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ARS Home » Pacific West Area » Albany, California » Western Regional Research Center » Bioproducts Research » Research » Publications at this Location » Publication #306086
Title: Lignocellulose hydrolysis by multienzyme complexes

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

Submitted to: American Chemical Society Abstracts
Publication Type: Abstract Only
Publication Acceptance Date: 6/5/2014
Publication Date: 8/10/2014
Citation: Templeton, P.D., Kibblewhite, R.E., Wagschal, K.C., Paavola, C., Lee, C.C. 2014. Lignocellulose hydrolysis by multienzyme complexes. American Chemical Society Abstracts. Biol (68).

Interpretive Summary: In order to convert biomass substrates into valuable renewable chemicals, we need efficient enzyme systems. We describe work in which we develop optimal enzyme blends that are attached to small (nano) protein rings. Attaching the enzymes to these small rings dramatically elevates the activity of the enzymes, thus allowing us to use less enzyme for the same amount of work. This increases the overall efficiency of the process.

Technical Abstract: Lignocellulosic biomass is the most abundant renewable resource on the planet. Converting this material into a usable fuel is a multi-step process, the rate-limiting step being enzymatic hydrolysis of organic polymers into monomeric sugars. While the substrate can be complex and require a multitude of enzymatic activities, many bacteria and fungal organisms have evolved efficient methods to combat this apparent bottleneck. One strategy is the tethering or harnessing of various enzymes onto a multifunctional “cellulosome”. We have developed an artificial ring scaffold which can tether up to eighteen lignocellulolytic enzymes to form designer cellulosomes. These artificial cellulosomes have been tested against pure cellulose substrates as well as more complex heterogenous biomass materials. We demonstrate that enzyme blends complexed onto the ring scaffold have greater enzymatic activity than free enzymes.