Improvement of Laccase Production by <i>Thielavia terrestris</i> Co3Bag1. Enhancing the Bio-Catalytic Performance of the Native Thermophilic <i>Tt</i>LacA via Immobilization in Copper Alginate Gel Beads
A 32-fold increase in laccase activity production by the thermophilic biomass-degrading fungus <i>T. terrestris</i> Co3Bag1 was achieved when the microorganism was grown on a modified medium containing fructose, sodium nitrate, and copper. A 70 kDa laccase (<i>Tt</i>LacA), pr...
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| Format: | Article |
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MDPI AG
2023-02-01
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| Series: | Journal of Fungi |
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| Online Access: | https://www.mdpi.com/2309-608X/9/3/308 |
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| author | Marina Gutiérrez-Antón Alejandro Santiago-Hernández Johan Rodríguez-Mendoza Claudia Cano-Ramírez Ismael Bustos-Jaimes Guillermo Aguilar-Osorio Jorge E. Campos María Eugenia Hidalgo-Lara |
| author_facet | Marina Gutiérrez-Antón Alejandro Santiago-Hernández Johan Rodríguez-Mendoza Claudia Cano-Ramírez Ismael Bustos-Jaimes Guillermo Aguilar-Osorio Jorge E. Campos María Eugenia Hidalgo-Lara |
| author_sort | Marina Gutiérrez-Antón |
| collection | DOAJ |
| description | A 32-fold increase in laccase activity production by the thermophilic biomass-degrading fungus <i>T. terrestris</i> Co3Bag1 was achieved when the microorganism was grown on a modified medium containing fructose, sodium nitrate, and copper. A 70 kDa laccase (<i>Tt</i>LacA), produced under the above conditions, was purified, immobilized in copper alginate gel beads, and characterized. <i>Tt</i>LacA, both free and immobilized enzymes, exhibited optimal activity at pH 3.0, at a temperature of 65 and 70 °C, respectively, although both displayed 70% of activity from 40 to 70 °C. Free and immobilized enzymes retained at least 80% of relative activity in the pH range from 3 to 4.6. Immobilized <i>Tt</i>LacA manifested a 2.3-fold higher thermal stability than the free form of the enzyme at 60 and 70 °C. Immobilized <i>Tt</i>LacA retained 95% initial activity for six consecutive reuse cycles at 60 °C, and also retained 86% of initial activity after 12 days of storage at 4 °C. Based on the biochemical features, thermophilic <i>Tt</i>LacA may be an efficient enzyme for dye decolorization and other industrial applications at high temperatures or acidic conditions. This work represents the first report about the immobilization and biochemical characterization of a thermophilic laccase from a member of the genus <i>Thielavia.</i> |
| first_indexed | 2024-03-11T06:19:51Z |
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| institution | Directory Open Access Journal |
| issn | 2309-608X |
| language | English |
| last_indexed | 2024-03-11T06:19:51Z |
| publishDate | 2023-02-01 |
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| series | Journal of Fungi |
| spelling | doaj.art-1c8f05086b424b658387b04fbaa9af6e2023-11-17T11:59:45ZengMDPI AGJournal of Fungi2309-608X2023-02-019330810.3390/jof9030308Improvement of Laccase Production by <i>Thielavia terrestris</i> Co3Bag1. Enhancing the Bio-Catalytic Performance of the Native Thermophilic <i>Tt</i>LacA via Immobilization in Copper Alginate Gel BeadsMarina Gutiérrez-Antón0Alejandro Santiago-Hernández1Johan Rodríguez-Mendoza2Claudia Cano-Ramírez3Ismael Bustos-Jaimes4Guillermo Aguilar-Osorio5Jorge E. Campos6María Eugenia Hidalgo-Lara7Laboratory Ingeniería de Proteínas, Departamento de Biotecnología y Bioingeniería, CINVESTAV-IPN, Av. Instituto Politécnico Nacional No. 2508, Ciudad de México 07360, MexicoLaboratory Ingeniería de Proteínas, Departamento de Biotecnología y Bioingeniería, CINVESTAV-IPN, Av. Instituto Politécnico Nacional No. 2508, Ciudad de México 07360, MexicoLaboratory Ingeniería de Proteínas, Departamento de Biotecnología y Bioingeniería, CINVESTAV-IPN, Av. Instituto Politécnico Nacional No. 2508, Ciudad de México 07360, MexicoLaboratory Variación Biológica y Evolución, ENCB-IPN, Prol. De Carpio y Plan de Ayala s/n, Col. Santo Tomas, Ciudad de México 11340, MexicoLaboratory Fisicoquímica e Ingeniería de Proteínas, Departamento de Bioquímica, Facultad de Medicina UNAM, Ciudad Universitaria, Ciudad de México 04510, MexicoGrupo de Fisiología de Hongos, Departamento de Alimentos y Biotecnología, Facultad de Química UNAM, Ciudad Universitaria, Ciudad de México 04510, MexicoLaboratory Bioquímica Molecular, UBIPRO, FES Iztacala, UNAM. Av. de los Barrios No. 1, Los Reyes Iztacala, Tlalnepantla de Baz 54090, MexicoLaboratory Ingeniería de Proteínas, Departamento de Biotecnología y Bioingeniería, CINVESTAV-IPN, Av. Instituto Politécnico Nacional No. 2508, Ciudad de México 07360, MexicoA 32-fold increase in laccase activity production by the thermophilic biomass-degrading fungus <i>T. terrestris</i> Co3Bag1 was achieved when the microorganism was grown on a modified medium containing fructose, sodium nitrate, and copper. A 70 kDa laccase (<i>Tt</i>LacA), produced under the above conditions, was purified, immobilized in copper alginate gel beads, and characterized. <i>Tt</i>LacA, both free and immobilized enzymes, exhibited optimal activity at pH 3.0, at a temperature of 65 and 70 °C, respectively, although both displayed 70% of activity from 40 to 70 °C. Free and immobilized enzymes retained at least 80% of relative activity in the pH range from 3 to 4.6. Immobilized <i>Tt</i>LacA manifested a 2.3-fold higher thermal stability than the free form of the enzyme at 60 and 70 °C. Immobilized <i>Tt</i>LacA retained 95% initial activity for six consecutive reuse cycles at 60 °C, and also retained 86% of initial activity after 12 days of storage at 4 °C. Based on the biochemical features, thermophilic <i>Tt</i>LacA may be an efficient enzyme for dye decolorization and other industrial applications at high temperatures or acidic conditions. This work represents the first report about the immobilization and biochemical characterization of a thermophilic laccase from a member of the genus <i>Thielavia.</i>https://www.mdpi.com/2309-608X/9/3/308<i>Thielavia terrestris</i>fungal laccasealginate immobilizationthermophilic thermostable enzyme |
| spellingShingle | Marina Gutiérrez-Antón Alejandro Santiago-Hernández Johan Rodríguez-Mendoza Claudia Cano-Ramírez Ismael Bustos-Jaimes Guillermo Aguilar-Osorio Jorge E. Campos María Eugenia Hidalgo-Lara Improvement of Laccase Production by <i>Thielavia terrestris</i> Co3Bag1. Enhancing the Bio-Catalytic Performance of the Native Thermophilic <i>Tt</i>LacA via Immobilization in Copper Alginate Gel Beads Journal of Fungi <i>Thielavia terrestris</i> fungal laccase alginate immobilization thermophilic thermostable enzyme |
| title | Improvement of Laccase Production by <i>Thielavia terrestris</i> Co3Bag1. Enhancing the Bio-Catalytic Performance of the Native Thermophilic <i>Tt</i>LacA via Immobilization in Copper Alginate Gel Beads |
| title_full | Improvement of Laccase Production by <i>Thielavia terrestris</i> Co3Bag1. Enhancing the Bio-Catalytic Performance of the Native Thermophilic <i>Tt</i>LacA via Immobilization in Copper Alginate Gel Beads |
| title_fullStr | Improvement of Laccase Production by <i>Thielavia terrestris</i> Co3Bag1. Enhancing the Bio-Catalytic Performance of the Native Thermophilic <i>Tt</i>LacA via Immobilization in Copper Alginate Gel Beads |
| title_full_unstemmed | Improvement of Laccase Production by <i>Thielavia terrestris</i> Co3Bag1. Enhancing the Bio-Catalytic Performance of the Native Thermophilic <i>Tt</i>LacA via Immobilization in Copper Alginate Gel Beads |
| title_short | Improvement of Laccase Production by <i>Thielavia terrestris</i> Co3Bag1. Enhancing the Bio-Catalytic Performance of the Native Thermophilic <i>Tt</i>LacA via Immobilization in Copper Alginate Gel Beads |
| title_sort | improvement of laccase production by i thielavia terrestris i co3bag1 enhancing the bio catalytic performance of the native thermophilic i tt i laca via immobilization in copper alginate gel beads |
| topic | <i>Thielavia terrestris</i> fungal laccase alginate immobilization thermophilic thermostable enzyme |
| url | https://www.mdpi.com/2309-608X/9/3/308 |
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