Structural and functional characterisation of CBP21, a non
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Transcript Structural and functional characterisation of CBP21, a non
Department of Chemistry, Biotechnology and Food Science
NORWEGIAN UNIVERSITY OF LIFE SCIENCES
Team 4 – Lignocellulose to biofuels
Topic: enzyme technology for
conversion of lignocellulosic biomass
www.umb.no
Department of Chemistry, Biotechnology and Food Science
NORWEGIAN UNIVERSITY OF LIFE SCIENCES
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.
www.umb.no
Department of Chemistry, Biotechnology and Food Science
NORWEGIAN UNIVERSITY OF LIFE SCIENCES
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)www.umb.no
+ Patent application
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NORWEGIAN UNIVERSITY OF LIFE SCIENCES
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 helper
proteins 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.
www.umb.no
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NORWEGIAN UNIVERSITY OF LIFE SCIENCES
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 enzymes that break down chitin chains
GH61 proteins are enzymes that break down cellulose chains
Identification of natural CBM33 proteins that break down
cellulose
Interesting ideas and findings at UMN concerning mechanism
GH61
CBM33
www.umb.no
Department of Chemistry, Biotechnology and Food Science
NORWEGIAN UNIVERSITY OF LIFE SCIENCES
A new paradigm for degradation of
crystalline polysaccharides
Endo
Exo-processive
+
”Oxidohydrolase”
(”CBM33” or ”GH61”),
catalyzing chain
cleavage in a fully
crystalline context
Vaaje-Kolstad et al., 2010,
Science 330:219-222
www.umb.no
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NORWEGIAN UNIVERSITY OF LIFE SCIENCES
UMN-UMB, Team 4 – Status June 2011
Very “hot” project. IP issues.
Lots of mutagenesis work on CBP21 has been done and
mutant 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 enzyme
”understanding”.
Several joint papers, including potential ”breakthrough”
papers on mechanism, are on their way.
Funding is running out (?)
www.umb.no
Department of Chemistry, Biotechnology and Food Science
NORWEGIAN UNIVERSITY OF LIFE SCIENCES
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, analytical
tools, theoretical biochemistry, many partners).
www.umb.no