Biocatalytic approach for the utilization of hemicellulose for ethanol production from agricultural residue using thermostable xylanase and thermotolerant yeast

Menon, Vishnu; Prakash, Gyan; Prabhune, Asmita; Rao, M. R. Raghavendra

doi:10.1016/j.biortech.2010.01.150

Cited by 58 publications

(34 citation statements)

References 29 publications

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“…On the basis of the similarity of amino acid sequences, most endo-␤-1,4-xylanases are confined to glycosyl hydrolase family 10 (GH10) and GH11 (http://www.cazy.org/) (3). GH10 xylanases have a catalytic domain of a classic (␣/␤) 8 barrel fold, in which the catalytic cleft is located on the surface of the C-terminal side of the central barrel (4,5). Two conserved glutamic acid residues are located in the open cleft of the catalytic module in order to recognize and interact with the substrate through hydrogen bonds or hydrophobic stacking interactions and act as the nucleophile and acid/base catalyst (3,6,7).…”

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confidence: 99%

“…Two conserved glutamic acid residues are located in the open cleft of the catalytic module in order to recognize and interact with the substrate through hydrogen bonds or hydrophobic stacking interactions and act as the nucleophile and acid/base catalyst (3,6,7). Xylanases have been attracting extensive attention because of their potential application in various industrial processes, such as textile, pulp and paper, food, animal feed, and biofuel production and biobleaching (8,9). In recent years, technical, environmental, and economic progress has triggered the exploration of greater microbial resources to obtain more efficient biocatalysts for industrial demands.…”

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confidence: 99%

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A C-Terminal Proline-Rich Sequence Simultaneously Broadens the Optimal Temperature and pH Ranges and Improves the Catalytic Efficiency of Glycosyl Hydrolase Family 10 Ruminal Xylanases

Xue

Zhao

et al. 2014

Appl Environ Microbiol

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c Efficient degradation of plant polysaccharides in rumen requires xylanolytic enzymes with a high catalytic capacity. In this study, a full-length xylanase gene (xynA) was retrieved from the sheep rumen. The deduced XynA sequence contains a putative signal peptide, a catalytic motif of glycoside hydrolase family 10 (GH10), and an extra C-terminal proline-rich sequence without a homolog. To determine its function, both mature XynA and its C terminus-truncated mutant, XynA-Tr, were expressed in Escherichia coli. The C-terminal oligopeptide had significant effects on the function and structure of XynA. Compared with XynA-Tr, XynA exhibited improved specific activity (12-fold) and catalytic efficiency (14-fold), a higher temperature optimum (50°C versus 45°C), and broader ranges of temperature and pH optima (pH 5.0 to 7.5 and 40 to 60°C versus pH 5.5 to 6.5 and 40 to 50°C). Moreover, XynA released more xylose than XynA-Tr when using beech wood xylan and wheat arabinoxylan as the substrate. The underlying mechanisms responsible for these changes were analyzed by substrate binding assay, circular dichroism (CD) spectroscopy, isothermal titration calorimetry (ITC), and xylooligosaccharide hydrolysis. XynA had no ability to bind to any of the tested soluble and insoluble polysaccharides. However, it contained more ␣ helices and had a greater affinity and catalytic efficiency toward xylooligosaccharides, which benefited complete substrate degradation. Similar results were obtained when the C-terminal sequence was fused to another GH10 xylanase from sheep rumen. This study reveals an engineering strategy to improve the catalytic performance of enzymes.

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confidence: 99%

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confidence: 99%

A C-Terminal Proline-Rich Sequence Simultaneously Broadens the Optimal Temperature and pH Ranges and Improves the Catalytic Efficiency of Glycosyl Hydrolase Family 10 Ruminal Xylanases

Xue

Zhao

et al. 2014

Appl Environ Microbiol

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“…This thermotolerant Debaryomyces sp. used both pentoses and hexoses to similar extents in sugar mixtures, and a preference for one carbohydrate does not inhibit the consumption of other (Menon et al 2010a). Neurospora crassa is known to produce ethanol directly from the cellulose/hemicellulose, since it produces both the cellulase and xylanase and also has the capacity to ferment the sugars to ethanol anaerobically (Dogaris et al 2013).…”

Section: Fermentationmentioning

confidence: 99%

Bioconversion of Cotton Gin Waste to Bioethanol

Sahu

Pramanik

2015

Soil Biology

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“…However, most surfactants are chemosynthetic, such that they have poor biodegradability and a negative effect on the environment . Natural surfactants, such as glycolipids, lipopeptides, saponin, phospholipids and microbial cells, are eco-friendly and have excellent surface activity, which make them a desirable replacement for traditional chemical surfactants Menon et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Enhancement of Bioethanol Production Using a Blend of Furfural Production Residue and Tea-seed Cake

Zheng¹,

Xing²,

Zhou³

et al. 2016

BioResources

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The price of raw material, energy demand in the pretreatment step, and enzyme usage rate are the major cost factors in the process of converting biomass to bioethanol. Unwashed furfural residues (FRs) possess great potential for application in bioethanol production. Surfactant addition is an effective method to enhance the fermentation rate. In this study, unwashed FRs were used directly as raw materials to produce bioethanol. Tea-seed cake (TSC), tea seed residues that contained protein and saponin, was added in the simultaneous saccharification and fermentation (SSF) process. The effect of TSC dosage on SSF was compared. TSC was added at the dosage of 10 g/L, which resulted in a final ethanol yield of 87.2%. However, a high concentration of TSC could induce cytotoxicity in yeast. The surface tension (approximately 33.92 mM/m) at SSF using TSC-medium was much lower than that of other fermentation systems (about 64.67 mN/m). Further contact angle testing showed that TSC-medium (21.7°) had better wetting capacity than FRs (45.6°). This study provided a proposed process strategy that SSF with the addition of TSC could be a minimum consumption of chemicals and enzymes for future cellulosic ethanol production process.

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Biocatalytic approach for the utilization of hemicellulose for ethanol production from agricultural residue using thermostable xylanase and thermotolerant yeast

Cited by 58 publications

References 29 publications

A C-Terminal Proline-Rich Sequence Simultaneously Broadens the Optimal Temperature and pH Ranges and Improves the Catalytic Efficiency of Glycosyl Hydrolase Family 10 Ruminal Xylanases

A C-Terminal Proline-Rich Sequence Simultaneously Broadens the Optimal Temperature and pH Ranges and Improves the Catalytic Efficiency of Glycosyl Hydrolase Family 10 Ruminal Xylanases

Bioconversion of Cotton Gin Waste to Bioethanol

Enhancement of Bioethanol Production Using a Blend of Furfural Production Residue and Tea-seed Cake

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