1. Biochemical Characterization of Low Molecular Weight Thermostable Xylanase from Aspergillus fumigatus JCM 10253.
- Author
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Paramjeet, S., Manasa, P., and Korrapati, N.
- Subjects
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XYLANASES , *ASPERGILLUS fumigatus , *MOLECULAR weights , *TRITON X-100 , *AMMONIUM sulfate , *ORGANIC solvents - Abstract
The thermostable xylanase from Aspergillus fumigatus JCM 10253 was purified and characterized. The purification of the enzyme was carried out by 80% ammonium sulphate precipitation followed by dialysis and DEAE-cellulose ion-exchange chromatography with a 17.1% yield. The molecular weight of purified xylanase was approximately 19 kDa. The optimum xylanase activity was achieved at 45°C and pH 6.0. The metal profile exhibited activating effect at 10 mM concentration of Ca2+, Fe2+, Mg2+, Mn2+, K+, Zn2+, Ba2+, and Co2+ ions. The xylanase activity was strongly inhibited by SDS, sodium sulfite, and phenylmethylsulfonyl fluoride whilst stimulated by Triton X-100. The presence of organic 30% solvents, 1-butanol and n-pentane, retained xylanase activity during a prolonged incubation period of 7 days. The purified enzyme had KM and Vmax values of 10.95 mg/mL and 115.8 µmol mg–1min–1, respectively, against beechwood xylan as a substrate. The purified xylanase from A. fumigatus JCM 10253 could be a potential candidate for developing high value-added products. [ABSTRACT FROM AUTHOR]
- Published
- 2021
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