Hyperactivation and thermostabilization of Phanerochaete chrysosporium lignin peroxidase by immobilization in xerogels

Asgher, Muhammad; Asad, Muhammad Javaid; Bhatti, Haq Nawaz; Legge, Raymond L.

doi:10.1007/s11274-006-9255-9

Cited by 24 publications

(14 citation statements)

References 27 publications

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“…Previously, we [16] reported that entrapment of lignin peroxidase (LiP) from P . chrysosporium in Sol-gels caused hyper-activation but an increase in hydrophobic character above certain optimum limits caused a decrease in LiP activity.…”

Section: Resultsmentioning

confidence: 99%

“…In spite of the existing physical/chemical technologies that are usually expensive and commercially or environmentally unattractive, biological processes seem as potential alternatives because they are cost effective, eco-friendly and can be applied to wide range of dye containing industrial effluents. WRF have the ability to degrade contaminants by virtue of its extracellular ligninolytic enzymes including lignin peroxidases (LiPs), manganese peroxidases (MnPs) and laccases [6,13-16]. Therefore, over the past several years, there has been great interest among researchers in the production of ligninolytic enzymes using various agro-based waste materials [5].…”

Section: Introductionmentioning

confidence: 99%

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Improvement of Catalytic Efficiency, Thermo-stability and Dye Decolorization Capability of Pleurotus ostreatusIBL-02 laccase by Hydrophobic Sol Gel Entrapment

Asgher

Kamal

Iqbal

2012

Chemistry Central Journal

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BackgroundIn serious consideration of the worldwide environmental issues associated with the extensive use of the textile dyes and effluents generated thereof, the scientists across the world are in search for potential treatment technologies for their treatment. In such scenario the ligninolytic enzymes provide a potential alternative because they are cost effective, eco-friendly and can be applied to wide range of dye containing industrial effluents.ResultsLaccase produced from Pleurotus ostreatus IBL-02 during decolorization of the reactive textile dye Drimarene brilliant red K-4BL (DBR K-4BL) was purified and immobilized by hydrophobic gel entrapment. The crude laccase was 4.2-fold purified with specific activity of 573.52 U/mg after passing through the DEAE-Sepharose ion exchange and Sephadex-G-100 chromatography columns. P. ostreatus IBL-02 laccase was found to be a homogenous monomeric protein as evident by single band corresponding to 67 kDa on native and sodium dodesylsulfate polyacrylamide gel electrophoresis (PAGE). The laccase was immobilized by entrapment in Sol–gel matrix of trimethoxysilane (T) and proplytetramethoxysilane (P) prepared using different T:P molar ratios. The free and immobilized laccases were compared to investigate the effect of immobilization on catalytic efficiency and thermo-stability features. Laccase immobilized in the Sol–gel of 1:5 T:P ratio was optimally active and thermo-stable fraction at pH 5, 60°C with half-life of 3 h and 50 min. Laccases immobilized in 1:2 and 1:5 T:P ratio gels had significantly higher Km (83 and100mM) and Vmax (1000 and 1111 mM/mg) values as compared to free laccase. After 5 h reaction time varying decolorization percentages with a maximum of 100% were achieved for different dyes and effluents.ConclusionsIn summary, P. ostreatus IBL-02 laccase was immobilized by entrapping in a Sol–gel matrix with an objective to enhance its catalytic and stability properties. Sol–gel entrapped laccase presented potential efficiency as a biocatalyst when applied for decolorization of different dyes and effluents. The main benefits of the Sol–gel matrix immobilization processes are the eco-friendly approach, chemical free and energy saving reaction conditions.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Improvement of Catalytic Efficiency, Thermo-stability and Dye Decolorization Capability of Pleurotus ostreatusIBL-02 laccase by Hydrophobic Sol Gel Entrapment

Asgher

Kamal

Iqbal

2012

Chemistry Central Journal

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“…Asgher et al entrapped LiP from P. chrysosporium in a Si(OMe) 4 /nPrSi(OMe) 3 xerogel. 83 The immobilised enzyme appeared to be more active than the soluble enzyme, judged by the conversion of VA. The background is a decrease of K M (from 13 to 10.6 mg ml À1 ) and an increase of V max (from 11.8 to 16.7 mmol min À1 ).…”

Section: Reactions Of Lignin Peroxidase With Lignin Building Blocksmentioning

confidence: 92%

“…Within the scope of this review, two lignin peroxidases were successfully immobilised in a xerogel made of Si(OMe) 4 /nPrSi(OMe) 3 . 83,84 Different enzymes can be co-immobilised on one matrix, for making enzyme cascades, removing deleterious side products or ensuring slow production of substrate. The latter reason was the background for the research by Qiu et al, 85 who co-immobilised glucose oxidase with lignin peroxidase.…”

Section: Entrapmentmentioning

confidence: 99%

Immobilised enzymes in biorenewables production

et al. 2013

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Oils, fats, carbohydrates, lignin, and amino acids are all important raw materials for the production of biorenewables. These compounds already play an important role in everyday life in the form of wood, fabrics, starch, paper and rubber. Enzymatic reactions do, in principle, allow the transformation of these raw materials into biorenewables under mild and sustainable conditions. There are a few examples of processes using immobilised enzymes that are already applied on an industrial scale, such as the production of High-Fructose Corn Syrup, but these are still rather rare. Fortunately, there is a rapid expansion in the research efforts that try to improve this, driven by a combination of economic and ecological reasons. This review focusses on those efforts, by looking at attempts to use fatty acids, carbohydrates, proteins and lignin (and their building blocks), as substrates in the synthesis of biorenewables using immobilised enzymes. Therefore, many examples (390 references) from the recent literature are discussed, in which we look both at the specific reactions as well as to the methods of immobilisation of the enzymes, as the latter are shown to be a crucial factor with respect to stability and reuse. The applications of the renewables produced in this way range from building blocks for the pharmaceutical and polymer industry, transport fuels, to additives for the food industry. A critical evaluation of the relevant factors that need to be improved for large-scale use of these examples is presented in the outlook of this review.

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“…xerogels, ambigels, aquagels, or aerogels) with additives to create hydrophilic or hydrophobic surfaces are commonly used [62]. When xerogels of high density entrap one or more enzymes by hydrolytic polymerization, the substrate selectivity of the extremely small pores can be particularly useful for the development of biosensors [63,64]. Entrapment matrices with hydrophobic surfaces can activate lipases, the most used enzymes in synthetic organic chemistry [65].…”

Section: Entrapment and Encapsulationmentioning

confidence: 99%

Biocatalysis and Strategies for Enzyme Improvement

Osbon¹,

Kumar²

2020

Biophysical Chemistry - Advance Applications

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Biotransformation with the help of enzymes can greatly improve the rate and stereospecificity of reactions in organic chemistry. However, the use of organic solvents and harsh conditions in biotechnological applications often correlates with enzyme deactivation or a dramatic drop in catalytic activity. Detailed molecular understanding of the protein structure and conformational dynamics allows us to address such limitations and to finely tune catalytic activity by modifying the solvent, the support, or the active site of the enzyme. Along with physico-chemical methods of enzyme stabilization, such as additive approach, chemical modification, and immobilization of enzymes, approaches of enzyme engineering based on DNA recombination can be used to enhance the performance of biocatalysts. Since successful synthetic and industrial applications of biocatalysts require systems that are not only stable and active, but can also be reused in a continuous flow process reducing the production cost, the goal of this chapter is to introduce the reader to the vast scope of techniques available for enzyme improvement, highlighting their opportunities and limitations for the real-world technological processes.

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Hyperactivation and thermostabilization of Phanerochaete chrysosporium lignin peroxidase by immobilization in xerogels

Cited by 24 publications

References 27 publications

Improvement of Catalytic Efficiency, Thermo-stability and Dye Decolorization Capability of Pleurotus ostreatusIBL-02 laccase by Hydrophobic Sol Gel Entrapment

Improvement of Catalytic Efficiency, Thermo-stability and Dye Decolorization Capability of Pleurotus ostreatusIBL-02 laccase by Hydrophobic Sol Gel Entrapment

Immobilised enzymes in biorenewables production

Biocatalysis and Strategies for Enzyme Improvement

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