Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost

Taibi, Z.; Saoudi, Boudjema; Boudelaa, Mokhtar; Trigui, Hé la; Belghith, Hafedh; Gargouri, Ali; Ladjama, Ali

doi:10.1007/s12010-011-9457-y

Cited by 63 publications

(44 citation statements)

References 44 publications

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“…Likewise, the activity of Actinomadura sp. strain Cpt20 xylanase was also found to be enhanced by Ca 2+ and Co 2+ , but was inhibited by Fe 2+ , Zn 2+ , Cu 2+ and Mg 2+ , yet almost unaffected by K + , Na + and Mn 2+ [24]. In contrast to the results obtained, ethanol, isopropanol and butanol had no effect on the Streptomyces rameus L2001 xylanase activity [26].…”

Section: Resultscontrasting

confidence: 66%

Insight into Glycoside Hydrolases for Debranched Xylan Degradation from Extremely Thermophilic Bacterium Caldicellulosiruptor lactoaceticus

Jia

Wang

et al. 2014

PLoS ONE

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Caldicellulosiruptor lactoaceticus 6A, an anaerobic and extremely thermophilic bacterium, uses natural xylan as carbon source. The encoded genes of C. lactoaceticus 6A for glycoside hydrolase (GH) provide a platform for xylan degradation. The GH family 10 xylanase (Xyn10A) and GH67 α-glucuronidase (Agu67A) from C. lactoaceticus 6A were heterologously expressed, purified and characterized. Both Xyn10A and Agu67A are predicted as intracellular enzymes as no signal peptides identified. Xyn10A and Agu67A had molecular weight of 47.0 kDa and 80.0 kDa respectively as determined by SDS-PAGE, while both appeared as homodimer when analyzed by gel filtration. Xyn10A displayed the highest activity at 80°C and pH 6.5, as 75°C and pH 6.5 for Agu67A. Xyn10A had good stability at 75°C, 80°C, and pH 4.5–8.5, respectively, and was sensitive to various metal ions and reagents. Xyn10A possessed hydrolytic activity towards xylo-oligosaccharides (XOs) and beechwood xylan. At optimum conditions, the specific activity of Xyn10A was 44.6 IU/mg with beechwood xylan as substrate, and liberated branched XOs, xylobiose, and xylose. Agu67A was active on branched XOs with methyl-glucuronic acids (MeGlcA) sub-chains, and primarily generated XOs equivalents and MeGlcA. The specific activity of Agu67A was 1.3 IU/mg with aldobiouronic acid as substrate. The synergistic action of Xyn10A and Agu67A was observed with MeGlcA branched XOs and xylan as substrates, both backbone and branched chain of substrates were degraded, and liberated xylose, xylobiose, and MeGlcA. The synergism of Xyn10A and Agu67A provided not only a thermophilic method for natural xylan degradation, but also insight into the mechanisms for xylan utilization of C. lactoaceticus.

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Section: Resultscontrasting

confidence: 66%

Insight into Glycoside Hydrolases for Debranched Xylan Degradation from Extremely Thermophilic Bacterium Caldicellulosiruptor lactoaceticus

Jia

Wang

et al. 2014

PLoS ONE

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“…°CBacteria Thermobifida halotolerans YIM 90462 T 34970––9.1––Zhang et al (2012) Actinomadura sp. strain Cpt202010805–1060–90–1.55–Taibi et al (2012) Bacillus pumilus SSP 34206504.5–950–6.51233Subramaniyan (2012) Cellulomonas flavigena 36, 536.565, 556–9855, 4.51.95, 0.78–Santiago-Hernández et al (2007) Streptomyces cyaneus SN3220.5660–65––8.511.145.45Ninawe et al (2008) Nesterenkonia xinjiangensis CCTCC AA001025197555–1160816.08, 9.2245.66, 16.05Kui et al (2010) Cellulosimicrobium cellulans CKMX1588606–1045–554.662.642000Walia et al (2013a, 2014)…”

Section: Xylanolytic Enzymesmentioning

confidence: 99%

“…However, a few organisms show constitutive production of the enzyme and also catabolic repression by carbon sources such as glucose or xylose (Walia et al 2013a, c). Xylan has been shown to be the best inducer of xylanase production in many cases (Taibi et al 2012; Guleria et al 2013; Walia et al 2014). Xylan, being a high molecular mass polymer, cannot enter the cell.…”

Section: Factors Affecting the Xylanase Productionmentioning

confidence: 99%

Microbial xylanases and their industrial application in pulp and paper biobleaching: a review

et al. 2017

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Xylanases are hydrolytic enzymes which cleave the β-1, 4 backbone of the complex plant cell wall polysaccharide xylan. Xylan is the major hemicellulosic constituent found in soft and hard food. It is the next most abundant renewable polysaccharide after cellulose. Xylanases and associated debranching enzymes produced by a variety of microorganisms including bacteria, actinomycetes, yeast and fungi bring hydrolysis of hemicelluloses. Despite thorough knowledge of microbial xylanolytic systems, further studies are required to achieve a complete understanding of the mechanism of xylan degradation by xylanases produced by microorganisms and their promising use in pulp biobleaching. Cellulase-free xylanases are important in pulp biobleaching as alternatives to the use of toxic chlorinated compounds because of the environmental hazards and diseases caused by the release of the adsorbable organic halogens. In this review, we have focused on the studies of structural composition of xylan in plants, their classification, sources of xylanases, extremophilic xylanases, modes of fermentation for the production of xylanases, factors affecting xylanase production, statistical approaches such as Plackett Burman, Response Surface Methodology to enhance xylanase production, purification, characterization, molecular cloning and expression. Besides this, review has focused on the microbial enzyme complex involved in the complete breakdown of xylan and the studies on xylanase regulation and their potential industrial applications with special reference to pulp biobleaching, which is directly related to increasing pulp brightness and reduction in environmental pollution.

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“…Such specifications relate to costeffectiveness, eco-friendliness, and ease of use (Taibi et al 2011). In this paper we reported kinetics of partially purified xylanases from T. harzianum and C. thermophilum ATCC 28076 under optimized culture conditions.…”

Section: Introductionmentioning

confidence: 99%

Comparative study for the kinetics of extracellular xylanases from Trichoderma harzianum and Chaetomium thermophilum

Ahmed¹,

Imdad²,

Jamil³

2012

Electron. J. Biotechnol.

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Xylanases assume special importance in the paper and pulp industry as they replace toxic chemicals such as chlorine and chlorine dioxide for developing eco-friendly processes. This study evaluated xylanases produced by two fungi, the mesophilic fungus Trichoderma harzianum and a thermophilic fungus Chaetomium thermophilum. Among the polymeric substrates studied for xylanase production by both the fungi, birch wood xylan was found to be the best inducer of xylanases. Xylanases induction was subject to glucose repression. Partially purified xylanases preparation from T. harzianum and C. thermophilum exhibited optimal activities at pH 5 and 6 and at 60ºC and 70ºC, respectively. The apparent Km and Vmax values for the partially purified xylanase from T. harzianum using oat spelt xylan as a substrate were 4.8 mg mL -1 and 0.526 µmol min -1 mg -1 , respectively. Whereas values of the partially purified xylanase from C. thermophilum were 2.96 mg mL -1 and 0.25 µmol min -1 mg -1 , respectively. These findings in this study have great implications for the future applications of xylanases.

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Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost

Cited by 63 publications

References 44 publications

Insight into Glycoside Hydrolases for Debranched Xylan Degradation from Extremely Thermophilic Bacterium Caldicellulosiruptor lactoaceticus

Insight into Glycoside Hydrolases for Debranched Xylan Degradation from Extremely Thermophilic Bacterium Caldicellulosiruptor lactoaceticus

Microbial xylanases and their industrial application in pulp and paper biobleaching: a review

Comparative study for the kinetics of extracellular xylanases from Trichoderma harzianum and Chaetomium thermophilum

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