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Xylanase
About: Xylanase is a research topic. Over the lifetime, 7099 publications have been published within this topic receiving 163793 citations.
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TL;DR: The symbiotic yeasts isolated from termite guts have demonstrated a competitive capability to produce xylanase and ferment xylanose, suggesting that the wood-feeding termite gut is a promising reservoir for novel xylanases-producing and xylose-fermenting yeasts that are potentially valued for biorefinery industry.
Abstract: The effective fermentation of xylose remains an intractable challenge in bioethanol industry. The relevant xylanase enzyme is also in a high demand from industry for several biotechnological applications that inevitably in recent times led to many efforts for screening some novel microorganisms for better xylanase production and fermentation performance. Recently, it seems that wood-feeding termites can truly be considered as highly efficient natural bioreactors. The highly specialized gut systems of such insects are not yet fully realized, particularly, in xylose fermentation and xylanase production to advance industrial bioethanol technology as well as industrial applications of xylanases. A total of 92 strains from 18 yeast species were successfully isolated and identified from the gut of wood-feeding termite, Reticulitermes chinensis. Of these yeasts and strains, seven were identified for new species: Candida gotoi, Candida pseudorhagii, Hamamotoa lignophila, Meyerozyma guilliermondii, Sugiyamaella sp.1, Sugiyamaella sp. 2, and Sugiyamaella sp.3. Based on the phylogenetic and phenotypic characterization, the type strain of C. pseudorhagii sp. nov., which was originally designated strain SSA-1542T, was the most frequently occurred yeast from termite gut samples, showed the highly xylanolytic activity as well as D-xylose fermentation. The highest xylanase activity was recorded as 1.73 and 0.98 U/mL with xylan or D-xylose substrate, respectively, from SSA-1542T. Among xylanase-producing yeasts, four novel species were identified as D-xylose-fermenting yeasts, where the yeast, C. pseudorhagii SSA-1542T, showed the highest ethanol yield (0.31 g/g), ethanol productivity (0.31 g/L·h), and its fermentation efficiency (60.7%) in 48 h. Clearly, the symbiotic yeasts isolated from termite guts have demonstrated a competitive capability to produce xylanase and ferment xylose, suggesting that the wood-feeding termite gut is a promising reservoir for novel xylanases-producing and xylose-fermenting yeasts that are potentially valued for biorefinery industry.
68 citations
TL;DR: In vitro studies carried out using Bifidobacterium spp and Lactobacillus spp suggested the prebiotic nature of the crude as well as purified xylo-oligosaccharides as revealed by growth characteristics such as high O.D. of the culture broth, decrease in its pH, increase in cell mass and the resultant fermentation products.
Abstract: Soluble polysaccharides (SP, 35 g) isolated from wheat bran (100 g) consisted mainly of arabinose and xylose with minor quantities of rhamnose, mannose, galactose and glucose. Wheat bran SP was subjected to purified endoxylanase (from 96 h ragi malt) treatment to obtain xylo-oligosaccharides (0.3 g/1 g wheat bran). The oligosaccharide mixture was purified on Biogel P-2 column into four major peaks designated as WO-1, WO-2, WO-3 and WO-4. Individual oligosaccharide purity was ascertained by HPLC and their composition was determined by GLC. The purified oligosaccharides were characterized by ESI-MS and 1H NMR analysis. WO-1 and WO-2 were identified as arabinose containing xylotetraose and xylotriose, respectively, whereas WO-3 and WO-4 were identified as unsubstituted xylotriose and xylobiose, respectively. In vitro studies carried out using Bifidobacterium spp and Lactobacillus spp suggested the prebiotic nature of the crude as well as purified xylo-oligosaccharides as revealed by growth characteristics such as high O.D. of the culture broth, decrease in its pH, increase in cell mass and the resultant fermentation products. β-xylanase, β-xylosidase, α-arabinofuranosidase, α/β-galactosidases and acetyl esterase activities were determined in 24 h old culture broth and xylanase activity (440–830 μU/ml) was found to be the most preponderant among all of them.
68 citations
TL;DR: The properties of the xylanase enzyme qualify the enzyme to be novel and potentially important for application in some industrial processes.
Abstract: A. GESSESSE AND B.A. GASHE. 1997. An alkaline xylanase-producing alkaliphilic Bacillus sp. AR-()09 was isolated from an alkaline soda lake in Ethiopia. The enzyme was optimally active at pH 9 and was stable over a broad pH range. The optimum temperature for xylanase activity, assayed at pH 9, was 60°-65°C. Measured at pH 8 and 9, the enzyme had good stability at 55° and 60°C. At both pH values, over 80% of its original activity was retained after heating for 2.5 h at 55°C. At 60°C, the enzyme maintained 63% of its original activity after 2.5 h incubation while at pH 9 it retained 54% of its original activity after 1 h heating. These properties qualify the enzyme to be novel and potentially important for application in some industrial processes.
68 citations
TL;DR: In vitro fermentations were carried out by using a model of the human colon to stimulate microbial activities of gut bacteria to induce induction of bacterial synthesis of extracellular hydrolytic enzymes xylanase and ferulic acid esterase which are both required for bacterial metabolism of WU-AX.
67 citations
TL;DR: The subunit composition of the extracellular complex from Clostridium thermocellum was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the presence of exoglucanase activity was indicated.
Abstract: The subunit composition of the extracellular complex from Clostridium thermocellum was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Twenty-six bands, representing proteins with apparent molecular sizes ranging from 37,500 to 185,000 Da, could be detected by silver staining. Cultivation of the bacteria with the substrate Avicel, Sigma cellulose, Solka floc, or cellobiose as the carbon source had no influence on the number of detectable protein bands. By activity staining with the substrate carboxymethyl cellulose or xylan added to the SDS-polyacrylamide gels, 15 of the 26 bands exhibited endoglucanase activity and 13 showed xylanase activity. In 8 of the 26 bands, both activities could be found. As minor activities, β-glucosidase, β-xylosidase, β-galactosidase, and β-mannosidase activities could be demonstrated in the cellulase complex. Upon measuring the release of para-nitrophenol (PNP) from PNP-cellobioside and determining the amount of glucose formed, the presence of exoglucanase activity was indicated. Upon glycoprotein staining of SDS-polyacrylamide gels, 14 of the 26 bands reacted positive, indicating the glycoprotein nature of the respective proteins. Four proteins (apparent molecular sizes, 58,000, 72,500, 94,000, and 110,000 Da) could be enriched from the originally bound cellulase complex by preparative SDS-PAGE. The two smaller proteins exhibited xylanase activity, whereas the 94,000-Da protein had endo- and exoglucanase activity, and the 110,000-Da protein degraded PNP-pyranosides. Images
67 citations