Purification and characterization of two thermostable cellulase-free xylanases from workers of the termite Macrotermes subhyalinus (Isoptera: Termitidae)

Faulet, Betty Meuwiah; Niamké, Sebastien; Gonnety, Jean Tia; Kouamé, Lucien Patrice

doi:10.1079/ijt2006106

Cited by 6 publications

(6 citation statements)

References 41 publications

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“…4b). These results agreed with the previous studies [21][22][23] . The xylanase from A. niger DSM 1957 is resistant to methanol, ethanol, isopropanol, and acetone.…”

Section: Effect Of Organic Solvents On Xylanase Activitysupporting

confidence: 94%

“…The addition of 1% (v/v) of Tween 80 and Triton X-100 to the xylanases from Termitomyces sp. 22 and from the termite Macrotermes subhyalinus worker 23 did not change significantly in the xylanase activity, only a slight decrease by 3-4% and 11% in comparison to the control reaction without the additives, respectively. However, SDS strongly inhibited the xylanase from M. subhyalinus and Termitomyces sp.…”

Section: Effect Of Detergents On Xylanase Activitymentioning

confidence: 79%

“…Activation of the xylanase from M. subhyalinus and from Termitomyces sp. was observed with the addition of acetone and dioxane at the concentration 23 of up to 15% and with the addition of acetone at the concentration 22 of up to 30%, respectively. However, in contrast to our study, alcohols (methanol, ethanol, propanol, and butanol) completely inhibited the enzyme from Termitomyces sp.…”

Section: Effect Of Organic Solvents On Xylanase Activitymentioning

confidence: 90%

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Purification and characterization of an acid-stable and organic solvent-tolerant xylanase from Aspergillus awamori VTCC-F312

Tuyen¹,

Quyen²,

Dam³

2012

ScienceAsia

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An acid-stable and organic solvent-tolerant extracellular xylanase was isolated and purified from Aspergillus awamori VTCC-F312 and its properties were investigated. The xylanase was purified by Sephadex G-100 gel filtration chromatography and DEAE-Sephadex A-50 ion exchange chromatography to homogeneity. The enzyme had a molecular mass of 32 kDa and a specific activity of 217 U/mg protein, with optimum temperature of 50-55°C and optimum pH of 5. This enzyme was stable at up to 45°C and no loss of enzyme activity was observed after incubation for 6 h at 40°C. The xylanase was stable within the pH range of 4-8 with no loss of enzyme activity after incubation at 30°C for 1-4 h, even the enzyme activity was found to increase by 60% after incubation at pH 4 for 4 h. The Km and Vmax values were 12.6 mg oat spelt xylan per ml and 1000 U/mg protein, respectively. Dithiothreitol, β-mercaptoethanol, and EDTA were found to increase the xylanase activity by 19%, 46%, and 138%, respectively. Except for Fe 3+ , the presence of 5 mM tested metal ions increased the enzyme activity by 18-52%. The enzyme showed high resistance to organic solvents and retained 63-86% and 44-61% of its activity in the presence of tested organic solvents at 30% and 80% (v/v), respectively. Triton X-100 and Tween 80 activated the xylanase to 128% and 116% of its activity, whereas SDS at the concentration of 5% completely inhibited the enzyme. These results suggested that the xylanase from A. awamori VTCC-F312 could potentially be used as a feed additive for monogastric animals.KEYWORDS: detergent-resistant, no disulphide bond, non-metal enzyme, free of cellulase and mannanase activity, corn cob, natural substrate

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“…4b). These results agreed with the previous studies [21][22][23] . The xylanase from A. niger DSM 1957 is resistant to methanol, ethanol, isopropanol, and acetone.…”

Section: Effect Of Organic Solvents On Xylanase Activitysupporting

confidence: 94%

Section: Effect Of Detergents On Xylanase Activitymentioning

confidence: 79%

Section: Effect Of Organic Solvents On Xylanase Activitymentioning

confidence: 90%

See 1 more Smart Citation

Purification and characterization of an acid-stable and organic solvent-tolerant xylanase from Aspergillus awamori VTCC-F312

Tuyen¹,

Quyen²,

Dam³

2012

ScienceAsia

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show abstract

“…The stability studies with hydrophilic solvents suggested it to be showing good solvent tolerance in 25% ethanol (91%), methanol (82%), and acetone (78%) ( Table 3 ). In contrast, complete inhibition of Macrotermes subhyalinus xylanase was observed at 30% and 60% v/v of alcohols (methanol, ethanol, propanol, and butanol) [ 39 ]. Impurities like metal ions and solvents, which can potentially inhibit the activity of xylanase, exist in raw pulp.…”

Section: Resultsmentioning

confidence: 99%

Characterization of a New Providencia sp. Strain X1 Producing Multiple Xylanases on Wheat Bran

Raj

Kumar

Singh

et al. 2013

The Scientific World Journal

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Providencia sp. strain X1 showing the highest xylanase activity among six bacterial isolates was isolated from saw-dust decomposing site. Strain X1 produced cellulase-free extracellular xylanase, which was higher in wheat bran medium than in xylan medium, when cultivated at pH 8.0 and 35°C. Zymogram analysis of crude preparation of enzymes obtained while growing on wheat bran and birchwood xylan revealed the presence of seven and two distinct xylanases with estimated molecular weight of 33; 35; 40; 48; 60; 75; and 95 kDa and 33 and 44 kDa, respectively. The crude xylanases were produced on wheat bran medium and showed optimum activity at pH 9.0 and 60°C. The thermotolerance studies showed activity retention of 100% and 85% at 40°C and 60°C after 30 min preincubation at pH 9.0. It was tolerant to lignin, ferulic acid, syringic acid, and guaiacol and retained 90% activity after ethanol treatment. The enzyme preparation was also tolerant to methanol and acetone and showed good activity retention in the presence of metal ions such as Fe2+, Mg2+, Zn2+, and Ca2+. The crude enzyme preparation was classified as endoxylanase based on the product pattern of xylan hydrolysis. Pretreatment of kraft pulp with crude xylanases for 3 h at 60°C led to a decrease in kappa number by 28.5%. The properties of present xylanases make them potentially useful for industrial applications.

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“…The addition of 1 % (v/v) Tween 80 to the xylanases from Termitomyces sp. [49] and from Macrotermes subhyalinus [50] did not significantly change the xylanase activity, but SDS strongly inhibited the activity of xylanase. Fialho and Carmona [51] reported that the xylanase from Aspergillus giganteus was completely inhibited by SDS.…”

Section: Discussionmentioning

confidence: 99%

Cloning, Expression, and Purification of Xylanase Gene from Bacillus licheniformis for Use in Saccharification of Plant Biomass

Zafar

Aftab

Din

et al. 2015

Appl Biochem Biotechnol

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The xylanase gene (xynA) of Bacillus licheniformis 9945A was cloned and expressed in Escherichia coli BL21(DE3) using pET-22b(+) as an expression vector. The recombinant xylanase enzyme was purified by ammonium sulfate precipitation, followed by single-step immobilized metal ion affinity chromatography with a 57.58-fold purification having 138.2 U/mg specific activity and recovery of 70.08 %. Molecular weight of the purified xylanase, 23 kDa, was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was stable for up to 70 °C with a broad pH range of 4-9 pH units. The enzyme activity was increased in the presence of metal ions especially Ca(+2) and decreased in the presence of EDTA, indicating that the xylanase was a metalloenzyme. However, an addition of 1-4 % Tween 80, β-mercaptoethanol, and DTT resulted in the increase of enzyme activity by 51, 52, and 5 %, respectively. Organic solvents with a concentration of 10-40 % slightly decreased the enzyme activity. The xylanase enzyme possesses the ability of bioconversion of plant biomasses like wheat straw, rice straw, and sugarcane bagasse. Among the different tested biomasses, the highest saccharification percentage was observed with 1 % sugarcane bagasse after 72 h of incubation at 50 °C with 20 units of enzyme. The results suggest that recombinant xylanase can be used in the bioconversion of natural biomasses into simple sugars which could be further used for the production of biofuel.

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Purification and characterization of two thermostable cellulase-free xylanases from workers of the termite Macrotermes subhyalinus (Isoptera: Termitidae)

Cited by 6 publications

References 41 publications

Purification and characterization of an acid-stable and organic solvent-tolerant xylanase from Aspergillus awamori VTCC-F312

Purification and characterization of an acid-stable and organic solvent-tolerant xylanase from Aspergillus awamori VTCC-F312

Characterization of a New Providencia sp. Strain X1 Producing Multiple Xylanases on Wheat Bran

Cloning, Expression, and Purification of Xylanase Gene from Bacillus licheniformis for Use in Saccharification of Plant Biomass

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