Isolation and Identification of a Newly Isolated Alternaria sp. ND-16 and Characterization of Xylanase

Li, Yin; Liu, Zhi‐Qiang; Cui, Fengjie; Ping, Lifeng; Qiu, Chongyan; Li, Geng; Yan, Liying

doi:10.1007/s12010-008-8239-7

Cited by 7 publications

(8 citation statements)

References 40 publications

(40 reference statements)

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“…The optimum temperature and the optimum pH of XYN186 were similar to other family 11 endoxylanases from many mesophilis fungi (Polizeli et al 2005). These enzyme properties suggest that XYN186 could be used as a feed additive working in the gastrointestinal tract under acidic conditions.…”

Section: Discussionsupporting

confidence: 52%

Molecular cloning and heterologous expression of an acid stable xylanase gene from Alternaria sp. HB186

Mao

Meng

Zhou

et al. 2011

World J Microbiol Biotechnol

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A new xylanase gene, named xyn186, was cloned by the genome-walking PCR method from the Alternaria sp. HB186. The sequence of xyn186 contains a 748 bp open reading frame separated by one intron with the size of 52 bp. The cDNA was obtained by DpnI-mediated intron deletion. The cDNA was cloned into pHBM905A and transformed into Pichia pastoris GS115 to screen xylanase-secreting transformants on RBB-xylan plates. The molecular mass of the enzyme was estimated to be 23 kDa on SDS-PAGE. The optimal pH and temperature of the purified enzyme is 6 and 50°C, respectively. The K (m) and V (max) valued for birchwood xylan are 1.404 mg ml(-1) and 0.2748 mmol min(-1) mg(-1), respectively. The inhibitory effects of various metal ions were investigated, Cu(2+) and Hg(2+) ions inhibited most of the enzyme activity. The gene copy number of xyn186 in the genome of P. pastoris was estimated as two by the Real-time PCR. To date, xyn186 gene is the first xylanase gene cloned from the genus Alternaria.

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Section: Discussionsupporting

confidence: 52%

Molecular cloning and heterologous expression of an acid stable xylanase gene from Alternaria sp. HB186

Mao

Meng

Zhou

et al. 2011

World J Microbiol Biotechnol

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“…Trichosporum cutaneum [14], Alternaria sp. ND-16 [15], Chaetomium thermophile [16], and Aspergillus tamarii [17], when cultivated on submerged fermentation using wheat bran as carbon source, presented xylanase activity of 39.7 U mL −1 , 20.0 U mL −1 , 27.8 U mL −1 , and 54.32 U mL −1 , respectively. Better results of xylanase activity of 107 U mL −1 , 102 U mL − 1, and 97 U mL −1 were obtained when Thermoascus aurantiacus was cultivated on solid-state fermentation using corncob, grass, and corn straw, respectively [9].…”

Section: Solid-state Fermentationmentioning

confidence: 99%

“…On the other hand, some authors use agroindustrial waste for submerged fermentation processes for cultivating bacteria or fungi, such as Bacillus circulans AB16 [11], Clostridium absonum CFR-702 [12], Aspergillus foetidus MTCC4898 [13], Trichosporon cutaneum SL409 [14], Alternaria sp. ND-16 [15], Chaetomium thermophile NIBGE [16], Aspergillus tamari [17]. Other authors use solidstate fermentation in minor scale for preferentially cultivating fungi, such as Thermoascus aurantiacus [9,18], Trichoderma harzianum [19], Bacillus sp.…”

Section: Introductionmentioning

confidence: 99%

Screening and Production Study of Microbial Xylanase Producers from Brazilian Cerrado

Alves-Prado

Pavezzi

Leite

et al. 2009

Appl Biochem Biotechnol

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Hemicelluloses are polysaccharides of low molecular weight containing 100 to 200 glycosidic residues. In plants, the xylans or the hemicelluloses are situated between the lignin and the collection of cellulose fibers underneath. The xylan is the most common hemicellulosic polysaccharide in cell walls of land plants, comprising a backbone of xylose residues linked by beta-1,4-glycosidic bonds. So, xylanolytic enzymes from microorganism have attracted a great deal of attention in the last decade, particularly because of their biotechnological characteristics in various industrial processes, related to food, feed, ethanol, pulp, and paper industries. A microbial screening of xylanase producer was carried out in Brazilian Cerrado area in Selviria city, Mato Grosso do Sul State, Brazil. About 50 bacterial strains and 15 fungal strains were isolated from soil sample at 35 degrees C. Between these isolated microorganisms, a bacterium Lysinibacillus sp. and a fungus Neosartorya spinosa as good xylanase producers were identified. Based on identification processes, Lysinibacillus sp. is a new species and the xylanase production by this bacterial genus was not reported yet. Similarly, it has not reported about xylanase production from N. spinosa. The bacterial strain P5B1 identified as Lysinibacillus sp. was cultivated on submerged fermentation using as substrate xylan, wheat bran, corn straw, corncob, and sugar cane bagasse. Corn straw and wheat bran show a good xylanase activity after 72 h of fermentation. A fungus identified as N. spinosa (strain P2D16) was cultivated on solid-state fermentation using as substrate source wheat bran, wheat bran plus sawdust, corn straw, corncob, cassava bran, and sugar cane bagasse. Wheat bran and corncobs show the better xylanase production after 72 h of fermentation. Both crude xylanases were characterized and a bacterial xylanase shows optimum pH for enzyme activity at 6.0, whereas a fungal xylanase has optimum pH at 5.0-5.5. They were stable in the pH range 5.0-10.0 and 5.5-8.5 for bacterial and fungal xylanase, respectively. The optimum temperatures were 55 and 60 degrees C for bacterial and fungal xylanase, respectively, and they were thermally stable up to 50 degrees C.

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“…Under heterogeneous environments, cells must adapt themselves for survival. Carbon sources are essential elements for microorganisms during the period of growth and metabolic process [30]. The strain BT14 could grow on soluble and insoluble polysaccharides including plant biomass such as corn hulls.…”

Section: Discussionmentioning

confidence: 99%

“…4C, lane 2) with a molecular mass range of 30 to 227 kDa. Zymograms revealed 4 proteins (30,92,148, and 227 kDa) having cellulase activity (Fig. 4D, lane 2) and 5 proteins (55, 92, 148, 221, 227 kDa) having xylanase activity (Fig.…”

Section: Strainmentioning

confidence: 97%

A Cellulolytic and Xylanolytic Enzyme Complex from an Alkalothermoanaerobacterium, Tepidimicrobium xylanilyticum BT14

Phitsuwan

Tachaapaikoon²,

Kosugi³

et al. 2010

J. Microbiol. Biotechnol.

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A cellulolytic and xylanolytic enzyme complex-producing alkalothermoanaerobacterium strain, Tepidimicrobium xylanilyticum BT14, is described. The cell was Grampositive, rod-shaped, and endospore-forming. Based on 16S rRNA gene analysis and various lines of biochemical and physiological properties, the strain BT14 is a new member of the genus Tepidimicrobium. The strain BT14 cells had the ability to bind to Avicel, xylan, and corn hull. The pH and temperature optima for growth were 9.0 and 60 o C, respectively. The strain BT14 was able to use a variety of carbon sources. When the bacterium was grown on corn hulls under an anaerobic condition, a cellulolytic and xylanolytic enzyme complex was produced. Crude enzyme containing cellulase and xylanase of the strain BT14 was active in broad ranges of pH and temperature. The optimum conditions for cellulase and xylanase activities were pH 8.0 and 9.0 at 60 o C, respectively. The crude enzyme had the ability to bind to Avicel and xylan. The analysis of native-PAGE and native-zymograms indicated the cellulosebinding protein showing both cellulase and xylanase activities, whereas SDS-PAGE zymograms showed 4 bands of cellulases and 5 bands of xylanases. Evidence of a cohesinlike amino acid sequence seemed to indicate that the protein complex shared a direct relationship with the cellulosome of Clostridium thermocellum. The crude enzyme from the strain BT14 showed effective degradation of plant biomass. When grown on corn hulls at pH 9.0 and 60 o C under anaerobic conditions, the strain BT14 produced ethanol and acetate as the main fermentation products.

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Isolation and Identification of a Newly Isolated Alternaria sp. ND-16 and Characterization of Xylanase

Cited by 7 publications

References 40 publications

Molecular cloning and heterologous expression of an acid stable xylanase gene from Alternaria sp. HB186

Molecular cloning and heterologous expression of an acid stable xylanase gene from Alternaria sp. HB186

Screening and Production Study of Microbial Xylanase Producers from Brazilian Cerrado

A Cellulolytic and Xylanolytic Enzyme Complex from an Alkalothermoanaerobacterium, Tepidimicrobium xylanilyticum BT14

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