglucanase I (EGI) with a 16-fold higher release of detected oligosaccharides, compared to the oligosaccharides release of MtLPMO9A and EGI alone. Conclusion: Now, for the first time, we demonstrate the activity of a lytic polysaccharide monooxygenase (MtLPMO9A) that shows oxidative cleavage of xylan in addition to cellulose. The ability of MtLPMO9A to cleave these rigid regions provides a new paradigm in the understanding of the degradation of xylan-coated cellulose. In addition, MtLPMO9A acts in strong synergism with endoglucanase I. The mode of action of MtLPMO9A is considered to be important for loosening the rigid xylan-cellulose polysaccharide matrix in plant biomass, enabling increased accessibility to the matrix for hydrolytic enzymes. This discovery provides new insights into how to boost plant biomass degradation by enzyme cocktails for biorefinery applications. © 2015 Frommhagen et al.

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