Characterization of a Yellow Laccase from Botrytis cinerea 241

Abstract

Typical laccases have four copper atoms, which form three different copper centers, of which the T1 copper is responsible for the blue color of the enzyme and gives it a characteristic absorbance around 610 nm. Several laccases have unusual spectral properties and are referred to as yellow or white laccases. Only two yellow laccases from the Ascomycota phylum have been described previously, and only one amino acid sequence of those enzymes is available. A yellow laccase Bcl1 from Botrytis cinerea strain 241 has been identified, purified and characterized in this work. The enzyme appears to be a dimer with a molecular mass of 186 kDa. The gene encoding the Bcl1 protein has been cloned, and the sequence analysis shows that the yellow laccase Bcl1 is phylogenetically distinct from other known yellow laccases. In addition, a comparison of amino acid sequences, and 3D modeling shows that the Bcl1 laccase lacks a conservative tyrosine, which is responsible for absorption quenching at 610 nm in another yellow asco-laccase from Sclerotinia sclerotiorum. High thermostability, high salt tolerance, broad substrate specificity, and the ability to decolorize dyes without the mediators suggest that the Bcl1 laccase is a potential enzyme for various industrial applications.

Yellow laccase produced by Trametes versicolor K1 on tomato waste: A comparative study with the blue one produced on semi-synthetic medium

“…GluLac and TmtLac optimal temperature was similar to reported ones (do Rosário Freixo et al, 2012;Radveikien ė et al, 2021). Some laccases showed higher optimal temperatures up to 80 • C from strains of T. versicolor (Freixo et al, 2008b) and T. oriantalis (Zheng et al, 2017).…”

“…AA. Leontievsky et al, 1997) but many other theories have been proposed afterwards, to understand the mechanism monitoring the shifting of the blue laccase to yellow one, including changes in oxidation level (Radveikien ė et al, 2021), structural sphere (Mate et al, 2013), glycosylation state (Mot ¸ et al, 2012), and interaction with metal ions (Radveikien ė et al, 2021). The evidence to be sought from an industrial standpoint will be whether the difference in color of the yellow laccase produced on lignocellulosic waste has an impact on its catalytic activity.…”

Green production of a yellow laccase by Coriolopsis gallica for phenolic pollutants removal

“…In general, a typical laccase molecule contains four copper atoms with three types of copper sites (T1, T2, and T3), both type I and type III copper ions have the characteristic absorption in the UV–vis spectrum except for type II (Dwivedi et al 2011 ; Rivera-Hoyos et al 2013 ). Herein, the absorption peak at 610 nm represents the T1 copper site of typical blue laccase, while the shoulder around 330 nm represents the T3 copper site of laccase (Radveikienė et al 2021 ). The UV–vis spectrum of CGLac performed a characteristic absorption peak of protein near 280 nm, but no peak near 610 nm and 330 nm (Fig.…”

“…In addition, the types of laccases probably relate to strains and growth conditions. Radveikienė et al ( 2021 ) reported Botrytis cinerea 241 secreted two different laccases (blue and yellow laccases) depending on the cultivation conditions. They found the medium with lower copper concentration was more efficient for yellow laccase production.…”

Laccases and Tyrosinases in Organic Synthesis

“…The absorption of the T1 site at 605 nm (in the Lac from Trametes versicolor ) is the cause of the blue color of Lac [ 8 ]. However, some laccases with an altered catalytic site structure may appear “yellow“ or “white“ [ 8 , 9 , 10 ]. We refer to previous studies [ 1 , 7 , 8 , 11 , 12 ] for an explanation of the catalytic mechanism and the structure-activity relationships in Lacs.…”