“…3a, for 10 min reaction the optimum temperature was 55 °C (assayed in the range 20–100 °C), the xylanase produced by Bacillus brevis is also optimally active at the same temperature (Goswami et al 2013). The optimum temperature of the enzyme is near to that of the xylanases from B. subtilis strain CXJZ isolated from the degumming line (60 °C) (Guo et al 2012) and Bacillus sp.…”
Section: Resultsmentioning
confidence: 99%
“…4 ), at 50 °C there was no significant decrease in xylanase activity during 4 h. The enzyme was stable at 50 °C, with a half-life time of 9 h, a half-life time of 6 and 4.72 h was respectively observed at 55 and 60 °C. B. brevis xylanase is less thermostable, it showed a half-life time of 3 h at 55 °C (Goswami et al 2013 ). Fig.…”
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.
“…3a, for 10 min reaction the optimum temperature was 55 °C (assayed in the range 20–100 °C), the xylanase produced by Bacillus brevis is also optimally active at the same temperature (Goswami et al 2013). The optimum temperature of the enzyme is near to that of the xylanases from B. subtilis strain CXJZ isolated from the degumming line (60 °C) (Guo et al 2012) and Bacillus sp.…”
Section: Resultsmentioning
confidence: 99%
“…4 ), at 50 °C there was no significant decrease in xylanase activity during 4 h. The enzyme was stable at 50 °C, with a half-life time of 9 h, a half-life time of 6 and 4.72 h was respectively observed at 55 and 60 °C. B. brevis xylanase is less thermostable, it showed a half-life time of 3 h at 55 °C (Goswami et al 2013 ). Fig.…”
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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