Purification and characterization of a moderately thermostable xylanase from Bacillus sp. strain SPS-0

Bataillon, Michel; Cardinali, Angela; Castillon, Nicolas; Duchiron, Francis

doi:10.1016/s0141-0229(99)00143-x

Cited by 89 publications

(45 citation statements)

References 13 publications

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“…Albeit most of the reported Bacillus sp. xylanases are strongly inhibited by Mn 2+ , the present finding rather agrees with those of Bataillon et al (2000) and Sá-Pereira et al (2002). Bacillus sp.…”

Section: Resultssupporting

confidence: 90%

Production, purification and characterization of Bacillus sp. GRE7 xylanase and its application in eucalyptus Kraft pulp biobleaching

Kiddinamoorthy

Anceno

Haki

et al. 2007

World J Microbiol Biotechnol

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Production of extracellular xylanase from Bacillus sp. GRE7 using a bench-top bioreactor and solidstate fermentation (SSF) was attempted. SSF using wheat bran as substrate and submerged cultivation using oat-spelt xylan as substrate resulted in an enzyme productivity of 3,950 IU g À1 bran and 180 IU ml À1 , respectively. The purified enzyme had an apparent molecular weight of 42 kDa and showed optimum activity at 70°C and pH 7. The enzyme was stable at 60-80°C at pH 7 and pH 5-11 at 37°C. Metal ions Mn 2+ and Co 2+ increased activity by twofold, while Cu 2+ and Fe 2+ reduced activity by fivefold as compared to the control. At 60°C and pH 6, the K m for oat-spelt xylan was 2.23 mg ml À1 and V max was 296.8 IU mg À1 protein. In the enzymatic prebleaching of eucalyptus Kraft pulp, the release of chromophores, formation of reducing sugars and brightness was higher while the Kappa number was lower than the control with increased enzyme dosage at 30% reduction of the original chlorine dioxide usage. The thermostability, alkali-tolerance, negligible presence of cellulolytic activity, ability to improve brightness and capacity to reduce chlorine dioxide usage demonstrates the high potential of the enzyme for application in the biobleaching of Kraft pulp.

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Section: Resultssupporting

confidence: 90%

Production, purification and characterization of Bacillus sp. GRE7 xylanase and its application in eucalyptus Kraft pulp biobleaching

Kiddinamoorthy

Anceno

Haki

et al. 2007

World J Microbiol Biotechnol

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“…Xylanase from Bacillus sp. SSP-0 was completely inhibited by Hg +2 [46], and in B. subtilis, Mn +2 ions enhanced xylanolytic activities by 2.7-fold, whereas Fe +3 completely inhibited the enzyme activity [47]. Khandeparker et al [48] observed that Fe +3 , Cu +2 , and EDTA inhibited the activity of the xylanase enzyme, while Ca +2 , Zn +2 , and Co +2 enhanced the xylanase activity.…”

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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“…JB-99 [14]), Bacillus amyloliquefaciens [6], and Bacillus sp. SPS-0 [3]. The increase in enzyme activity by reducing agents indicates that involvement of disulWde The enzyme activity was completely inhibited by sulphydryl oxidant metals, such as Cu 2+ and Hg 2+ , and moderately inhibited by Ba 2+ , Fe 2+ , and Zn 2+ .…”

Section: Evects Of Metal Ions and Chemicalsmentioning

confidence: 92%

A novel thermostable xylanase of Paenibacillus macerans IIPSP3 isolated from the termite gut

Dheeran

Nandhagopal

Kumar

et al. 2012

Journal of Industrial Microbiology and Biotechnology

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Xylanase is an enzyme in high demand for various industrial applications, such as those in the biofuel and pulp and paper fields. In this study, xylanase-producing microbes were isolated from the gut of the wood-feeding termite at 50°C. The isolated microbe produced thermostable xylanase that was active over a broad range of temperatures (40-90°C) and pH (3.5-9.5), with optimum activity (4,170 ± 23.5 U mg⁻¹) at 60°C and pH 4.5. The enzyme was purified using a strong cation exchanger and gel filtration chromatography, revealing that the protein has a molecular mass of 205 kDa and calculated pI of 5.38. The half-life of xylanase was 6 h at 60°C and 2 h at 90°C. The isolated thermostable xylanase differed from other xylanases reported to date in terms of size, structure, and mode of action. The novelty of this enzyme lies in its high specific activity and stability at broad ranges of temperature and pH. These properties suggest that this enzyme could be utilized in bioethanol production as well as in the paper and pulp industry.

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Purification and characterization of a moderately thermostable xylanase from Bacillus sp. strain SPS-0

Cited by 89 publications

References 13 publications

Production, purification and characterization of Bacillus sp. GRE7 xylanase and its application in eucalyptus Kraft pulp biobleaching

Production, purification and characterization of Bacillus sp. GRE7 xylanase and its application in eucalyptus Kraft pulp biobleaching

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

A novel thermostable xylanase of Paenibacillus macerans IIPSP3 isolated from the termite gut

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