Expression of a deep-sea bacterial laccase from Halomonas alkaliantartica and its application in dyes decolorization
Abstract Introduction Laccase is a copper-containing polyphenolic oxidase widely found in bacteria, archaea, fungi, animals, and plants. As a green biocatalyst with considerable potential for numerous environmental and industrial applications, the enzyme production efficiency of laccase in nature is...
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| Format: | Article |
| Language: | English |
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BMC
2023-06-01
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| Series: | Annals of Microbiology |
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| Online Access: | https://doi.org/10.1186/s13213-023-01723-w |
| _version_ | 1797806893929857024 |
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| author | Jingjing Wang Ran Zhang Guilan Zhu Lingling Wang Han Bai Yong Qian Xiazhen Zhou Qiang Yin Yan Zhang |
| author_facet | Jingjing Wang Ran Zhang Guilan Zhu Lingling Wang Han Bai Yong Qian Xiazhen Zhou Qiang Yin Yan Zhang |
| author_sort | Jingjing Wang |
| collection | DOAJ |
| description | Abstract Introduction Laccase is a copper-containing polyphenolic oxidase widely found in bacteria, archaea, fungi, animals, and plants. As a green biocatalyst with considerable potential for numerous environmental and industrial applications, the enzyme production efficiency of laccase in nature is low, and the cost is high. Purpose To examine the characterization and potential applications of laccase in this study, a novel laccase from Halomonas alkaliantartica (LacHa) was cloned and heterologously expressed it in Escherichia coli. Results To achieve heterologous and efficient laccase expression, a bacterial laccase gene designed as LacHa from Halomonas alkaliantartica of deep sea was cloned and expressed in E. coli. The results showed that the optimum temperature and pH of the enzyme reaction were 45 °C and 7.5. The 100 μM Cu2+ and Fe2+ ions had the strongest stimulatory effect on laccase activity, the surface-active agent SDS and organic solvent 5% ethanol had opposite effect. EDTA, and 5% DMSO have no effect on LacHa activity. The activity of LacHa was enhanced 1.5-fold by chloride at concentrations lower than 500 mM, and 57.6% of its initial activity remained in the reaction system containing 1000 mM. NaCl. Furthermore, LacHa showed decolorization rates ranging from 90.28 to 100% for indigo carmine and two azo dyes without mediators, with wide pH (5.0–9.0) and temperature (25–65 °C) ranges. Conclusions In this study, LacHa was expressed and showed unusual properties, indicating its great application potential in textile industries or environmental fields. |
| first_indexed | 2024-03-13T06:14:18Z |
| format | Article |
| id | doaj.art-26646cc7263c4bd4972d77279fdca4b7 |
| institution | Directory Open Access Journal |
| issn | 1869-2044 |
| language | English |
| last_indexed | 2024-03-13T06:14:18Z |
| publishDate | 2023-06-01 |
| publisher | BMC |
| record_format | Article |
| series | Annals of Microbiology |
| spelling | doaj.art-26646cc7263c4bd4972d77279fdca4b72023-06-11T11:03:56ZengBMCAnnals of Microbiology1869-20442023-06-0173111110.1186/s13213-023-01723-wExpression of a deep-sea bacterial laccase from Halomonas alkaliantartica and its application in dyes decolorizationJingjing Wang0Ran Zhang1Guilan Zhu2Lingling Wang3Han Bai4Yong Qian5Xiazhen Zhou6Qiang Yin7Yan Zhang8School of Life Sciences, Hefei Normal UniversitySchool of Life Sciences, Hefei Normal UniversitySchool of Life Sciences, Hefei Normal UniversitySchool of Life Sciences, Hefei Normal UniversitySchool of Life Sciences, Hefei Normal UniversitySchool of Life Sciences, Hefei Normal UniversitySchool of Life Sciences, Hefei Normal UniversityAgricultural Engineering Research Institute, Anhui Academy of Agricultural SciencesSchool of Life Sciences, Hefei Normal UniversityAbstract Introduction Laccase is a copper-containing polyphenolic oxidase widely found in bacteria, archaea, fungi, animals, and plants. As a green biocatalyst with considerable potential for numerous environmental and industrial applications, the enzyme production efficiency of laccase in nature is low, and the cost is high. Purpose To examine the characterization and potential applications of laccase in this study, a novel laccase from Halomonas alkaliantartica (LacHa) was cloned and heterologously expressed it in Escherichia coli. Results To achieve heterologous and efficient laccase expression, a bacterial laccase gene designed as LacHa from Halomonas alkaliantartica of deep sea was cloned and expressed in E. coli. The results showed that the optimum temperature and pH of the enzyme reaction were 45 °C and 7.5. The 100 μM Cu2+ and Fe2+ ions had the strongest stimulatory effect on laccase activity, the surface-active agent SDS and organic solvent 5% ethanol had opposite effect. EDTA, and 5% DMSO have no effect on LacHa activity. The activity of LacHa was enhanced 1.5-fold by chloride at concentrations lower than 500 mM, and 57.6% of its initial activity remained in the reaction system containing 1000 mM. NaCl. Furthermore, LacHa showed decolorization rates ranging from 90.28 to 100% for indigo carmine and two azo dyes without mediators, with wide pH (5.0–9.0) and temperature (25–65 °C) ranges. Conclusions In this study, LacHa was expressed and showed unusual properties, indicating its great application potential in textile industries or environmental fields.https://doi.org/10.1186/s13213-023-01723-wBacterial laccaseChloride toleranceDye decolorizationRedox mediator |
| spellingShingle | Jingjing Wang Ran Zhang Guilan Zhu Lingling Wang Han Bai Yong Qian Xiazhen Zhou Qiang Yin Yan Zhang Expression of a deep-sea bacterial laccase from Halomonas alkaliantartica and its application in dyes decolorization Annals of Microbiology Bacterial laccase Chloride tolerance Dye decolorization Redox mediator |
| title | Expression of a deep-sea bacterial laccase from Halomonas alkaliantartica and its application in dyes decolorization |
| title_full | Expression of a deep-sea bacterial laccase from Halomonas alkaliantartica and its application in dyes decolorization |
| title_fullStr | Expression of a deep-sea bacterial laccase from Halomonas alkaliantartica and its application in dyes decolorization |
| title_full_unstemmed | Expression of a deep-sea bacterial laccase from Halomonas alkaliantartica and its application in dyes decolorization |
| title_short | Expression of a deep-sea bacterial laccase from Halomonas alkaliantartica and its application in dyes decolorization |
| title_sort | expression of a deep sea bacterial laccase from halomonas alkaliantartica and its application in dyes decolorization |
| topic | Bacterial laccase Chloride tolerance Dye decolorization Redox mediator |
| url | https://doi.org/10.1186/s13213-023-01723-w |
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