An extracellular laccase with potent dye decolorizing ability from white rot fungus Trametes sp. LAC-01
A novel laccase was purified from fermentation broth of white rot fungus Trametes sp. LAC-01 using an isolation procedure involving three ion-exchange chromatography steps on DEAE-cellulose, SP-Sepharose, and Q-Sepharose, and one gel-filtration step. The purified enzyme (TSL) was proved as a monomeric protein with a Mr of 59kDa based on SDS-PAGE and FPLC. Partial amino acid sequences were obtained by LC-MS/MS sharing considerably high sequence similarity with that of other laccases. It possessed optimal pH of 2.6 and temperature of 60°C using ABTS as the substrate. The Km of the laccase toward ABTS was estimated to 30.28μM at pH 2.6 and 40°C. TSL manifested considerably high oxidizing activity toward ABTS, but was avoid of degradative activity toward benzidine, caftaric acid, etc. It was effective in the decolorization of phenolic dyes - Bromothymol Blue and Malachite Green with decolorization rate higher than 60% after 24h of incubation. Adjunction of Cu(2+) with the final concentration of 2.0mmol/L significantly activated laccase production with a steady high level of 275.8-282.2U/mL in 96-144h. The high yield and short production period makes Trametes sp. LAC-01 and TSL potentially useful for industrial and environmental application and commercialization..
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
2015 |
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| Erschienen: |
2015 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:81 |
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| Enthalten in: |
International journal of biological macromolecules - 81(2015), Seite 785-793 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Ling, Zhuo-Ren [VerfasserIn] |
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| Links: |
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| BKL: |
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| doi: |
10.1016/j.ijbiomac.2015.09.011 |
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| funding: |
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| PPN (Katalog-ID): |
OLC1968212663 |
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| 245 | 1 | 3 | |a An extracellular laccase with potent dye decolorizing ability from white rot fungus Trametes sp. LAC-01 |
| 264 | 1 | |c 2015 | |
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| 520 | |a A novel laccase was purified from fermentation broth of white rot fungus Trametes sp. LAC-01 using an isolation procedure involving three ion-exchange chromatography steps on DEAE-cellulose, SP-Sepharose, and Q-Sepharose, and one gel-filtration step. The purified enzyme (TSL) was proved as a monomeric protein with a Mr of 59kDa based on SDS-PAGE and FPLC. Partial amino acid sequences were obtained by LC-MS/MS sharing considerably high sequence similarity with that of other laccases. It possessed optimal pH of 2.6 and temperature of 60°C using ABTS as the substrate. The Km of the laccase toward ABTS was estimated to 30.28μM at pH 2.6 and 40°C. TSL manifested considerably high oxidizing activity toward ABTS, but was avoid of degradative activity toward benzidine, caftaric acid, etc. It was effective in the decolorization of phenolic dyes - Bromothymol Blue and Malachite Green with decolorization rate higher than 60% after 24h of incubation. Adjunction of Cu(2+) with the final concentration of 2.0mmol/L significantly activated laccase production with a steady high level of 275.8-282.2U/mL in 96-144h. The high yield and short production period makes Trametes sp. LAC-01 and TSL potentially useful for industrial and environmental application and commercialization. | ||
| 540 | |a Nutzungsrecht: Copyright © 2015 Elsevier B.V. All rights reserved. | ||
| 700 | 1 | |a Wang, Shan-Shan |4 oth | |
| 700 | 1 | |a Zhu, Meng-Juan |4 oth | |
| 700 | 1 | |a Ning, Ying-Jie |4 oth | |
| 700 | 1 | |a Wang, Shou-Nan |4 oth | |
| 700 | 1 | |a Li, Bing |4 oth | |
| 700 | 1 | |a Yang, Ai-Zhen |4 oth | |
| 700 | 1 | |a Zhang, Guo-Qing |4 oth | |
| 700 | 1 | |a Zhao, Xiao-Meng |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |t International journal of biological macromolecules |d Guilford : Butterworth-Heinemann, 1979 |g 81(2015), Seite 785-793 |w (DE-627)129859893 |w (DE-600)282732-3 |w (DE-576)015168255 |x 0141-8130 |7 nnns |
| 773 | 1 | 8 | |g volume:81 |g year:2015 |g pages:785-793 |
| 856 | 4 | 1 | |u http://dx.doi.org/10.1016/j.ijbiomac.2015.09.011 |3 Volltext |
| 856 | 4 | 2 | |u http://www.ncbi.nlm.nih.gov/pubmed/26361865 |
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