Production and characterization of tyrosinase activity in Pycnoporus sanguineus CCT-4518 crude extract

Duarte, Lívia Teixeira; Tiba, Joyce Batista; Santiago, Mariângela Fontes; García, Telma Alves

doi:10.1590/s1517-83822012000100003

Cited by 8 publications

(5 citation statements)

References 30 publications

(50 reference statements)

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“…B13, respectively. The factors affecting our findings may not be precisely identifiable at the moment, however, our deduction disagrees with the observations of Duarte et al [29] and Valipour and Arikan [23], who reported 48 h and 16 h optima for Pycnoporus sanguineus and Bacillus megaterium, respectively.…”

Section: Optimization Studies On Tyrosinase Productioncontrasting

confidence: 99%

Optimization and Characterization of Tyrosinases from Multi-enzyme Producing Fusarium solani and Fumago sp.

Odeniyi

Ogunsanya

Unuofin

2019

Period. Polytech. Chem. Eng.

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Tyrosinase is a copper-containing metalloprotein that catalyzes the oxidation of tyrosine, in particular, L-DOPA to L-Dopaquinone, which are precursors of brown pigments in some wounded eukaryotic tissues. The present study focused on screening, production and characterization of tyrosinase from multi-enzyme producing Fusarium solani B1 and Fumago sp. A total of 25 strains were isolated from rotting wood samples and screened for hydrolytic and oxidative multi-enzyme potentials using different polymeric substrates. The two most consistent strains: Fusarium solani B1 and Fumago sp. B13 were further evaluated for tyrosinase production. Some media cultural parameters and physiological conditions were optimized in order to maximize tyrosinase production. Incubation of Fumago sp. B13 and Fusarium solani B1 for 96 and 144 h in medium containing 2 % and 0.2 % ratios of Glucose and NaNO3 with pH 6 and 7, respectively, was most suitable for tyrosinase production. Characterization of the partially purified tyrosinase from Fumago sp. B13 and Fusarium solani B1 exhibited optimal activities at pH 6-7, 30 °C, and 1 mM Cu2+, respectively, thereby suggesting their potentials for novel biotechnological applications.

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Section: Optimization Studies On Tyrosinase Productioncontrasting

confidence: 99%

Optimization and Characterization of Tyrosinases from Multi-enzyme Producing Fusarium solani and Fumago sp.

Odeniyi

Ogunsanya

Unuofin

2019

Period. Polytech. Chem. Eng.

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“…The thermostability of the tyrosinase from L. pulmonaria resembles that of the enzyme from free-living fungi (e.g. Duarte et al 2012) (Fig. 4).…”

Section: Kinetics Of Tyrosinase and Other Redox Enzymesmentioning

confidence: 84%

Characterization and role of tyrosinases in the lichenLobaria pulmonaria(L.) Hoffm.

et al. 2016

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Tyrosinases are a widespread family of multicopper oxidase enzymes. In our earlier work, we identified the presence of tyrosinases in lichenized Ascomycetes based on their substratum specificity, sensitivity to inhibitors and molecular mass. Here, we present a more detailed characterization of a tyrosinase from the lichen Lobaria pulmonaria. We also compare tyrosinase activity with the activities of laccases and peroxidases, the other redox enzymes present in this species. The importance of tyrosinases in lichen biology was studied by testing their role in melanin synthesis. Laboratory experiments clearly showed that tyrosinases from L. pulmonaria resemble those from other lichens and in free-living fungi. While the tyrosinases can metabolize the melanin precursor L-DOPA, L-DOPA can also be metabolized by peroxidases and laccases. A field experiment showed that exposing shade-adapted L. pulmonaria to normal solar radiation induces L-DOPA melanin synthesis. Synthesis occurred when lichens were exposed to either direct sunlight, or placed under a wavelength-neutral filter that slightly reduced overall light. In lichens receiving unfiltered sunlight, melanin synthesis was accompanied by increased laccase activity; by contrast, no changes in enzyme activity occurred in lichens placed under the wavelength-neutral filter. Melanization was reduced by placing lichens under filters that removed UV-B, and prevented by filters that removed both UV-A and UV-B. Removing UV-B had no effect on enzyme activity, whereas removing both UV-A and UV-B increased tyrosinase activity. Results from this study indicate that under some conditions laccases may be involved in melanin synthesis, but they provide no evidence for a role for tyrosinases in melanization. Although high tyrosinase activities are widespread in lichens, many questions on the role of this enzyme in lichen biology remain to be answered.

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“…The latter finding is somewhat unexpected since enzyme activity, e.g. the activity of tyrosinase, is related to temperature and becomes reduced below 37°C (Boron & Boulpaep, 2012; Duarte et al, 2012). However, a possible cause of the lower percentage of pigment-containing cells found at higher storage temperatures could be poorer cell integrity at these temperatures, with subsequent loss of pigment granules to the extracellular space.…”

Section: Discussionmentioning

confidence: 99%

Cultured Human Retinal Pigment Epithelial (hRPE) Sheets: A Search for Suitable Storage Conditions

et al. 2018

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The advancement of human retinal pigment epithelial cell (hRPE) replacement therapy is partly dependent on optimization of cell culture, cell preservation, and storage medium. This study was undertaken to search for a suitable storage temperature and storage medium for hRPE. hRPE monolayer sheets were cultured under standard conditions at 37°C and then randomized for storage at six temperatures (4, 16, 20, 24, 28, and 37°C) for 7 days. After revealing a suitable storage temperature, hRPE sheets were subsequently stored with and without the silk protein sericin added to the storage medium. Live/dead assay, light microscopy, pH, and phenotypic expression of various proteins were used to assess cell cultures stored at different temperatures. After 7 days of storage, hRPE morphology was best preserved at 4°C. Addition of sericin to the storage medium maintained the characteristic morphology of the preserved cells, and improved pigmentation and levels of pigmentation-related proteins in the cultured hRPE sheets following a 7-day storage period at 4°C.

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Production and characterization of tyrosinase activity in Pycnoporus sanguineus CCT-4518 crude extract

Cited by 8 publications

References 30 publications

Optimization and Characterization of Tyrosinases from Multi-enzyme Producing Fusarium solani and Fumago sp.

Optimization and Characterization of Tyrosinases from Multi-enzyme Producing Fusarium solani and Fumago sp.

Characterization and role of tyrosinases in the lichenLobaria pulmonaria(L.) Hoffm.

Cultured Human Retinal Pigment Epithelial (hRPE) Sheets: A Search for Suitable Storage Conditions

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