Purification and characterization of a thermostable xylanase from Bacillus amyloliquefaciens

Breccia, Javier D.; Siñeríz, Faustino; Baigorí, Mario Domingo; Castro, Guillermo R.; Hatti‐Kaul, Rajni

doi:10.1016/s0141-0229(97)00102-6

Cited by 108 publications

(61 citation statements)

References 33 publications

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“…24) However, certain rXyn11A properties, such as its broad pH range (pH 3 to pH 10) for activity ( Fig. 2A), which are consistent with previous reports on native homologs, 25,26) are of potential interest in feed and food applications. 27) In conclusion, wild-type K. lactis CBS 1065 efficiently expressed and secreted B. halodurans recombinant Xyn11A.…”

Section: )supporting

confidence: 89%

High-Level Heterologous Expression ofBacillus haloduransPutative Xylanase Xyn11A (BH0899) inKluyveromyces lactis

Wamalwa

Zhao

Sakka

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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Section: )supporting

confidence: 89%

High-Level Heterologous Expression ofBacillus haloduransPutative Xylanase Xyn11A (BH0899) inKluyveromyces lactis

Wamalwa

Zhao

Sakka

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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“…Other research groups reported purification of xylanase by employing a combination of two or more different methods including salt fractionation, ion-exchange, gel filtration and hydrophobic interaction chromatography (1,5,7,16,24,29,35,36). The overall purification in the present study using one step was higher than that reported from Bacillus amyloliquefaciens (7) and Bacillus circulans (36) using a multistep sequence of purification.…”

Section: Purification Of Xylanasementioning

confidence: 99%

One-step purification and characterization of cellulase-free xylanase produced by alkalophilic Bacillus subtilis ash

Sanghi¹,

Garg²,

Gupta³

et al. 2010

Braz. J. Microbiol.

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The present study describes the one-step purification and characterization of an extracellular cellulase-free xylanase from a newly isolated alkalophilic and moderately thermophilic strain of Bacillus subtilis ASH.Xylanase was purified to homogeneity by 10.5-fold with ~43% recovery using ion-exchange chromatography through CM-Sephadex C-50. The purified enzyme revealed a single band on SDS-PAGE gel with a molecular mass of 23 kDa. It showed an optimum pH at 7.0 and was stable over the pH range 6.0-9.0. The optimum temperature for enzyme activity was 55 °C. The purified xylanase did not lose any activity up to 45 ºC, however, it retained 80% and 51% of its activity after pre-incubation at 55 ºC and 60 ºC, respectively. The enzyme obeyed Michaelis-Menton kinetics towards birch wood xylan with apparent K m 3.33 mg/ml and V max 100 IU/ml. The enzyme was strongly inhibited by Hg 2+ and Cu 2+ while enhanced by Co 2+ and Mn 2+. The purified enzyme could be stored at 4 ºC for six weeks without any loss of catalytic activity. The faster and economical purification of the cellulase-free xylanase from B. subtilis ASH by onestep procedure together with its appreciable stability at high temperature and alkaline pH makes it potentially effective for industrial applications.

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“…The multiplicity of forms is commonly described for β-xylanases from fungi and bacteria as result of differential mRNA processing and posttranslational modifications (4,14). Since all xylosidic linkages are not equivalent and equally accessible in xylan molecule, its catalytic cleavage requires the action of multiple forms of xylan-degrading enzyme systems (4).…”

mentioning

confidence: 99%

Production of xylan-degrading enzymes by a Trichoderma harzianum strain

Cacais¹,

Silveira²,

Filho³

2001

Braz. J. Microbiol.

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Trichoderma harzianum strain 4 produced extracellular xylan-degrading enzymes, namely β-xylanase, β-xylosidase and α-arabinofuranosidase, when grown in liquid medium cultures containing oat spelt xylan as inducer. Cellulase activity was not detected. The pattern of xylan-degrading enzymes induction was influenced by the form of xylan present in the medium. They were detected in different incubation periods. Electrophoretic separation of the proteins from liquid culture filtrates by SDS-PAGE showed a variety of bands with high and low molecular weights.

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Purification and characterization of a thermostable xylanase from Bacillus amyloliquefaciens

Cited by 108 publications

References 33 publications

High-Level Heterologous Expression ofBacillus haloduransPutative Xylanase Xyn11A (BH0899) inKluyveromyces lactis

High-Level Heterologous Expression ofBacillus haloduransPutative Xylanase Xyn11A (BH0899) inKluyveromyces lactis

One-step purification and characterization of cellulase-free xylanase produced by alkalophilic Bacillus subtilis ash

Production of xylan-degrading enzymes by a Trichoderma harzianum strain

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