umn june2011 eijsink web

7/30/2019 Umn June2011 Eijsink Web

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Team 4 Lignocellulose to biofuels

Topic: enzyme technology for

conversion of lignocellulosic biomass
http://upload.wikimedia.org/wikipedia/commons/4/43/Strohr%C3%A4der.jpg


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The biorefinery, 2nd generation

biofuels and enzymes Notes

Enzymatic deconstruction is the method of

choice.

Enzymes are a major cost.

Biofuel is only one of many possible products.
http://www.bioforsk.no/ikbViewer/page/forsidehttp://www.bioforsk.no/ikbViewer/page/forsidehttp://www.bioforsk.no/ikbViewer/page/forsidehttp://www.bioforsk.no/ikbViewer/page/forsidehttp://www.bioforsk.no/ikbViewer/page/forsidehttp://www.bioforsk.no/ikbViewer/page/forsidehttp://www.bioforsk.no/ikbViewer/page/forsidehttp://upload.wikimedia.org/wikipedia/commons/4/43/Strohr%C3%A4der.jpghttp://www.bioforsk.no/ikbViewer/page/forside


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www.umb.no

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mistry,Bio

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dFoodScien

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UMN-UMB, Team 4 specific project: CBP21,

a helper protein from the CBM33 family

Gustav Vaaje-Kolstad et al., Journal of Biological Chemistry 280: 11313 -11319 & 280:28492-28497 (2005) + Patent application


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UMN-UMB, Team 4 specific project

starting point

Goals:

Use of directed evolution (mutagenesis) to produce

accessory proteins that act on cellulose.

Generation of fundamental knowledge about how helperproteins such as CBP21 work.

People:

Claudia Schmidt-Dannert group with post-doc Jake Vick. Eijsink group with post-doc Gustav Vaaje-Kolstad and

(since 2010) Ph.D. student Zarah Forsberg.


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UMN-UMB, Team 4 specific project

Developments since 2007

GH61 proteins act synergistically with cellulose and show

structural similarity with CBM33 (CBP21)

CBM33 proteins are enzymesthat break down chitin chains

GH61 proteins are enzymesthat break down cellulose chains

Identification of natural CBM33 proteins that break downcellulose

Interesting ideas and findings at UMN concerning mechanism

CBM33 GH61


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www.umb.no

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A new paradigm for degradation ofcrystalline polysaccharides

Oxidohydrolase(CBM33 or GH61),

catalyzing chain

cleavage in a fully

crystalline context

+Endo

Exo-processive

Vaaje-Kolstad et al., 2010,

Science 330:219-222


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Very hot project. IP issues.

Lots of mutagenesis work on CBP21 has been done andmutant characterization is in progress.

Several new, active CBM33s available.

NMR structure of CBP21 (a CBM33) has been solved.

Shift of focus from enzyme development to enzymeunderstanding.

Several joint papers, including potential breakthrough

papers on mechanism, are on their way.

Funding is running out (?)

UMN-UMB, Team 4 Status June 2011


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Notes about the future

Funding ? (currently only one PhD student at UMB)

Many applications sent in Norway (but)

MSc student exchange: Sophanit Mengesha

PhD student exchange: Zarah Forsberg (?)

Nb. Current potential is huge and progress is good, but

very high complexity (protein production, analyticaltools, theoretical biochemistry, many partners).

umn june2011 eijsink web

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