Laccases 2 &amp; 3 as biomarkers of Botrytis cinerea infection in sweet white wines

Ployon, Sarah; Attina, A.; Vialaret, Jérôme; Walker, Anne Sophie; Hirtz, Christophe; Saucier, Cédric

doi:10.1016/j.foodchem.2020.126233

Cited by 8 publications

(5 citation statements)

References 21 publications

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“…The sequence of Bcl1 is highly similar (differs by five amino acid residues only) to the Bclcc7 protein from Botrytis cinerea B05.10. According to the published data, the bclcc7 gene is functional and the corresponding laccase has been detected in the vineyards and botrytized wines [36,38,67], however, the Bclcc7 enzyme has not been purified and characterized previously. In addition, a phylogenetic analysis shows, that Bcl1 and Sclerotinia sclerotiorum laccase has a low similarity (38% of identical amino acids) and are located on two different phylogenetic branches (Figure 3).…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Yellow Laccase from Botrytis cinerea 241

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et al. 2021

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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.

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Section: Discussionmentioning

confidence: 99%

Characterization of a Yellow Laccase from Botrytis cinerea 241

Radveikienė

Vidžiūnaitė

Meškienė

et al. 2021

JoF

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“…Enzymatic oxidation mainly occurs in grape must, but further wine browning may be due to chemical oxidation reactions [ 7 , 13 ] or to Botrytis cinerea laccase that can be very stable during wine ageing [ 14 ]. Two oxidation enzymatic activities may occur on phenolic substrates: monophenol oxidase activity characterized by the hydroxylation of an existing hydroxyl group adjacent position and diphenol oxidase activity corresponding to the oxidation of ortho -dihydroxybenzenes to ortho -benzoquinones.…”

Section: Introductionmentioning

confidence: 99%

“…The aim of this work was first to compare by UHPLC-MS the dimeric (+)-catechin oxidation products profiles in the presence of three oxidoreductase extracts, i.e., PPO extracted from grapes, laccase from the fungus Botrytis cinerea present in botrytized sweet wines [ 14 ], and laccase from Trametes versicolor.…”

Section: Introductionmentioning

confidence: 99%

Unambiguous NMR Structural Determination of (+)-Catechin—Laccase Dimeric Reaction Products as Potential Markers of Grape and Wine Oxidation

et al. 2021

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(+)-Catechin—laccase oxidation dimeric standards were hemi-synthesized using laccase from Trametes versicolor in a water-ethanol solution at pH 3.6. Eight fractions corresponding to eight potential oxidation dimeric products were detected. The fractions profiles were compared with profiles obtained with two other oxidoreductases: polyphenoloxidase extracted from grapes and laccase from Botrytis cinerea. The profiles were very similar, although some minor differences suggested possible dissimilarities in the reactivity of these enzymes. Five fractions were then isolated and analyzed by 1D and 2D NMR spectroscopy. The addition of traces of cadmium nitrate in the samples solubilized in acetone-d6 led to fully resolved NMR signals of phenolic protons, allowing the unambiguous structural determination of six reaction products, one of the fractions containing two enantiomers. These products can further be used as oxidation markers to investigate their presence and evolution in wine during winemaking and wine ageing.

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“…Moreover, botrytized grapes possess more polysaccharides of high molecular weight, which may cause problems during fermentation processes (Blanco-Ulate et al, 2015). Additionally, laccase secreted by B. cinerea can catalyze the oxidation of phenolic compounds into the corresponding quinones, which react further to dark-colored polymers to form brown pigments, a biomarker for B. cinerea infection (Ployon et al, 2020). B. cinerea was responsible for some unwanted wine off flavors such as earthy mushroom aroma (La Guerche et al, 2006).…”

Section: Roles Of B Cinerea In Noble Wine Productionmentioning

confidence: 99%