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...
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| Language: | English |
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North Carolina State University
2015-01-01
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| Series: | BioResources |
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| Online Access: | http://ojs.cnr.ncsu.edu/index.php/BioRes/article/view/BioRes_10_1_1627_Lee_Purification_Xylanase_Penicillium |
| _version_ | 1811208706979790848 |
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| author | Kok Chang Lee Takamitsu Arai Darah Ibrahim Panida Prawitwong Lan Deng Yoshinori Murata Yutaka Mori Akihiko Kosugi |
| author_facet | Kok Chang Lee Takamitsu Arai Darah Ibrahim Panida Prawitwong Lan Deng Yoshinori Murata Yutaka Mori Akihiko Kosugi |
| author_sort | Kok Chang Lee |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T04:26:08Z |
| format | Article |
| id | doaj.art-d8a706f9406947ba890288687ed0154b |
| institution | Directory Open Access Journal |
| issn | 1930-2126 1930-2126 |
| language | English |
| last_indexed | 2024-04-12T04:26:08Z |
| publishDate | 2015-01-01 |
| publisher | North Carolina State University |
| record_format | Article |
| series | BioResources |
| spelling | doaj.art-d8a706f9406947ba890288687ed0154b2022-12-22T03:48:05ZengNorth Carolina State UniversityBioResources1930-21261930-21262015-01-011011627164310.15376/biores.10.1.1627-1643Purification and Characterization of a Xylanase from the Newly Isolated Penicillium rolfsii c3-2(1) IBRLKok Chang Lee0Takamitsu Arai1Darah Ibrahim2Panida Prawitwong3Lan Deng4Yoshinori Murata5Yutaka Mori6Akihiko Kosugi7School of Biological Sciences, Universiti Sains Malaysia, 11800 Penang, Malaysia; MalaysiaJapan International Research Center for Agricultural Sciences; JapanSchool of Biological Sciences, Universiti Sains Malaysia, 11800 Penang, Malaysia; MalaysiaJapan International Research Center for Agricultural SciencesJapan International Research Center for Agricultural SciencesJapan International Research Center for Agricultural SciencesJapan International Research Center for Agricultural SciencesJapan International Research Center for Agricultural SciencesAn 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.http://ojs.cnr.ncsu.edu/index.php/BioRes/article/view/BioRes_10_1_1627_Lee_Purification_Xylanase_PenicilliumOil palm trunkThermostabilityXylanaseXylo-oligosaccharidePenicillium rolfsii |
| spellingShingle | Kok Chang Lee Takamitsu Arai Darah Ibrahim Panida Prawitwong Lan Deng Yoshinori Murata Yutaka Mori Akihiko Kosugi Purification and Characterization of a Xylanase from the Newly Isolated Penicillium rolfsii c3-2(1) IBRL BioResources Oil palm trunk Thermostability Xylanase Xylo-oligosaccharide Penicillium rolfsii |
| title | Purification and Characterization of a Xylanase from the Newly Isolated Penicillium rolfsii c3-2(1) IBRL |
| title_full | Purification and Characterization of a Xylanase from the Newly Isolated Penicillium rolfsii c3-2(1) IBRL |
| title_fullStr | Purification and Characterization of a Xylanase from the Newly Isolated Penicillium rolfsii c3-2(1) IBRL |
| title_full_unstemmed | Purification and Characterization of a Xylanase from the Newly Isolated Penicillium rolfsii c3-2(1) IBRL |
| title_short | Purification and Characterization of a Xylanase from the Newly Isolated Penicillium rolfsii c3-2(1) IBRL |
| title_sort | purification and characterization of a xylanase from the newly isolated penicillium rolfsii c3 2 1 ibrl |
| topic | Oil palm trunk Thermostability Xylanase Xylo-oligosaccharide Penicillium rolfsii |
| url | http://ojs.cnr.ncsu.edu/index.php/BioRes/article/view/BioRes_10_1_1627_Lee_Purification_Xylanase_Penicillium |
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