Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Development of Thermophilic Tailor-Made Enzyme Mixtures for the Bioconversion of Agricultural and Forest Residues
Luleå tekniska universitet, Institutionen för samhällsbyggnad och naturresurser, Kemiteknik.
Luleå tekniska universitet, Institutionen för samhällsbyggnad och naturresurser, Kemiteknik.ORCID-id: 0000-0002-3687-6173
Luleå tekniska universitet, Institutionen för samhällsbyggnad och naturresurser, Kemiteknik. Department of Chemical Engineering, Biotechnology Laboratory, National Technical University of Athens.ORCID-id: 0000-0003-0078-5904
Luleå tekniska universitet, Institutionen för samhällsbyggnad och naturresurser, Kemiteknik.ORCID-id: 0000-0001-7500-2367
Visa övriga samt affilieringar
2016 (Engelska)Ingår i: Frontiers in Microbiology, ISSN 1664-302X, E-ISSN 1664-302X, Vol. 7, artikel-id 177Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Even though the main components of all lignocellulosic feedstocks include cellulose, hemicellulose, as well as the protective lignin matrix, there are some differences in structure, such as in hardwoods and softwoods, which may influence the degradability of the materials. Under this view, various types of biomass might require a minimal set of enzymes that has to be tailor-made. Partially defined complex mixtures that are currently commercially used are not adapted to efficiently degrade different materials, so novel enzyme mixtures have to be customized. Development of these cocktails requires better knowledge about the specific activities involved, in order to optimize hydrolysis. The role of filamentous fungus Myceliophthora thermophila and its complete enzymatic repertoire for the bioconversion of complex carbohydrates has been widely proven. In this study, four core cellulases (MtCBH7, MtCBH6, MtEG5, and MtEG7), in the presence of other four “accessory” enzymes (mannanase, lytic polyssacharide monooxygenase MtGH61, xylanase, MtFae1a) and β-glucosidase MtBGL3, were tested as a nine-component cocktail against one model substrate (phosphoric acid swollen cellulose) and four hydrothermally pretreated natural substrates (wheat straw as an agricultural waste, birch, and spruce biomass, as forest residues). Synergistic interactions among different enzymes were determined using a suitable design of experiments methodology. The results suggest that for the hydrolysis of the pure substrate (PASC), high proportions of MtEG7 are needed for efficient yields. MtCBH7 and MtEG7 are enzymes of major importance during the hydrolysis of pretreated wheat straw, while MtCBH7 plays a crucial role in case of spruce. Cellobiohydrolases MtCBH6 and MtCBH7 act in combination and are key enzymes for the hydrolysis of the hardwood (birch). Optimum combinations were predicted from suitable statistical models which were able to further increase hydrolysis yields, suggesting that tailor-made enzyme mixtures targeted toward a particular residual biomass can help maximize hydrolysis yields. The present work demonstrates the change from “one cocktail for all” to “tailor-made cocktails” that are needed for the efficient saccharification of targeted feed stocks prior to the production of biobased products through the biorefinery concept.

Ort, förlag, år, upplaga, sidor
2016. Vol. 7, artikel-id 177
Nationell ämneskategori
Bioprocessteknik
Forskningsämne
Biokemisk processteknik
Identifikatorer
URN: urn:nbn:se:ltu:diva-8498DOI: 10.3389/fmicb.2016.00177PubMedID: 26909078Scopus ID: 2-s2.0-84962140634Lokalt ID: 703259a7-c6ca-486d-a5c6-c121a057b9f8OAI: oai:DiVA.org:ltu-8498DiVA, id: diva2:981436
Anmärkning

Validerad; 2016; Nivå 2; 20160216 (leomat)

Tillgänglig från: 2016-09-29 Skapad: 2016-09-29 Senast uppdaterad: 2018-07-10Bibliografiskt granskad

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

Förlagets fulltextPubMedScopus

Personposter BETA

Karnaouri, Anthi CMatsakas, LeonidasTopakas, EvangelosRova, UlrikaChristakopoulos, Paul

Sök vidare i DiVA

Av författaren/redaktören
Karnaouri, Anthi CMatsakas, LeonidasTopakas, EvangelosRova, UlrikaChristakopoulos, Paul
Av organisationen
Kemiteknik
I samma tidskrift
Frontiers in Microbiology
Bioprocessteknik

Sök vidare utanför DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetricpoäng

doi
pubmed
urn-nbn
Totalt: 433 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf