Characterization and application of a novel laccase derived from Bacillus amyloliquefaciens
| Autor: | Yanzhen Li, Jieying Ma, Fuping Lu, Yuanfu Zhang, Hongbin Wang, Shuang Wang, Nan Wang, Yihan Liu, Lin Huang, Xiuqi Ge |
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| Rok vydání: | 2020 |
| Předmět: |
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Molecular Hot Temperature Bacillus amyloliquefaciens 02 engineering and technology medicine.disease_cause Biochemistry Anthraquinone Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Structural Biology RNA Ribosomal 16S Escherichia coli medicine Cloning Molecular Molecular Biology Soil Microbiology 030304 developmental biology chemistry.chemical_classification Laccase 0303 health sciences ABTS Triphenylmethane biology Water Decolorization Substrate (chemistry) Gene Expression Regulation Bacterial General Medicine Hydrogen-Ion Concentration 021001 nanoscience & nanotechnology biology.organism_classification Recombinant Proteins Kinetics Enzyme chemistry Textile Industry 0210 nano-technology Sequence Alignment |
| Zdroj: | International Journal of Biological Macromolecules. 150:982-990 |
| ISSN: | 0141-8130 |
| Popis: | As the copper-containing enzymes, laccases demonstrate a promising potential in various environmental and industrial applications. In this study, a bacterial strain isolated from soil exhibited the laccase activity, which was subsequently characterized and named as Bacillus amyloliquefaciens TCCC 111018. The novel gene encoding CotA-laccase (lac) was amplified using the genome of B. amyloliquefaciens TCCC 111018 as the template and efficiently and actively expressed in Escherichia coli. The recombinant LAC (rLAC) exhibited its highest activity at 80 °C and pH 5.5 for 2,2′-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) oxidization and 80 °C and pH 7.0 for 2,6-dimethoxyphenol (2,6-DMP) oxidization. rLAC was stable at up to 60 °C and within the pH ranging from 3.0 to 9.0 when using the substrate ABTS. Furthermore, rLAC demonstrated the relatively high tolerance to NaCl, SDS, and most metal ions. Moreover, rLAC was capable of decolorizing the structurally different azo, anthraquinone, and triphenylmethane with different mediator at 60 °C under pH 5.5, 7.0, and 9.0. Therefore, rLAC would be an ideal candidate for lots of biotechnological and industrial applications due to its stability in the extreme conditions, including but not limit to pH, high temperature, halides, heavy metals and detergents. |
| Databáze: | OpenAIRE |
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