Strain effect on extracellular laccase activities from<i>Botrytis cinerea</i>

Quijada-Morín, Natalia; Garcia, François; Lambert, Karen; Walker, Anne‐Sophie; Tiers, Laurent; Viaud, Muriel; Sauvage, François-Xavier; Hirtz, Christophe; Saucier, Cédric

doi:10.1111/ajgw.12322

Cited by 15 publications

(12 citation statements)

References 57 publications

(104 reference statements)

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“…On the other hand, laccase activity is important in cocoa fermentation, as this enzyme is involved in the breakdown of lignin, hemicellulose, and cellulose present in the cocoa shell; in addition, it could also have an impact on the oxidation of phenolic substances, such as anthocyanidins present in cocoa beans [ 45 ]. This activity was the most diffused among all the tested species: P. kudriavzevii (24/54), S. cerevisiae (10/38), P. mashurica (2/13), W. anomalus (2/6), Torulapora pretoriens (2/2), Z. bisporus (1/1), S. sorbosivorans , and T. asahii var.…”

Section: Resultsmentioning

confidence: 99%

Functional Biodiversity of Yeasts Isolated from Colombian Fermented and Dry Cocoa Beans

et al. 2020

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Yeasts play an important role in the cocoa fermentation process. Although the most relevant function is the degradation of sugars and the production of ethanol, there is little understanding of the enzyme activities and attributes that allow them to survive even after drying. The present study explored the functional biodiversity of yeasts associated with Criollo Colombian cocoa fermented beans, able to survive after drying. Twelve species belonging to 10 genera of osmo-, acid-, thermo-, and desiccation-tolerant yeasts were isolated and identified from fermented and dry cocoa beans, with Pichia kudriavzevii and Saccharomyces cerevisiae standing out as the most frequent. For the first time, we reported the presence of Zygosaccharomyces bisporus in cocoa fermented beans. It was found that resistance to desiccation is related to the different degradation capacities of fermentation substrates, which suggests that associative relationships may exist between the different yeast species and their degradation products. Besides, the increased thermotolerance of some species was related to the presence of polyphenols in the medium, which might play a fundamental role in shaping the microbial community composition.

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Section: Resultsmentioning

confidence: 99%

Functional Biodiversity of Yeasts Isolated from Colombian Fermented and Dry Cocoa Beans

et al. 2020

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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%

“…Usually, each Botrytis spp. strain can produce several laccase isoenzymes of rather different physico-chemical features [ 32 , 33 , 34 , 35 , 36 , 37 , 38 ]. Such abundance of laccases produced by these fungi is not surprising, as 15 genes encoding laccases have been identified in the genome of B. cinerea [ 39 , 40 ].…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Yellow Laccase from Botrytis cinerea 241

Radveikienė

Vidžiūnaitė

Meškienė

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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“…Laccase from Botrytis cinerea was obtained as described by Quijada-Morin et al [ 36 ]. It was produced from the VA612 strain (collected in 2005 in a vineyard in Hautvillers, Champagne, France, from the Pinot Noir cultivar).…”

Section: Methodsmentioning

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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Strain effect on extracellular laccase activities fromBotrytis cinerea

Cited by 15 publications

References 57 publications

Functional Biodiversity of Yeasts Isolated from Colombian Fermented and Dry Cocoa Beans

Functional Biodiversity of Yeasts Isolated from Colombian Fermented and Dry Cocoa Beans

Characterization of a Yellow Laccase from Botrytis cinerea 241

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

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