Some Properties of a New Thermostable Xylanase from Alkaliphilic and Thermophilic Bacillus sp. Isolate DM-15

Özcan, Bahri Devrim; Coşkun, Ali Levent; Özcan, Neslihan Keser; Baylan, Makbule

doi:10.3923/javaa.2011.138.143

Cited by 3 publications

(4 citation statements)

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“…strain SPS-0 (Bataillon et al 2000 ); in this experiment, maximum xylanase production was reported in the presence of Ca 2+ (138%); some other researchers also reported that Ca 2+ ion strongly stimulated xylanase activity. Slightly stimulation was also observed by addition of Mg 2+ (106%) (Mamo et al 2006 ; Lv et al 2008 ; Ozcan et al 2011 ).…”

Section: Resultsmentioning

confidence: 98%

“…The enzyme produced by Bacillus sp. strain DM-15 was stable for 15 min at 60 °C while 95% of the original activity was lost at 90 °C (Ozcan et al 2011 ).…”

Section: Resultsmentioning

confidence: 99%

“…Triton X-100 and β-mercaptoethanol had little effect on the xylanase activity (Table 2 ) whereas the Bacillus DM-15 xylanase is sensitive (Ozcan et al 2011 ).…”

Section: Resultsmentioning

confidence: 99%

“…The effect of metallic ions at concentration of 5 mM, chelating agents, surfactants, and inhibitors on the activity of crude xylanase were determined by preincubating the enzyme in the presence of Na + , Mg 2+ , Ca 2+ , Mn 2+ , Fe 2+ , Zn 2+ , Cu 2+ , K + , Hg 2+ , and Cd 2+ , EDTA (5 Mm), SDS (1%), β-mercaptoethanol (20 mM), and Triton X-100 (1%) for 30 min at 55 °C before adding the substrate (Ozcan et al 2011 ). Subsequently, relative xylanase activities were measured at standard enzyme assay conditions.…”

Section: Methodsmentioning

confidence: 99%

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Biochemical properties of a new thermo- and solvent-stable xylanase recovered using three phase partitioning from the extract of Bacillus oceanisediminis strain SJ3

Boucherba

Gagaoua

Bouanane‐Darenfed

et al. 2017

Bioresour. Bioprocess.

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The present study investigates the production and partial biochemical characterization of an extracellular thermostable xylanase from the Bacillus oceanisediminis strain SJ3 newly recovered from Algerian soil using three phase partitioning (TPP). The maximum xylanase activity recorded after 2 days of incubation at 37 °C was 20.24 U/ml in the presence of oat spelt xylan. The results indicated that the enzyme recovered in the middle phase of TPP system using the optimum parameters were determined as 50% ammonium sulfate saturation with 1.0:1.5 ratio of crude extract: t-butanol at pH and temperature of 8.0 and 10 °C, respectively. The xylanase was recovered with 3.48 purification fold and 107% activity recovery. The enzyme was optimally active at pH 7.0 and was stable over a broad pH range of 5.0–10. The optimum temperature for xylanase activity was 55 °C and the half-life time at this temperature was of 6 h. At this time point the enzyme retained 50% of its activity after incubation for 2 h at 95 °C. The crude enzyme resist to sodium dodecyl sulfate and β-mercaptoethanol, while all the tested ions do not affect the activity of the enzyme. The recovered enzyme is, at least, stable in tested organic solvents except in propanol where a reduction of 46.5% was observed. Further, the stability of the xylanase was higher in hydrophobic solvents where a maximum stability was observed with cyclohexane. These properties make this enzyme to be highly thermostable and may be suggested as a potential candidate for application in some industrial processes. To the best of our knowledge, this is the first report of xylanase activity and recoverey using three phase partitioning from B. oceanisediminis.

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Section: Resultsmentioning

confidence: 98%

“…The enzyme produced by Bacillus sp. strain DM-15 was stable for 15 min at 60 °C while 95% of the original activity was lost at 90 °C (Ozcan et al 2011 ).…”

Section: Resultsmentioning

confidence: 99%

“…Triton X-100 and β-mercaptoethanol had little effect on the xylanase activity (Table 2 ) whereas the Bacillus DM-15 xylanase is sensitive (Ozcan et al 2011 ).…”

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations