Immobilization of lignin peroxidase from Alcaligenes aquatilis and its application in dye decolorization (original) (raw)
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Bioresources, 2019
Lignin peroxidase (LiP), which has been studied extensively in white-rot Basidiomycetes with regard to bio-pulping and bio-bleaching, plays a role in the biodegradation of plant cell wall lignin. In the current study, LiP obtained from a wild isolate of Phanerochaete chrysosporium immobilized on polyurethane foam cubes was purified 21-fold using ammonium sulphate precipitation and size exclusion chromatography. The enzyme with a molecular mass of 55 kDa exhibited a considerably higher pH tolerance and thermostability compared with the native enzyme. It showed a strong affinity for the substrate veratryl alcohol and had kinetic constant values of 142.86 µmol and 65 µM. Cysteine, sodium azide, mercaptoethanol, and silver nitrate inhibited the activity, while ethanol, EDTA, Cu2+, Mn+, Na+, and Fe2+ exhibited induction. Purified LiP completely decolorized (100%) bromo phenyl blue, bromothymol blue, and bromocresol green. The 96 and 72% degradation obtained with phenol and congo red was ...
Investigation into the kinetic properties of immobilized lignin peroxidases
Journal of Biotechnology, 1994
Mixtures of lignin peroxidase isozymes were immobilized onto controlled-pore glass (CPG) beads through three different functional groups (free amino groups, free carboxylate groups, or the aldehyde groups of the metaperiodate-oxidized carbohydrate portions of the proteins) and catalytic properties of the immobilized proteins were determined. Some loss of activity occurred in all immobilized samples, but relatively high activities were maintained with enzymes immobilized via the modified carbohydrate moieties. The effectiveness of using the immobilized enzymes to treat anthracene and pulp mill bleach plant effluent was tested. Bleach plant effluent precipitated onto the aminopropyl-CPG beads inactivating the enzymes, probably due to reactions with free amino groups. In contrast, anthracene was rapidly and completely degraded by the immobilized lignin peroxidases.
Industrial dye decolorizing lignin peroxidase from Kocuria rosea MTCC 1532
Annals of Microbiology, 2012
Lignin peroxidase (LiP) enzyme was purified from Kocuria rosea MTCC 1532. The enzyme was produced and subjected to purification by ion exchange chromatography followed by gel filtration chromatography; 79-fold purity was obtained. The molecular weight of LiP was determined to be 66 kDa. The pH optimum of the purified enzyme was 3.0, and the temperature optimum was found to be around 50°C. Purified LiP showed a much higher activity towards n-propanol than towards L-Dopa, 8-hydroquinone, mimosine, veratryl alcohol, and xylidine. The effect of inhibitor and metal ion on LiP activity was analyzed. Purified LiP was able to decolorize synthetic dyes from various groups, indicating that it is a versatile peroxidase.
Decolorization of synthetic textile dyes by lignin peroxidase of Phanerochaete chrysosporium
Folia Microbiologica, 2002
Neem hull waste (containing a high amount of lignin and other phenolic compounds) was used for lignin peroxidase production byPhanerochaete chrysosporum under solid-state fermentation conditions. Maximum decolorization achieved by partially purified lignin peroxidase was 80% for Porocion Brilliant Blue HGR, 83 for Ranocid Fast Blue, 70 for Acid Red 119 and 61 for Navidol Fast Black MSRL. The effects of different concentrations of veratryl alcohol, hydrogen peroxide, enzyme and dye on the efficiency of decolorization have been investigated. Maximum decolorization efficiency was observed at 0.2 and 0.4 mmol/L hydrogen peroxide, 2.5 mmol/L veratryl alcohol and pH 5.0 after a 1-h reaction, using 50 ppm of dyes and 9.96 mkat/L of enzyme.
Saudi Journal of Biological Sciences, 2016
The majority of the textile dyes are harmful to the environment and potentially carcinogenic. Among strategies for their exclusion, the treatment of dye contaminated wastewater with fungal extract, containing lignin peroxidase (LiP), may be useful. Two fungi isolates, Pleurotus ostreatus (PLO9) and Ganoderma lucidum (GRM117), produced the enzymatic extract by fermentation in the lignocellulosic residue, Jatropha curcas seed cake. The extracts from PLO9 and GRM117 were immobilized on carbon nanotubes and showed an increase of 18 and 27-fold of LiP specific activity compared to the free enzyme. Also, LiP from both fungi extracts showed higher Vmax and lower Km values. Only the immobilized extracts could be efficiently reused in the dye decolourization, contrary, the carbon nanotubes became saturated and they should be discarded over time. This device may offer a final biocatalyst with higher catalytic efficiency and capability to be reused in the dye decolourization process.
Journal of Chemical Technology and Biotechnology, 2009
BACKGROUND: The present work aims to study the production of lignin peroxidase (LiP) enzyme by Comamonas sp UVS using various media, and lignocellulosic waste materials, and its effect on decolorization of Direct Blue GLL (DBGLL).RESULTS: Yeast extract medium was found to be more effective for the production of LiP and also for the decolorization of DBGLL. The bagasse powder along with yeast extract induced LiP activity. Comamonas sp UVS decolorized DBGLL dye (50 mg L−1) within 13 h at static condition in YE broth. It could degrade up to 300 mg L−1 of dye within 55 h. The maximum rate (Vmax) of decolorization was 12.41 ± 0.55 mg dye g cell−1 h−1 with the Michaelis constant (Km) value as 6.20 ± 0.27 mg L−1. The biodegradation was monitored by UV-Vis, GC-MS and HPLC.CONCLUSION: The use of agricultural by-products for the activity enhancement of the ligninolytic enzymes is a cost effective process. It also resolves the problem of the disposal of agro-residues. This system can be applied for the degradation of different recalcitrant compounds. Copyright © 2008 Society of Chemical Industry
Advances in Bioresearch, 2020
Today with growing textile industry, the major problem which India is facing is to remove dye from effluent before discharge in the water bodies. In the present study, Lignin peroxidase (Lip) enzyme producing microbial strain FSV 3was studied for decolorization and detoxification of various synthetic dye like Congo red, Methyl orange, Methylene blue and Remazol brillent blue R. From the study, it was found that FSV 3 strain is able to decolorize and detoxify methylene blue and Remazol brillent blue R upto 100mg/L by 44 and 77% respectively on 144 hours of study, while for congo red and methylene orange show bioabsorption of dye.
BMC Biotechnology, 2012
Background Cost-effective production of industrially important enzymes is a key for their successful exploitation on industrial scale. Keeping in view the extensive industrial applications of lignin peroxidase (LiP), this study was performed to purify and characterize the LiP from an indigenous strain of Trametes versicolor IBL-04. Xerogel matrix enzyme immobilization technique was applied to improve the kinetic and thermo-stability characteristics of LiP to fulfil the requirements of the modern enzyme consumer sector of biotechnology. Results A novel LiP was isolated from an indigenous T. versicolor IBL-04 strain. T. versicolor IBL-04 was cultured in solid state fermentation (SSF) medium of corn cobs and maximum LiP activity of 592 ± 6 U/mL was recorded after five days of incubation under optimum culture conditions. The crude LiP was 3.3-fold purified with specific activity of 553 U/mg after passing through the DEAE-cellulose and Sephadex-G-100 chromatography columns. The purified ...
International journal of pharma and bio sciences, 2016
Active laccase and LiP fractions purified from Phanerochaete chrysosporium broth cultures designed for degradation of phenols in sewage samples were immobilized by entrapping in Sol-Gel matrix of trimethoxysilane (TMOS) and propyltetramethoxysilane (PTMS). A maximum of 90.7% and 92.3% of immobilization efficiencies were achieved with a 2 mg/mL pure laccase and pure LiP each. Immobilized laccase and LiP retained 80% and 84% of their activities at pH 4.5 and 5.5 respectively compared to free enzymes. The capacity of the enzyme laccase to withstand the effect of inhibitors (cystein, EDTA, and Ag+) was also enhanced by up to 80% by immobilization. Immobilized Laccase was active in the reaction mixture for three hours, but degraded only 45% of the phenol in one hour whereas immobilized LiP which remained active for one and half hour degraded 95% of phenol in the stipulated one hour time. When immobilized laccase was treated with divalent metal ions Ca ++ and Cu ++ it worked faster equal ...