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Updated: Jun 26, 2026
Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
Published on: February 24, 2026
Laccase isoforms with unusual properties from the basidiomycete Steccherinum ochraceum strain 1833
A Chernykh1, N Myasoedova, M Kolomytseva
1G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms RAS, Pushchino, Moscow Region, Russia.
Aims:
To isolate and characterize the laccase isoforms from S. ochraceum 1833 - a new active producer of high extracellular laccase activity.
Methods And Results:
Three laccase isoforms (laccases I, II and III) with 57.5, 59.5 and 63 kDa molecular masses respectively were purified from S. ochraceum 1833 and in contrast to the known laccases had strongly pronounced absorption at 611 nm with molar extinction coefficients ranging from 7170 to 7830 mol(-1) l cm(-1). All isoforms showed maximal activity with ABTS at low pH (
Conclusions:
Elevated temperature optima, high thermo- and pH-stabilities, the broad substrate specificity of the isoforms make the laccases from S. ochraceum 1833 a suitable model for biotechnological processes proceeding at high temperatures.
Significance And Impact Of The Study:
For the first time, new basidiomycete strain S. ochraceum was reported as a producer of novel thermostable, pH stable, acidophilic laccases with unusual spectral properties.
