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Open AccessCommunication

Laccases with Variable Properties from Different Strains of Steccherinum ochraceum: Does Glycosylation Matter?

A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Moscow 119071, Russia
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Int. J. Mol. Sci. 2019, 20(8), 2008; https://doi.org/10.3390/ijms20082008
Received: 15 March 2019 / Revised: 14 April 2019 / Accepted: 19 April 2019 / Published: 24 April 2019
(This article belongs to the Special Issue Industrial Enzymes: Structure, Function and Applications)
Laccases are blue multi-copper oxidases with an extensive number of actual and potential industrial applications. It is known that laccases from different fungal strains may vary in properties; however, the reason of this remains unclear. In the current study we have isolated and characterized seven laccases from different strains of Steccherinum ochraceum obtained from regions of central Russia. Although all seven laccases had the same primary sequences, there was a little variation in their molecular weights and thermostabilities. Moreover, statistically significant differences in laccases’ catalytic parameters of oxidation of phenolic substrates and ABTS were observed. After the deglycosylation of four selected laccases by Endo H and PNGase F, their affinities to pyrocatechol and ABTS became the same, suggesting a substantial role of N-linked glycosylation in moderation of enzymatic properties of laccases. View Full-Text
Keywords: catalytic parameters; Steccherinum ochraceum; laccase; isoform; glycosylation catalytic parameters; Steccherinum ochraceum; laccase; isoform; glycosylation
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Glazunova, O.A.; Moiseenko, K.V.; Kamenihina, I.A.; Isaykina, T.U.; Yaropolov, A.I.; Fedorova, T.V. Laccases with Variable Properties from Different Strains of Steccherinum ochraceum: Does Glycosylation Matter? Int. J. Mol. Sci. 2019, 20, 2008.

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