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Characterization of acid catalytic domains for cellulose hydrolysis and glucose degradation.

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TLDR
Results show that acid catalyzed hydrolysis is proportional to H+ concentration, and overall yields of glucose obtained from cellobiose and cellulose are higher for the best carboxylic acid tested, maleic acid, when compared to sulfuric acid at equivalent solution pH.
Abstract
Cellulolytic enzymes consist of a catalytic domain, a linking peptide, and a binding domain. The paper describes research on carboxylic acids that have potential as catalytic domains for constructing organic macromolecules for use in cellulose hydrolysis that mimic the action of enzymes. The tested domains consist of the series of mono-, di-, and tricarboxylic acids with a range of pK(a)'s. This paper systematically characterizes the acids with respect to hydrolysis of cellobiose, cellulose in biomass, and degradation of glucose and compares these kinetics data to dilute sulfuric acid. Results show that acid catalyzed hydrolysis is proportional to H+ concentration. The tested carboxylic acids did not catalyze the degradation of glucose while sulfuric acid catalyzed the degradation of glucose above that of water alone. Consequently, overall yields of glucose obtained from cellobiose and cellulose are higher for the best carboxylic acid tested, maleic acid, when compared to sulfuric acid at equivalent solution pH.

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Citations
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Features of promising technologies for pretreatment of lignocellulosic biomass.

TL;DR: This paper reviews process parameters and their fundamental modes of action for promising pretreatment methods and concludes that pretreatment processing conditions must be tailored to the specific chemical and structural composition of the various, and variable, sources of lignocellulosic biomass.
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Progress in bioethanol processing

TL;DR: A review of the biological and thermochemical methods that could be used to produce bioethanol is made and an analysis of its global production trends is carried out in this paper, where the authors evaluate the utilization of different feedstocks (i.e., sucrose containing, starchy materials, lignocellulosic biomass) is required considering the big share of raw materials in bio-ethanol costs.
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Synergies between Bio‐ and Oil Refineries for the Production of Fuels from Biomass

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Recent updates on different methods of pretreatment of lignocellulosic feedstocks: a review

TL;DR: An extensive research is still required for the development of new and more efficient pretreatment processes for lignocellulosic feedstocks yielding promising results.
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Hemicellulose biorefineries: a review on biomass pretreatments

TL;DR: In this paper, the authors provide a review of the use of pre-treatment for hemicellulose in a lignocellulose feedstock-based biorefinery.
References
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Journal ArticleDOI

The generation of fermentation inhibitors during dilute acid hydrolysis of softwood

TL;DR: In this paper, the influence of dilute sulfuric acid hydrolysis of spruce (softwood) on sugar yield and on the fermentability of the hydrolysate by Saccharomyces cerevisiae (Baker's yeast) was investigated.
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Mechanisms of enzymatic glycoside hydrolysis

TL;DR: The determination of a large number of three-dimensional structures of Glycosidases, both free and in complex with ligands, has provided valuable new insights into glycosidase catalysis, especially when coupled with results from studies of specifically labelled glyCosidases and kinetic analyses of point mutants.
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The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei.

TL;DR: The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined and may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose.
Journal ArticleDOI

Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma reesei

TL;DR: The three-dimensional structure of a cellulase, the enzymatic core of CBHII from the fungus Trichoderma reesei reveals an alpha-beta protein with a fold similar to but different from the widely occurring barrel topology first observed in triose phosphate isomerase.
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