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Search Results: 1 - 10 of 223804 matches for " R Sarnthima "
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Laccase isozymes of Pleurotus sajor-caju culture on husk and bran of black sticky rice and their potential on indigo carmine decolourisation
R Sarnthima, S Khammuang
African Journal of Biotechnology , 2008,
Abstract: Extracellular laccases of Pleurotus sajor-caju grown on solid state medium consisted of husk and bran of black sticky rice, were partially purified by DEAE–cellulose chromatography. These laccases could be separated into three groups: unboundLac and bound fractions (pool1Lac and pool2Lac). The optimum pH of these laccases was studied using ABTS as substrate. It was found that the pH optimum for unboundLac fell in the range of 3–5 and 3–4 for pool1Lac and pool2Lac. The indigo carmine decolourisation capacity was compared between unboundLac and pool2Lac. It was found that the optimal pH for indigo carmine decolourisation were 5 and 3 for unboundLac and pool2Lac, respectively. In the range of various dye concentrations tested, it was found that indigo carmine at 10 ìM with the enzyme activity of 0.01 U, gave the best dye decolourisation with 40.47% within 120 min for unboundLac and with 18.61% within 150 min for pool2Lac. High amount of enzyme used of these laccases might improve decolourisation ability.
Evaluation of Dyes Decolourisation by the Crude Enzyme from Pleurotus sajor-caju Grown on Sorghum Seed Media
R. Sarnthima,S. Khammuang
Pakistan Journal of Biological Sciences , 2008,
Abstract: The extracellular enzymes from Pleurotus sajor-caju were studied for lignin degrading enzyme patterns and dye decolourisation potential. Laccases are major ligninolytic enzymes excreted by the fungus. The results from a native-PAGE revealed that there were at least two isoenzymes. The crude enzyme had a pH and a temperature optimum at 6.0 and 40°C, respectively when 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) was used as substrate. The pH and thermal stability were at 5.0 and 30°C. The pH optima for decolourisation of Indigo Carmine and Methyl Red were at 5.0 and 6.0, respectively. Indigo Carmine could be decolorized efficiently above 90% within 180 min, whereas Methyl Red could be decolorized only 3.5%. High efficiency decolourisation of Indigo Carmine makes this fungus to be a promise choice in biological treatment of waste water containing Indigo Carmine.
Mediator-Assisted Rhodamine B Decolorization by Tramates versicolor Laccase
S. Khammuang,R. Sarnthima
Pakistan Journal of Biological Sciences , 2009,
Abstract: This study reported the decolorization of hazardous xanthenes dye, Rhodamine B by the Laccase Mediator System (LMS). Seven redox mediators were investigated in the mediators-assisted lacase catalyze oxidation reactions. Among redox mediators tested, 2, 2’-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) was the best one which gave the highest Rhodamine B decolorization for more than 80% within 48 h while only 20% achieved with no mediator added. In the laccase-ABTS mediator system, the best molar ratio of dye/mediator was 1:10 and dye/enzyme ratio was 0.5 μmol U-1. The optimum conditions for Rhodamine B decolorization were at pH 4.0-5.0 and temperature 35-40°C. The laccase-ABTS system could be a promising biotechnology developed for treatment of textile waste waters containing Rhodamine B.
Laccase-Aided Antioxidant Activity Assay and Antioxidant Activity of Selected Thai Vegetables
S. Khammuang,R. Sarnthima
Journal of Applied Sciences , 2008,
Abstract: This study aimed to develop the enzymatic preparation of ABTS-+ radical cation using laccase from Trametes versicolor. The result revealed that ABTS-+ preparation with the aid of the enzyme was reasonable easy, quick and high yield. The radical yields were controlled by concentration of ABTS substrate and enzyme amount. These ABTS-+ radicals were used for antioxidant activity assay of 31 Thai vegetables. The dried sample powders extracted by ethyl alcohol showed as high TEAC values as in Spondias pinnata, Eugenia grata and Polygonum odoratum. TEAC values determined using ABTS-+ and DPPH- radical decolourisation methods were strongly consistency and correlate with total phenolic content in the samples. The quick and easy of the method as well as stability of the radical and reliable of the antioxidant capacity including environmental friendly suggest it to be a potential method for a total antioxidant activity measurement in biological samples.
Antioxidant Activity of Crude Polysaccharides from Edible Fresh and Dry Mushroom Fruiting Bodies of Lentinus sp. Strain RJ-2
C. Thetsrimuang,S. Khammuang,R. Sarnthima
International Journal of Pharmacology , 2011,
Abstract: Crude polysaccharides of mature fresh (FB) and dried fruiting bodies (DB) of the edible mushroom, Lentinus sp. strain RJ-2 were evaluated for their antioxidant properties. The crude polysaccharides yields in FB and DB were 115.84 and 93.66 mg g-1 dry weight mushroom, respectively. Trolox equivalent values in scavenging abilities of both crude polysaccharides against both 2, 2'-azino-bis-(3-ethylbenzthiazoline-6-sulphonic acid (ABTS) radical and 1, 1-diphenyl-2-picrylhydrazyl (DPPH) radicals as well as reducing properties were in similar ranges. The crude polysaccharides contained protein, reducing sugar and phenol compounds. The results from Fourier transform infrared (FTIR) spectroscopy and Thin Layer Chromatography (TLC) suggested that the crude polysaccharide contained a monosaccharide with six carbon atoms in a pyranose ring and mannose are proposed to be the majority. This study suggested that the crude polysaccharides from Lentinus sp. mushrooms could potentially be used as natural antioxidants.
Copper-Alginate Encapsulation of Crude laccase from Lentinus polychrous Lev. and their Effectiveness in Synthetic Dyes Decolorizations
J. Phetsom,S. Khammuang,P. Suwannawong,R. Sarnthima
Journal of Biological Sciences , 2009,
Abstract: Crude laccase from Lentinus polychrous Lev. was entrapped in alginate beads for application in decolorization of synthetic dyes. The percentages of alginate, types and concentrations of bivalent cations (Cu2+, Zn2+, Ca2+) influenced on immobilized enzyme activity as well as immobilized yield. The sensitivity of the immobilized Cu-alginate enzyme towards pH change was lowest when compared to the immobilized enzymes of other bivalent cations including free enzyme. By using ABTS substrate, the optimum temperature of the Ca-, Cu- and Zn-alginate enzymes were 60, 55 and 55°C, respectively while the optimum temperature of the free enzyme was 50°C. The Cu- and Zn-alginate enzymes were well stabilized for a week in all tested pH values except for pH 8.0 (0.1 M Tris-HCl). The Cu- and Zn-alginate enzymes revealed better temperature stability than the Ca-alginate and the free enzymes. Decolorizations of four structurally different synthetic dyes by the immobilized Cu-alginate enzymes in a continuous pack-bed approach were reported. The Cu-alginate enzymes were being able to repeated use effectively more than two times in dye removal experiments.
Laccase from Spent Mushroom Compost of Lentinus polychrous Lev. And its Potential for Remazol Brilliant Blue R Decolourisation
Saranyu Khammuang,Rakrudee Sarnthima
Biotechnology , 2007,
Abstract: Laccases from spent Lentinus polychrous Lev. mushroom compost were extracted, purified and characterized including evaluation of its potential in synthetic dye decolourisation. The enzyme was partial purified by ammonium sulfate fractionation, chromatography on DEAE-cellulose and Superdex 200 HR columns, respectively. The final step purification provided an 18.5% yield and a purification of 48.4 fold. The results from SDS-PAGE indicated that the laccase had a molecular weight of about 32 kDa. The enzyme’s pH optimum was pH 3.0 when using 2, 2-azinobis (3-ethylbenzothiazoline-6-sulfonate) (ABTS) as substrate and the optimum temperature was 55°C. The decolourisation of a model dye, Remazol Brilliant Blue R (RBBR), by the partial purified enzyme was investigated. The results showed that decolourisation ability was highest at about 66% within 3.5 h at pH 4.0.
Laccase Activity from Fresh Fruiting Bodies of Ganoderma sp. MK05: Purification and Remazol Brilliant Blue R Decolorization
Saranyu Khammuang,Rakrudee Sarnthima
Journal of Biological Sciences , 2009,
Abstract: The primary aim of this study was to screen for laccase activity from various mushroom fruiting bodies found in Maha Sarakham and nearby provinces of Northeast of Thailand. The enzyme activity was followed by a spectroscopic property of an oxidized product of 2, 2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) at 420 nm. The results found that crude water extract of mushroom Ganoderma sp. MK05 gave the highest specific activity of laccase. Consequence aim was to partial purification of the crude water extract of the selected mushroom and to evaluate the dye decolorization activity. The crude enzyme was partial purified by ammonium sulfate fractionation in the range of 40-70% saturation and followed with DEAE-cellulose anion exchange column to 1.34 and 3.07 purification folds, respectively. Native gel electrophoresis result showed one protein band with laccase activity. The partial purified laccase from this mushroom showed a high efficient decolorization ability of anthraquinone dye, Remazol Brilliant Blue R with above 80% within 5 h at 30°C.
Decolorization of rhodamine B and congo red by partial purified laccase from Lentinus polychrous Lév.
Pimjai Suwannawong,Saranyu Khammuang,,Rakrudee Sarnthima
Journal of Biochemical Technology , 2010,
Abstract: This study reports decolorization of Rhodamine B and Congo redby a partially purified laccase from Lentinus polychrous Lév. in thepresence or absence of 2,2-azinobis (3-ethylbenzothiazoline-6-sulfonate) diammonium salt (ABTS) as a redox mediator. Thedecolorization study showed that about 90% of Rhodamine B couldbe decolorized within 52 h, whereas Congo red could bedecolorized more than 75% within 3 h. The most effectiveconcentration of the redox mediator was 0.10 mM ABTS. Theoptimum pH for Rhodamine B decolorization was at pH 4.0-5.0and optimum temperature was at 50 oC. The optimum pH forCongo red decolorization was at pH 6.0-7.0, but increasingtemperature had less of an effect. The results and availability of thefungus indicated that laccase from L. polychrous Lév. has highpotential for the treatment of waste dyes.
Ligninolytic Enzymes of Lentinus polychrous Grown on Solid Substrates and its Application in Black Liquor Treatment
Wipawadee Budda,Rakrudee Sarnthima,Saranyu Khammuang,Nipa Milintawisamai
Journal of Biological Sciences , 2012,
Abstract: In nature, lignin can be degraded by ligninolytic enzymes from several of white rot fungi. Since, they can produce and secrete ligninolytic enzymes for lignin degradation and use as a carbon source. In this study, ligninolytic enzymes from Lentinus polychrous were investigated using CuSO4 at various concentrations (0-2.4 mol g-1 solid substrate) as laccase inducer. It was found that ligninolytic enzymes production by the fungus showed similar pattern. The main enzyme activities detected was laccase, following with manganese independent peroxidase and manganese dependence peroxidase, respectively. No lignin peroxidase activity was detected. Carbohydrate degrading enzymes, -glucosidase and cellulase activities have been found in a low quantity. Optimum conditions for catalysis were at pH 3-4 and temperature of 55C. The crude laccase showed a good stability in distilled water as well as in buffers pH 6-8. The highest stability was at pH 7 and 30C. The crude laccase of Lentinus polychrous was also evaluated for black liquor decolorization.
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