Deconstruction

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GLBRC's Deconstruction Research Area

Deconstruction

GLBRC's Deconstruction Lead takes top academic slot

Located at the intersection of the U.S.’s agricultural heartland and its northern forests, the GLBRC has access to a rich diversity of raw biomass for study. The Center's Deconstruction research focuses on identifying the best combinations of enzymes, chemicals, and physical processing methods for enhancing the digestibility of specific biomass sources.

Learn about the Center's research approach

Deconstruction Leadership

Deconstruction Lead

Dale is an expert on making ethanol from cellulose, plant stalks, grass, corn cobs and other woody plant parts and has developed a patented process called ammonia fiber expansion (AFEXTM), which makes the breakdown of cellulose more efficient, thus tackling...

Deconstruction Lead

Fox's research goals are to define the structure and the reactivity of the active site diiron center, to probe the catalytic contributions of the active site protein residues and to determine the consequences of protein-protein and protein-substrate interactions on the...

Project Overview

A biofuels reactor designed to produce ethanol at Michigan State University's Biomass Conversion Research Lab (BCRL)GLBRC Deconstruction research maintains a focus on the entire biofuels production pipeline: in addition to identifying and improving natural cellulose-degrading enzymes extracted from diverse environments, researchers apply unique biomass pretreatment technologies—such as ammonia fiber expansion (AFEX™), alkaline hydrogen peroxide (AHP), and extractive ammonia (EA)—that enable conversion technologies to maximize plant biomass utilization.. Researchers also explore strategies to add value to these processes by developing co-products from materials that would otherwise be treated as waste, such as lignin. Specific deconstruction projects include:

  • Pretreatment effects on biomass, alkaline peroxide pretreatment, fuel production from alkaline-pretreated biomass
  • Optimization of enzymes for biomass conversion, discovery of natural cellulolytic microbes, identification of novel microbial enzymes, and combinatorial discovery of enzymes and proteins

Deconstruction Publications

Scaling up and benchmarking of ethanol production from pelletized pilot scale AFEX treated corn stover using Zymomonas mobilis 8b

Cory Sarks; Bryan D. Bals; Jim Wynn; Farzaneh Teymouri; Stefan Schwegmann; Karyn Sanders; Mingjie Jin; Venkatesh Balan; Bruce E. Dale

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2016

This report outlines the recent scale-up of AFEX pretreatment from the laboratory to pilot scale. Sugar yields were improved by 19 and 15% for glucose and xylose, respectively. Further improvement was achieved when scaling up the hydrolysis and fermentation of AFEX-treated corn stover to 2500 L working volume. Benchmarking was performed using CTec 3 and HTec 3 enzymes along with Zymomonas mobilis 8b. Subsequently, the seed train was modified to use a hydrolysate-based medium as a replacement for pure sugars and nutrients. Fermentation performance was comparable following this change. Economic analysis showed a 19% reduction in MESP for the new process over the previous benchmark process.

Single-amino acid modifications reveal additional controls on the proton pathway of [FeFe]-hydrogenase

Adam J. Cornish; Bojana Ginovska; Adam Thelen; Julio C.S. da Silva; Thereza A. Soares; Simone Raugei; Michel Dupuis; Wendy J. Shaw; Eric L. Hegg

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2016

Structure and mechanism of NOV1, a resveratrol-cleaving dioxygenase

Ryan P. McAndrew; Noppadon Sathitsuksanoh; Michael M. Mbughuni; Richard A. Heins; Jose H. Pereira; Anthe George; Kenneth L. Sale; Brian G. Fox; Blake A. Simmons; Paul D. Adams

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2016

Stilbenes are diphenyl ethene compounds produced naturally in a wide variety of plant species and some bacteria. Stilbenes are also derived from lignin during kraft pulping. Stilbene cleavage oxygenases (SCOs) cleave the central double bond of stilbenes, forming two phenolic aldehydes. Here, we report the structure of an SCO. The X-ray structure of NOV1 from Novosphingobium aromaticivorans was determined in complex with its substrate resveratrol (1.89 Å), its product vanillin (1.75 Å), and without any bound ligand (1.61 Å). The enzyme is a seven-bladed β-propeller with an iron cofactor coordinated by four histidines. In all three structures, dioxygen is observed bound to the iron in a side-on fashion. These structures, along with EPR analysis, allow us to propose a mechanism in which a ferric-superoxide reacts with substrate activated by deprotonation of a phenol group at position 4 of the substrate, which allows movement of electron density toward the central double bond and thus facilitates reaction with the ferric superoxide electrophile. Correspondingly, NOV1 cleaves a wide range of other stilbene-like compounds with a 4′-OH group, offering potential in processing some solubilized fragments of lignin into monomer aromatic compounds.

Techniques for the evolution of robust pentose-fermenting yeast for bioconversion of lignocellulose to ethanol

Patricia J. Slininger; Maureen A. Shea-Andersh; Stephanie R. Thompson; Bruce S. Dien; Cletus P. Kurtzman; Leonardo da Costa Sousa; Venkatesh Balan

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2016

The Complete Genome Sequence of Hyperthermophile Dictyoglomus turgidum DSM 6724™ Reveals a Specialized Carbohydrate Fermentor

Phillip J. Brumm; Krishne Gowda; Frank T. Robb; David A. Mead

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2016

Here we report the complete genome sequence of the chemoorganotrophic, extremely thermophilic bacterium, Dictyoglomus turgidum, which is a Gram negative, strictly anaerobic bacterium. D. turgidum and D. thermophilum together form the Dictyoglomi phylum. The two Dictyoglomus genomes are highly syntenic, and both are distantly related to Caldicellulosiruptor spp. D. turgidum is able to grow on a wide variety of polysaccharide substrates due to significant genomic commitment to glycosyl hydrolases, sixteen of which were cloned and expressed in our study. The GH5, GH10 and GH42 enzymes characterized in this study suggest that D. turgidum can utilize most plant-based polysaccharides except crystalline cellulose. The DNA polymerase I enzyme was also expressed and characterized. The pure enzyme showed improved amplification of long PCR targets compared to Taq polymerase. The genome contains a full complement of DNA modifying enzymes, and an unusually high copy number (4) of a new, ancestral family of polB type nucleotidyltransferases designated as MNT (minimal nucleotidyltransferases). Considering its optimal growth at 72ºC, D. turgidum has an anomalously low G+C content of 39.9% that may account for the presence of reverse gyrase, usually associated with hyperthermophiles.

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