Comprehensive investigation of the enzymatic oligomerization of esculin by laccase in ethanol : water mixtures

Muñiz-Mouro, Abel; Oliveira, Isabel; Gullón, Beatriz; Lú-Chau, Thelmo A.; Moreira, Marı́a Teresa; Lema, Juan M.; Eibes, Gemma

doi:10.1039/c7ra06972c

Cited by 24 publications

(32 citation statements)

References 31 publications

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“…Both the greatest loss of enzymatic activity and the highest rutin conversion occurred during the first 5-6 hours of reaction in both experiments. At that time, the losses in laccase activity reached values close to 50% of the initial activity, which is consistent with the decrease due to the presence of ethanol in the reaction medium, as previously reported [15]. Nevertheless, during the first two hours, the decrease in laccase activity in reaction B was lower than that observed in reaction A (14% and 33%, respectively).…”

Section: Polymerization Reactionsupporting

confidence: 91%

“…As shown in Figure S1, rutin solubility increased from 97.1 mg/L (0% EtOH) up to 3370.1 mg/L (50% EtOH). Combining this result with previous studies on laccase stability in the presence of EtOH [15], the value of 50% EtOH: acetate buffer (pH 5, 10 mM) was chosen as the appropriate reaction medium for this work.…”

Section: Polymerization Reactionmentioning

confidence: 99%

“…Intermediate compounds with lower intensities would correspond to rutin oligomers lacking one or several methyl, OH, glucose, rhamnose, or rutinose substituents. With this in mind, reaction mechanisms similar to those found in esculin oligomerization [15] could be assumed.…”

Section: Maldi-tof Analysismentioning

confidence: 99%

“…However, both its low solubility in aqueous and non-toxic organic solvents, which imply scarce bioavailability, and poor thermal stability [9][10][11], restrict its application. Enzymatic polymerization of polyphenolic monomers has been shown to produce higher molecular weight polyphenols with improved solubility, thermostability, and superior antioxidant properties [12][13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

“…The main advantage of laccase compared to peroxidases is that it requires oxygen as a final electron acceptor rather than hydrogen peroxide [18]. Laccases have been used in the food, pharmaceutical, and cosmetics sectors and have proved their usefulness as catalysts for the oligomerization or polymerization of phenolic compounds [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

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Laccase Activity as an Essential Factor in the Oligomerization of Rutin

et al. 2018

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The enzyme-mediated polymerization of bioactive phenolic compounds, such as the flavonoid rutin, has gained interest due to the enhanced physico-chemical and biological properties of the products, which increases their potential application as a nutraceutical. In this work, the influence of enzyme activity on rutin oligomerization was evaluated in reactions with low (1000 U/L) and high (10,000 U/L) initial laccase activities. For both reactions, high molecular weight oligomer fractions showed better properties compared to lower weight oligomers. Products of the reaction with low laccase activity exhibited thermal stability and antioxidant potential similar to control reaction, but led to higher inhibitory activity of xanthine oxidase and apparent aqueous solubility. Oligomers obtained in the reaction with high laccase activity showed better apparent aqueous solubility but decreased biological activities and stability. Their low antioxidant activity was correlated with a decreased phenolic content, which could be attributed to the formation of several bonds between rutin molecules.

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Section: Polymerization Reactionsupporting

confidence: 91%

Section: Polymerization Reactionmentioning

confidence: 99%

Section: Maldi-tof Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Laccase Activity as an Essential Factor in the Oligomerization of Rutin

et al. 2018

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Bundling the removal of emerging contaminants with the production of ligninolytic enzymes from residual streams

González-Rodríguez

Lú-Chau

Trueba-Santiso

et al. 2022

Appl Microbiol Biotechnol

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Enzymes offer interesting features as biological catalysts for industry: high specificity, activity under mild conditions, accessibility, and environmental friendliness. Being able to produce enzymes in large quantities and having them available in a stable and reusable form reduces the production costs of any enzyme-based process. Agricultural residues have recently demonstrated their potential as substrates to produce ligninolytic enzymes by different white rot fungi. In this study, the biotechnological production of a manganese peroxidase (MnP) by Irpex lacteus was conducted through solid-state fermentation (SSF) with wheat straw as substrate and submerged fermentation (SmF) employing wheat straw extract (WSE). The obtained enzyme cocktail also showed manganese-independent activity (MiP), related to the presence of a short MnP and a dye-decolorizing peroxidase (DyP) which was confirmed by shotgun proteomic analyses. In view of the enhanced production of ligninolytic enzymes in SmF, different parameters such as WSE concentration and nitrogen source were evaluated. The highest enzyme titers were obtained with a medium formulated with glucose and peptone (339 U/L MnP and 15 U/L MiP). The scale-up to a 30 L reactor achieved similar activities, demonstrating the feasibility of enzyme production from the residual substrate at different production scales. Degradation of five emerging pollutants was performed to demonstrate the high oxidative capacity of the enzyme. Complete removal of hormones and bisphenol A was achieved in less than 1 h, whereas almost 30% degradation of carbamazepine was achieved in 24 h, which is a significant improvement compared to previous enzymatic treatments of this compound. Key points • Wheat straw extract is suitable for the growth of I. lacteus. • The enzyme cocktail obtained allows the degradation of emerging contaminants. • Mn-dependent and Mn-independent activities increases the catalytic potential. Graphical abstract

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Bioremediation of phenolic pollutant bisphenol A using optimized reverse micelles system of Trametes versicolor laccase in non-aqueous environment

Trivedi¹,

Chhaya²

2021

3 Biotech

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Comprehensive investigation of the enzymatic oligomerization of esculin by laccase in ethanol : water mixtures

Abstract: The oligomerization of esculin by laccase in aqueous medium resulted in a precipitate fraction with excellent antioxidant properties.

Cited by 24 publications

References 31 publications

Laccase Activity as an Essential Factor in the Oligomerization of Rutin

Laccase Activity as an Essential Factor in the Oligomerization of Rutin

Bundling the removal of emerging contaminants with the production of ligninolytic enzymes from residual streams

Bioremediation of phenolic pollutant bisphenol A using optimized reverse micelles system of Trametes versicolor laccase in non-aqueous environment

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