<i>Bacillus</i> sp. GLN Laccase Characterization: Industry and Biotechnology Implications
Laccases are multicopper oxidases that exhibit a broad substrate spectrum, making them excellent biocatalysts for clean technological processes. The study isolated novel laccase-producing bacteria from decomposed wood samples and characterized the enzyme for potential industrial and biotechnological...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-05-01
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| Series: | Applied Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2076-3417/15/9/5144 |
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| Summary: | Laccases are multicopper oxidases that exhibit a broad substrate spectrum, making them excellent biocatalysts for clean technological processes. The study isolated novel laccase-producing bacteria from decomposed wood samples and characterized the enzyme for potential industrial and biotechnological applications. The results showed that three bacteria, SP-2, SP-1, and WP-2, out of the eight isolated bacteria, oxidized both guaiacol and α-naphthol in the plate assay and exhibited extracellular laccase activity of 7.0 ± 0.01, 6.67 ± 0.02, and 7.40 ± 0.04 (U/mL), respectively. WP-2 was selected for further study and was identified as <i>Bacillus</i> sp. GLN (accessioned number: MK290989). Strain GLN maximally secreted laccase 48 h post-fermentation, with an enzyme yield of 36.83 ± 2.47 U/mL in optimized conditions. The crude laccase was optimally active at pH 9.0 and 90 °C and showed excellent pH and thermal stability, retaining approximately 65% residual activity at 100 °C for 270 min. GLN laccase demonstrated remarkable stability after treatment with organic solvents and metal ions, retaining more than 50% of its original activity in the presence of 100 mM inhibitors. The data from this study highlight the relevance of <i>Bacillus</i> sp. GLN and its laccase in promoting clean technology. |
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| ISSN: | 2076-3417 |