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Cloning, Expression, and Characterization of an Alkalophillic Endo-1,4-beta-xylanase from Paenibacillus Sp. Hpl-002
| Content Provider | Semantic Scholar |
|---|---|
| Author | Park, N. Lim, Hee Kyung Song, Ha Young Lee, Kee-In |
| Copyright Year | 2012 |
| Abstract | The biochemical properties of a purified enzyme of a new alkalophillic endo-1,4-beta-xylanase gene, KRICT PX2 (GU967374), which was isolated from Paenibacillus sp. HPL-002 (KCTC11410BP) and expressed in E. coli, were investigated. The specific activity of the purified xylanase was 51.26 μmol/min/mg proteins. The Km and Vmax values of the protein for birch wood xylan were also verified to have 0.061 μM and 55.3 μmol/min/mg proteins, respectively. The optimum pH and temperature for the activity of the enzyme were pH 8~9 and 50oC, respectively, and, the activity was stably maintained at 40oC. Most metallic salts, ethylenediamine tetra-acetic acid, 2-mercaptoethanol, phenylmethane-sulphonyl fluoride, and furfural, have no impact on the enzyme’s activity at 1 mM. The simulated 3-D structure of this xylanase is similar to Xyn10B from Paenibacillus barcinonensis. Further research on the degradation of different-origin xylans and enzyme production will be necessary for practical applications. |
| Starting Page | 727 |
| Ending Page | 742 |
| Page Count | 16 |
| File Format | PDF HTM / HTML |
| DOI | 10.15376/biores.7.1.0727-0742 |
| Alternate Webpage(s) | https://bioresources.cnr.ncsu.edu/BioRes_07/BioRes_07_1_0727_Park_LSKLH_Cloning_Expr_Char_Xylanase_2303.pdf |
| Alternate Webpage(s) | https://bioresources.cnr.ncsu.edu/BioRes_07/BioRes_07_Unsecured/BioRes_07_1_0727_Park_LSKLH_Cloning_Expr_Char_Xylanase_2303.pdf |
| Alternate Webpage(s) | https://doi.org/10.15376/biores.7.1.0727-0742 |
| Volume Number | 7 |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
