Purification and Characterization of a Xylanase from the Newly Isolated Penicillium rolfsii c3-2(1) IBRL
An extracellular xylanase was purified from the mesophilic fungus Penicillium rolfsii c3-2(1) IBRL. After three consecutive purification steps, the extracellular cellulase-free xylanase was successfully purified to homogeneity with a recovery yield of 24%. A single protein band of 35 kDa was detecte...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
North Carolina State University
2015-01-01
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| Series: | BioResources |
| Subjects: | |
| Online Access: | http://ojs.cnr.ncsu.edu/index.php/BioRes/article/view/BioRes_10_1_1627_Lee_Purification_Xylanase_Penicillium |
| Summary: | An extracellular xylanase was purified from the mesophilic fungus Penicillium rolfsii c3-2(1) IBRL. After three consecutive purification steps, the extracellular cellulase-free xylanase was successfully purified to homogeneity with a recovery yield of 24%. A single protein band of 35 kDa was detected by SDS-PAGE, which had an optimum catalytic activity at pH 5.0 and 50 °C. This purified enzyme was stable at pH 5 to 7, thermostable up to 55 °C, and retained up to 83% of its activity after 4 hours of pre-incubation. A kinetic study yielded estimated Km and Vmax values of 5.73 mg/mL and 691.6 µmol/min/mg, respectively. Thin layer chromatography experiments showed that the purified xylanase was capable of hydrolyzing xylotriose, xylotetraose, xylopentaose, and xylohexaose but not xylobiose, suggesting it is an endo-xylanase. Enzymatic hydrolysis of oil palm trunk residues by commercial enzymes supplemented with the purified xylanase showed a considerable increase in total sugar conversion compared with the commercial enzymes alone, suggesting that xylanase is a key enzyme in the hydrolysis of oil palm trunk residues. |
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| ISSN: | 1930-2126 1930-2126 |