Sequential batch reactor for eucalypt kraft pulp effluent treatment with <i>Trametes versicolor</i>

Xavier, Ana M. R. B.; Tavares, Ana P. M.; Agapito, M S M; Evtuguin, Dmitry V.

doi:10.1002/jctb.1954

Cited by 5 publications

(5 citation statements)

References 21 publications

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“…With improved pH stability and thermal stability, laccase from the mutant S152 would be more suitable for biotechnological and environmental applications, such as decoloration of waste water from textile (under neutral or alkaline pH conditions), pulp delignification, and biotransformation [3,5]. …”

Section: Effect Of Ph and Temperature On Enzyme Stabilitymentioning

confidence: 99%

“…Their wide substrates spectrum allows laccases to be extensively used in various areas such as pulp delignification, dye decoloration, environmental pollutant detoxification, biopolymer modification, biotransformation, and food dechlorination [1,[3][4][5][6][7]. However, industrial applications of laccases are usually hindered by their long fermentation period, low laccase yield, as well as poor enzyme stability.…”

Section: Introductionmentioning

confidence: 99%

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Improvement of laccase production and its properties by low-energy ion implantation

Liu

Zhang

Hua

et al. 2009

Bioprocess Biosyst Eng

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Low-energy ion implantation was employed to breed laccase producing strain Paecilomyces sp. WSH-L07 and a mutant S152 that exhibited an activity of more than three times over the wild strain was obtained. The optimum substrate of both the wild and mutant laccases was 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate), and followed by guaiacol with optimal pH at 3.4 and 5.0, respectively, while the mutant laccase exhibited a broader active pH range. The mutant laccase had a higher optimal catalytic temperature (60-65 degrees C) than the wild one (55 degrees C), and the wild laccase deactivated rapidly when temperature increased above 55 degrees C. Furthermore, the mutant laccase was more stable under neutral and alkaline conditions. A thermostability experiment revealed that the mutant laccase was superior to the wild laccase. Both laccases were stable in the presence of metal ions, mildly inhibited by SDS (0.5 mM), EDTA (1 mM) and 1,4-dithiothreitol (0.5 mM), and almost completely inhibited by 0.1 mM NaN(3).

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Section: Effect Of Ph and Temperature On Enzyme Stabilitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Improvement of laccase production and its properties by low-energy ion implantation

Liu

Zhang

Hua

et al. 2009

Bioprocess Biosyst Eng

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“…Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are multicopper oxidase enzymes, being characterized by high activity and remarkable ability to oxidize a wide range of substrates, including phenolic compounds [1][2][3]. Due to these advantageous properties, numerous potential industrial applications have been reported [4] for such enzymes, like dye decolourization [5][6][7], pulp delignification [8,9], soil bioremediation [2,10], and detection of specific analytes [10].…”

Section: Introductionmentioning

confidence: 99%

Bacterial cellulose as carrier for immobilization of laccase: Optimization and characterization

Frazão

Silva

Freire

et al. 2014

Engineering in Life Sciences

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Bacterial cellulose (BC) has attracted attention as a new functional material due to its excellent mechanical strength, tridimensional nanostructure, high purity, and increased water absorption, compared to plant cellulose. In this work, commercial laccase was immobilized on BC and the influence of enzyme concentration, contact time, and pH was optimized toward the recovery activity of immobilized laccase. This optimization was carried out using a 33 experimental design and response surface methodology. Enzyme concentration played a critical role in laccase immobilization. Under optimized conditions (0.15 μL L−1 of enzyme concentration, 4.8 h of contact time, pH 5.4), the predicted and experimental response were equal to 47.88 and 49.30%, respectively. The thermal stability of the immobilized laccase was found to increase notably at 60 and 70°C presenting stabilization factor equal to 1.79 and 2.11, respectively. The immobilized laccase showed high operational stability, since it retained 86% of its initial activity after seven consecutive biocatalytic cycles of reaction with 2,2′‐azinobis‐(3‐ethylbenzothiazoline‐6‐sulfonic acid). Kinetic studies showed that the values of Michaelis–Menten constant and maximum reaction rate decreased upon immobilization (9.9‐ and 1.6‐fold, respectively). Globally, the use of immobilized laccase on BC offers an interesting tool for industrial biocatalytic applications.

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“…When other substrates are not available, the role of these enzymes on woods is the delignification of hemicelluloses by oxidative reactions in order to ensure survival of these carbon staffs. The biocatalytic potential of T. versicolor has been studied for different industrial applications such as bleaching of Kraft pulps [17,18], effluents decolorization and biotreatment [19] and also to find out oxidation mechanisms with lignin models [20,21]. This fungus is also reported to be a medicinal fungus producing an exopolysaccharide with antitumor activity when it is grown in specific experimental conditions [22].…”

Section: Introductionmentioning

confidence: 99%

Image Analysis Technique as a Tool to Identify Morphological Changes in Trametes versicolor Pellets According to Exopolysaccharide or Laccase Production

Tavares

Silva

Amaral

et al. 2013

Appl Biochem Biotechnol

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Image analysis technique was applied to identify morphological changes of pellets from white-rot fungus Trametes versicolor on agitated submerged cultures during the production of exopolysaccharide (EPS) or ligninolytic enzymes. Batch tests with four different experimental conditions were carried out. Two different culture media were used, namely yeast medium or Trametes defined medium and the addition of lignolytic inducers as xylidine or pulp and paper industrial effluent were evaluated. Laccase activity, EPS production, and final biomass contents were determined for batch assays and the pellets morphology was assessed by image analysis techniques. The obtained data allowed establishing the choice of the metabolic pathways according to the experimental conditions, either for laccase enzymatic production in the Trametes defined medium, or for EPS production in the rich Yeast Medium experiments. Furthermore, the image processing and analysis methodology allowed for a better comprehension of the physiological phenomena with respect to the corresponding pellets morphological stages.

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Sequential batch reactor for eucalypt kraft pulp effluent treatment with Trametes versicolor

Cited by 5 publications

References 21 publications

Improvement of laccase production and its properties by low-energy ion implantation

Improvement of laccase production and its properties by low-energy ion implantation

Bacterial cellulose as carrier for immobilization of laccase: Optimization and characterization

Image Analysis Technique as a Tool to Identify Morphological Changes in Trametes versicolor Pellets According to Exopolysaccharide or Laccase Production

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