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ARS Home » Pacific West Area » Albany, California » Western Regional Research Center » Bioproducts Research » Research » Publications at this Location » Publication #335408

Title: Conversion of biomass to value-added bioproducts by enzyme nanoassemblies

Author
item Lee, Charles
item Kibblewhite, Rena
item PAAVOLA, CHAD - National Aeronautics And Space Administration (NASA)
item Wagschal, Kurt

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 2/2/2017
Publication Date: 4/4/2017
Citation: Lee, C.C., Kibblewhite, R.E., Paavola, C.D., Wagschal, K.C. 2017. Conversion of biomass to value-added bioproducts by enzyme nanoassemblies. Meeting Abstract. American Chemical Society. p.100.

Interpretive Summary:

Technical Abstract: Lignocellulosic biomass represents a tremendous resource to supply the world’s fuel and chemical feedstock needs. An effective strategy to unlock the potential of this biomass involves hydrolysis of this material into simpler components that can then be further transformed. One of the most efficient enzymatic methods for hydrolyzing biomass substrates is the use of multienzyme complexes called cellulosomes produced by various anaerobic bacteria. These complexes are comprised of a protein scaffold containing multiple recognition sites called cohesins. Biomass-degrading enzymes with complementary recognition motifs called dockerins bind to the cohesins to form large complexes that are very effective at hydrolyzing cellulosic biomass. In order to design custom cellulosomes that will target specific biomass substrates and extend the functionality of the complexes, we have created an artificial scaffold protein that will self-assemble into an eighteen-subunit structure. We demonstrate that these artificial complexes, called rosettazymes, hydrolyze biomass substrates more efficiently than enzymes free in solution. We also incorporated enzymes to convert the substrate into value-added bioproducts, such as diacids. Furthermore, we show the effect that varying the relative enzyme ratios in the complex has upon product formation.