Optimization of Laccase Fermentation and Evaluation of Kinetic and Thermodynamic Parameters of a Partially Purified Laccase Produced by<i>Daedalea flavida</i>

Singha, Siddhartha; Panda, T.

doi:10.1080/10826068.2014.887581

Cited by 8 publications

(3 citation statements)

References 47 publications

(53 reference statements)

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“…This indicates that a lower level of energy is required to break down the enzyme's stability, and that the destabilization of enzyme bonds is easier to achieve [58]. The negative values of ∆S* has also been reported in other studies for different enzymes, such as laccase from D. flavida, lipase from B. cepacian, and palatase from R. miehei [59,60]. It has also been suggested that negative values correlated more with an unfolded transition state in contrast to a ground-state native structure [59].…”

Section: Thermodynamicssupporting

confidence: 72%

Laccase and Biomass Production via Submerged Cultivation of Pleurotus ostreatus Using Wine Lees

Bakratsas,

Antoniadis,

Athanasiou

et al. 2023

Biomass

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Large quantities of wine lees are produced annually by the wine industry. The high phenolic content makes them unsuitable for disposal in the environment or animal feed without a suitable treatment. In this study, wine lees were treated by Pleurotus ostreatus in submerged cultivation, producing a high-value biomass and elevated levels of laccase, an important industrial enzyme. Biomass and laccase production reached 21 g/L and 74,000 Units/L, respectively, at the optimal conditions of initial pH 6.0, 20% v/v wine lees, 30 g/L glucose, and 20 g/L yeast extract, while decolorization and dephenolization rates of the waste were over 90%. The mycelial biomass was rich in proteins and essential amino acids reaching up to 43% and 16% per dry weight, respectively. Carbohydrates and lipids were the second richest bioactive compound in biomass, with values of 29.4 ± 2.7% and 29.5 ± 2.7%, respectively. The crude laccase in the culture supernatant was purified via a simple two-step purification procedure by 4.4-fold with a recovery of 44%. The molecular weight of the enzyme was determined to be 62 kDa via SDS electrophoresis. Enzyme activity was optimal at pH 5.0 and 70 °C. The activation energy of the enzyme was calculated at a value of 20.0 ± 0.2 kJ/mol. The pH stability and thermostability of the purified laccase were studied. The enzyme was remarkably stable at pH 8.0 and at temperatures up to 40 °C. The thermal inactivation energy of the enzyme was determined to be 76.0 ± 1.2 kJ/mol. The thermodynamic parameters (ΔH*, ΔG*, and ΔS*) for the thermal deactivation of the purified laccase at a temperature range of 20–60 °C were: 73.8 ≤ ΔH* ≤ 74.3 kJ·mol−1, 98.7 ≤ ΔG* ≤ 101.9 kJ·mol−1, and −90.5 ≤ ΔS* ≤ −84.3 J·mol−1·K−1. Wine lees could be ideal substrates of fungal cultivation for laccase production and biomass with a high protein content in an eco-friendlier way.

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Section: Thermodynamicssupporting

confidence: 72%

Laccase and Biomass Production via Submerged Cultivation of Pleurotus ostreatus Using Wine Lees

Bakratsas,

Antoniadis,

Athanasiou

et al. 2023

Biomass

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“…As a rule of thumb, a process of isolation and purification or at least partially enzyme purification [7] should be done before proceeding with detailed structure-function characterization including determination of kinetic parameters. More than one chromatographic step is usually performed during purification procedures in order to obtain an enzymeenriched preparation free of other proteins or contaminant compounds such as inhibitors.…”

Section: Introductionmentioning

confidence: 99%

An Easy Method for Screening and Detection of Laccase Activity

Dias¹,

Matos²,

Fraga³

et al. 2017

TOBIOTJ

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Objective: An instrument-free assay was developed for simultaneous detection of laccase activity in a large number of samples as diverse as screening of laccase-producing microbial cultures or chromatographic fractions. Method: Dried paper discs previously impregnated with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) were placed on a flat-bottom microplate (a simple way to avoid misidentification) and loaded with an aliquot from each sample. Results: Discs corresponding to samples containing laccase activity become green-bluish colored within first ten minutes of reaction, allowing direct detection through simple naked-eye inspection. Conclusion: As an example, this easy process was applied to the laccase purification in order to eliminate chromatographic fractions that did not contain laccase activity, thus reducing the number of spectrophotometric assays.

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“…Despite the high demand for laccase, enzyme production is limited due to its long fermentation period and the low yield by fungal cultures . In order to meet the high demand for low‐cost laccase, different strategies have been developed to improve laccase production, such as the utilization of different inducers , the optimization of fermentation conditions and media , and the isolation and breeding of new strains . Although there are many methods to reduce the cost and improve the production of laccase, these methods are still unable to meet the demand for industrial applications.…”

Section: Introductionmentioning

confidence: 99%

Farnesol stimulates laccase production in Trametes versicolor

Wang

et al. 2016

Engineering in Life Sciences

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Farnesol, a quorum-sensing molecule, was used successfully to improve laccase production in submerged cultures of Trametes versicolor. At the optimal farnesol concentration of 60 μM added at the beginning of the culture, the extracellular laccase activity reached 629.3 U L −1 after 6 days of cultivation, which represented a 1.92-fold increase relative to the control without farnesol treatment. The addition of farnesol resulted in an increase in the accumulation of H 2 O 2 and an increased expression of the laccase (lac) gene and the RhoA gene. The RhoA gene correlated with hyperbranched mycelia, which facilitated the secretion of the intracellular laccase. This study provides a basis for understanding the induction mechanism of farnesol for enhancing laccase production.

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Optimization of Laccase Fermentation and Evaluation of Kinetic and Thermodynamic Parameters of a Partially Purified Laccase Produced byDaedalea flavida

Cited by 8 publications

References 47 publications

Laccase and Biomass Production via Submerged Cultivation of Pleurotus ostreatus Using Wine Lees

Laccase and Biomass Production via Submerged Cultivation of Pleurotus ostreatus Using Wine Lees

An Easy Method for Screening and Detection of Laccase Activity

Farnesol stimulates laccase production in Trametes versicolor

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