Studies of some biochemical and physicochemical properties of an inducible form of extracellular laccase from the basidiomyceteCoriolus hirsutus

Gorbatova, O. N.; Степанова, Елена В.; Королева, О. В.

doi:10.1007/bf02742571

Cited by 1 publication

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“… 40 , 41 The thermostability and the pH and temperature optima of isoenzymes should be determined under specific conditions. 41 , 42 , 43 , 44 , 45 Our data showed that laccase activity was maximal at pH 3.6, consistent with reported data. 46 This value is somewhat lower than the usual pH range for enzyme activity (between 4 and 6).…”

Section: Discussionsupporting

confidence: 92%

Preliminary studies of new strains of Trametes sp. from Argentina for laccase production ability

Fonseca

Tejerina

Sawostjanik-Afanasiuk

et al. 2016

Brazilian Journal of Microbiology

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Oxidative enzymes secreted by white rot fungi can be applied in several technological processes within the paper industry, biofuel production and bioremediation. The discovery of native strains from the biodiverse Misiones (Argentina) forest can provide useful enzymes for biotechnological purposes. In this work, we evaluated the laccase and manganese peroxidase secretion abilities of four newly discovered strains of Trametes sp. that are native to Misiones. In addition, the copper response and optimal pH and temperature for laccase activity in culture supernatants were determined.The selected strains produced variable amounts of laccase and MnP; when Cu2+ was added, both enzymes were significantly increased. Zymograms showed that two isoenzymes were increased in all strains in the presence of Cu2+. Strain B showed the greatest response to Cu2+ addition, whereas strain A was more stable at the optimal temperature and pH. Strain A showed interesting potential for future biotechnological approaches due to the superior thermo-stability of its secreted enzymes.

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