Production of manganese peroxidase and laccase in a solid-state bioreactor and modeling of enzyme production kinetics

Moilanen, Ulla; Winquist, Erika; Mattila, Tiina; Hatakka, Annele; Eerikäinen, Tero

doi:10.1007/s00449-014-1243-0

Cited by 22 publications

(7 citation statements)

References 47 publications

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“…Moilanen et al [16] reported that the maximum MnP activity (340 nkat/g DM) occurred after 14 days of fermentation in a solid-state reactor with an internal conveyor, but their MnP activity stayed at almost the same level at 100 g-scale in plastic jars and 4 kg-scale in bioreactor cultivation. A similar study was carried out by Vivekanand et al [32] using a bioreactor that contained four circular aluminum trays, and the maximum MnP activity (1,339.0 ± 131.23 U/l) was obtained after 6 days of SSF by Aspergillus fumigatus VkJ2.4.5.…”

Section: Discussionmentioning

confidence: 99%

Fungal Growth and Manganese Peroxidase Production in a Deep Tray Solid-State Bioreactor, and In Vitro Decolorization of Poly R-478 by MnP

Zhao¹,

Huang²,

Yao³

et al. 2015

Journal of Microbiology and Biotechnology

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The growth of Irpex lacteus F17 and manganese peroxidase (MnP) production in a selfdesigned tray bioreactor, operating in solid-state conditions at a laboratory scale, were studied. The bioreactor was divided into three layers by three perforated trays. Agroindustrial residues were used both as the carrier of bound mycelia and as a nutrient medium for the growth of I. lacteus F17. The maximum biomass production in the bioreactor was detected at 60 h of fermentation, which was consistent with the CO2 releasing rate by the fungus. During the stationary phase of fungal growth, the maximum MnP activity was observed, reaching 950 U/l at 84 h. Scanning electron microscopy images clearly showed the growth situation of mycelia on the support matrix. Furthermore, the MnP produced by I. lacteus F17 in the bioreactor was isolated and purified, and the internal peptide sequences were also identified with mass spectrometry. The optimal activity of the enzyme was detected at pH 7 and 25 °C, with a long half-life time of 9 days. In addition, the MnP exhibited significant stability within a broad pH range of 4-7 and at temperature up to 55 °C. Besides this, the MnP showed the ability to decolorize the polymeric model dye Poly R-478 in vitro.

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Section: Discussionmentioning

confidence: 99%

Fungal Growth and Manganese Peroxidase Production in a Deep Tray Solid-State Bioreactor, and In Vitro Decolorization of Poly R-478 by MnP

Zhao¹,

Huang²,

Yao³

et al. 2015

Journal of Microbiology and Biotechnology

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“…In order to carry out large-scale laccase production by SSF, culture parameters should be investigated at a large scale, and some adjustments are necessary. Moilanen et al (2014) found a change in laccase activity obtained for a large-scale laboratory culture [63]. Among the culture parameters, the water content is one of the key points for the scaling up of laccase production by SSF.…”

Section: Comparison Of Laccase Production From Lignocellulosic Agricumentioning

confidence: 99%

Fungal Laccase Production from Lignocellulosic Agricultural Wastes by Solid-State Fermentation: A Review

et al. 2019

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Laccases are copper-containing oxidase enzymes found in many fungi. They have received increasing research attention because of their broad substrate specificity and applicability in industrial processes, such as pulp delignification, textile bleaching, phenolic removal, and biosensors. In comparison with traditional submerged fermentation (SF), solid-state fermentation (SSF) is a simpler technique for laccase production and has many advantages, including higher productivity, efficiency, and enzyme stability as well as reduced production costs and environmental pollution. Here, we review recent advances in laccase production technology, with focus on the following areas: (i) Characteristics and advantages of lignocellulosic agricultural wastes used as SSF substrates of laccase production, including detailed suggestions for the selection of lignocellulosic agricultural wastes; (ii) Comparison of fungal laccase production from lignocellulosic substrates by either SSF or SF; (iii) Fungal performance and strain screening in laccase production from lignocellulosic agricultural wastes by SSF; (iv) Applications of laccase production under SSF; and (v) Suggestions and avenues for future studies of laccase production by fungal SSF with lignocellulosic materials and its applications.

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“…Soy medium also in this case supported a high expression of Rb5 bleaching activity. One of the efficient producer of VP activity was Cerrena unicolor PM170798, which is known as a very efficient producer of laccase [43], like many other C. unicolor strains [44].…”

Section: Production Of Lignin-modifying Peroxidasesmentioning

confidence: 99%

Improved Efficiency in Screening for Lignin-Modifying Peroxidases and Laccases of Basidiomycetes

Kinnunen

Maijala

Järvinen

et al. 2017

CBIOT

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Abstract:Background: Wood rotting white-rot and litter-decomposing basidiomycetes form a huge reservoir of oxidative enzymes, needed for applications in the pulp and paper and textile industries and for bioremediation.Objective: The aim was (i) to achieve higher throughput in enzyme screening through miniaturization and automatization of the activity assays, and (ii) to discover fungi which produce efficient oxidoreductases for industrial purposes.Methods: Miniaturized activity assays mostly using dyes as substrate were carried out for lignin peroxidase, versatile peroxidase, manganese peroxidase and laccase. Methods were validated and 53 species of basidiomycetes were screened for lignin modifying enzymes when cultivated in liquid mineral, soy, peptone and solid state oat husk medium.Results: Manganese peroxidases were the most common enzymes produced by 96% of the species. They typically had acidic pH optima, although Hyphodontia sp., Pleurotus pulmonarius and Trametes ochracea produced enzymes highly active at pH 7. Versatile peroxidase was produced by 66% of the fungi with efficient production from Phlebia radiata, P. pulmonarius and Galerina marginata. Novel lignin peroxidase producing fungi Cylindrobasidium evolvens and Daedaleopsis septentrionalis were found among the 26% of the species showing here lignin peroxidase production. Laccase was shown in 92% of the species. Several fungi produced laccase active at pH 7, which is noteworthy because usually laccases of white-rot fungi are efficient and relevant for many industrial applications. Conclusion:Automated screening allowed us to monitor many specific enzyme activities and extend the range of assay conditions from relatively small fungal cultivation sample volumes.

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Production of manganese peroxidase and laccase in a solid-state bioreactor and modeling of enzyme production kinetics

Cited by 22 publications

References 47 publications

Fungal Growth and Manganese Peroxidase Production in a Deep Tray Solid-State Bioreactor, and In Vitro Decolorization of Poly R-478 by MnP

Fungal Growth and Manganese Peroxidase Production in a Deep Tray Solid-State Bioreactor, and In Vitro Decolorization of Poly R-478 by MnP

Fungal Laccase Production from Lignocellulosic Agricultural Wastes by Solid-State Fermentation: A Review

Improved Efficiency in Screening for Lignin-Modifying Peroxidases and Laccases of Basidiomycetes

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