Physiological Peculiarities of Lignin-Modifying Enzyme Production by the White-Rot Basidiomycete Coriolopsis gallica Strain BCC 142
Sixteen white-rot Basidiomycota isolates were screened for production of lignin-modifying enzymes (LME) in glycerol- and mandarin peel-containing media. In the synthetic medium, Cerrena unicolor strains were the only high laccase (Lac) (3.2–9.4 U/mL) and manganese peroxidase (MnP) (0.56–1.64 U/mL) p...
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MDPI AG
2017-11-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/5/4/73 |
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| author | Vladimir Elisashvili Eva Kachlishvili Mikheil D. Asatiani Ramona Darlington Katarzyna H. Kucharzyk |
| author_facet | Vladimir Elisashvili Eva Kachlishvili Mikheil D. Asatiani Ramona Darlington Katarzyna H. Kucharzyk |
| author_sort | Vladimir Elisashvili |
| collection | DOAJ |
| description | Sixteen white-rot Basidiomycota isolates were screened for production of lignin-modifying enzymes (LME) in glycerol- and mandarin peel-containing media. In the synthetic medium, Cerrena unicolor strains were the only high laccase (Lac) (3.2–9.4 U/mL) and manganese peroxidase (MnP) (0.56–1.64 U/mL) producers while one isolate Coriolopsis gallica was the only lignin peroxidase (LiP) (0.07 U/mL) producer. Addition of mandarin peels to the synthetic medium promoted Lac production either due to an increase in fungal biomass (Funalia trogii, Trametes hirsuta, and T. versicolor) or enhancement of enzyme production (C. unicolor, Merulius tremellosus, Phlebia radiata, Trametes ochracea). Mandarin peels favored enhanced MnP and LiP secretion by the majority of the tested fungi. The ability of LiP activity production by C. gallica, C. unicolor, F. trogii, T. ochracea, and T. zonatus in the medium containing mandarin-peels was reported for the first time. Several factors, such as supplementation of the nutrient medium with a variety of lignocellulosic materials, nitrogen source or surfactant (Tween 80, Triton X-100) significantly influenced production of LME by a novel strain of C. gallica. Moreover, C. gallica was found to be a promising LME producer with a potential for an easy scale up cultivation in a bioreactor and high enzyme yields (Lac-9.4 U/mL, MnP-0.31 U/mL, LiP-0.45 U/mL). |
| first_indexed | 2024-04-12T09:20:38Z |
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| language | English |
| last_indexed | 2024-04-12T09:20:38Z |
| publishDate | 2017-11-01 |
| publisher | MDPI AG |
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| series | Microorganisms |
| spelling | doaj.art-999adae558824001b57dad71ad14aaad2022-12-22T03:38:39ZengMDPI AGMicroorganisms2076-26072017-11-01547310.3390/microorganisms5040073microorganisms5040073Physiological Peculiarities of Lignin-Modifying Enzyme Production by the White-Rot Basidiomycete Coriolopsis gallica Strain BCC 142Vladimir Elisashvili0Eva Kachlishvili1Mikheil D. Asatiani2Ramona Darlington3Katarzyna H. Kucharzyk4Agricultural University of Georgia, 240 David Agmashenebeli Alley, 0159 Tbilisi, GeorgiaAgricultural University of Georgia, 240 David Agmashenebeli Alley, 0159 Tbilisi, GeorgiaAgricultural University of Georgia, 240 David Agmashenebeli Alley, 0159 Tbilisi, GeorgiaBattelle Memorial Institute, 505 King Ave, Columbus, OH 43212, USABattelle Memorial Institute, 505 King Ave, Columbus, OH 43212, USASixteen white-rot Basidiomycota isolates were screened for production of lignin-modifying enzymes (LME) in glycerol- and mandarin peel-containing media. In the synthetic medium, Cerrena unicolor strains were the only high laccase (Lac) (3.2–9.4 U/mL) and manganese peroxidase (MnP) (0.56–1.64 U/mL) producers while one isolate Coriolopsis gallica was the only lignin peroxidase (LiP) (0.07 U/mL) producer. Addition of mandarin peels to the synthetic medium promoted Lac production either due to an increase in fungal biomass (Funalia trogii, Trametes hirsuta, and T. versicolor) or enhancement of enzyme production (C. unicolor, Merulius tremellosus, Phlebia radiata, Trametes ochracea). Mandarin peels favored enhanced MnP and LiP secretion by the majority of the tested fungi. The ability of LiP activity production by C. gallica, C. unicolor, F. trogii, T. ochracea, and T. zonatus in the medium containing mandarin-peels was reported for the first time. Several factors, such as supplementation of the nutrient medium with a variety of lignocellulosic materials, nitrogen source or surfactant (Tween 80, Triton X-100) significantly influenced production of LME by a novel strain of C. gallica. Moreover, C. gallica was found to be a promising LME producer with a potential for an easy scale up cultivation in a bioreactor and high enzyme yields (Lac-9.4 U/mL, MnP-0.31 U/mL, LiP-0.45 U/mL).https://www.mdpi.com/2076-2607/5/4/73Coriolopsis gallicawhite-rot basidiomyceteslignin-modifying enzymesproductionoptimizationsubmerged fermentation |
| spellingShingle | Vladimir Elisashvili Eva Kachlishvili Mikheil D. Asatiani Ramona Darlington Katarzyna H. Kucharzyk Physiological Peculiarities of Lignin-Modifying Enzyme Production by the White-Rot Basidiomycete Coriolopsis gallica Strain BCC 142 Microorganisms Coriolopsis gallica white-rot basidiomycetes lignin-modifying enzymes production optimization submerged fermentation |
| title | Physiological Peculiarities of Lignin-Modifying Enzyme Production by the White-Rot Basidiomycete Coriolopsis gallica Strain BCC 142 |
| title_full | Physiological Peculiarities of Lignin-Modifying Enzyme Production by the White-Rot Basidiomycete Coriolopsis gallica Strain BCC 142 |
| title_fullStr | Physiological Peculiarities of Lignin-Modifying Enzyme Production by the White-Rot Basidiomycete Coriolopsis gallica Strain BCC 142 |
| title_full_unstemmed | Physiological Peculiarities of Lignin-Modifying Enzyme Production by the White-Rot Basidiomycete Coriolopsis gallica Strain BCC 142 |
| title_short | Physiological Peculiarities of Lignin-Modifying Enzyme Production by the White-Rot Basidiomycete Coriolopsis gallica Strain BCC 142 |
| title_sort | physiological peculiarities of lignin modifying enzyme production by the white rot basidiomycete coriolopsis gallica strain bcc 142 |
| topic | Coriolopsis gallica white-rot basidiomycetes lignin-modifying enzymes production optimization submerged fermentation |
| url | https://www.mdpi.com/2076-2607/5/4/73 |
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