| Autor: |
Kok Chang Lee, Takamitsu Arai, Darah Ibrahim, Panida Prawitwong, Lan Deng, Yoshinori Murata, Yutaka Mori, Akihiko Kosugi |
| Jazyk: |
angličtina |
| Rok vydání: |
2015 |
| Předmět: |
|
| Zdroj: |
BioResources, Vol 10, Iss 1, Pp 1627-1643 (2015) |
| Druh dokumentu: |
article |
| ISSN: |
1930-2126 |
| DOI: |
10.15376/biores.10.1.1627-1643 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
|
