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| Content Provider | Springer Nature Link |
|---|---|
| Author | Cheng, Rui Xu, Linxiang Wang, Shiming Wang, Yang Zhang, Jianfa |
| Copyright Year | 2013 |
| Abstract | A new β-1,3-1,4-glucanase gene (PlicA) was cloned from Paenibacillus sp. S09. The ORF contained 717 bp coding for a 238 amino acid protein. PlicA, expressed in Escherichia coli and purified by Ni2+-affinity chromatography, had optimum activity at 55 °C and pH 6.2. The specific activity toward barley β-glucan reached 7,055 U/mg. K m and V max values with barley β-glucan were 3.7 mg/ml and 3.3 × 103 μmol/min mg, respectively. The enzyme exhibited acid- and alkali-tolerance with more than 80 % activity remaining after incubation for 4 h at pH 3.5–12. PlicA was salt-tolerant (>90 % activity retained in 4 M NaCl at 25 °C for 24 h) and salt-activated: activity rising 1.5-fold in 0.5 M NaCl. The thermostability was improved by NaCl and CaCl2. This is the first report of an acid-, alkali- and salt-tolerant bacterial β-1,3-1,4-glucanase with high catalytic efficiency. |
| Starting Page | 797 |
| Ending Page | 803 |
| Page Count | 7 |
| File Format | |
| ISSN | 01415492 |
| Journal | Biotechnology Letters |
| Volume Number | 36 |
| Issue Number | 4 |
| e-ISSN | 15736776 |
| Language | English |
| Publisher | Springer Netherlands |
| Publisher Date | 2013-12-10 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Acid tolerance Alkali tolerance β-1,3-1,4-Glucanase Halotolerance Paenibacillus Salt-activated enzyme Microbiology Biotechnology Applied Microbiology Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology |
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