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- 저자 : ( Sanjay Govindwar ) (검색결과 31 건)
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Xiong, Jiu-Qiang,Govindwar, Sanjay,Kurade, Mayur B.,Paeng, Ki-Jung,Roh, Hyun-Seog,Khan, Moonis Ali,Jeon, Byong-Hun Pergamon Press 2019 Chemosphere Vol. No.
<P><B>Abstract</B></P> <P>A comprehensive ecotoxicological evaluation of a sulfamethazine (SMZ) and sulfamethoxazole (SMX) mixture was conducted using an indicator microalga, <I>Scenedesmus obliquus</I>. The toxicological effects of this mixture were studied using microalgal growth patterns, biochemical characteristics (total chlorophyll, carotenoid, carbohydrate, fatty acid methyl ester), and elemental and Fourier-transform infrared spectroscopy analyses. The 96-h half maximal effective concentration (EC<SUB>50</SUB>) of the SMZ and SMX mixture was calculated to be 0.15 mg L<SUP>−1</SUP> according to the dose-response curves obtained. The chlorophyll content decreased with elevated SMZ and SMX concentrations, while the carotenoid content initially increased and then decreased as concentration raised. The unsaturated fatty acid methyl esters (FAMEs) content was enhanced with higher SMZ and SMX concentrations, while that of saturated FAMEs simultaneously decreased due to SMZ and SMX stress. Elemental analyses showed an improved percentage of nitrogen and sulfur in the microalgal biomass as SMZ and SMX concentrations increased. The microalga <I>S. obliquus</I> was shown to biodegrade the chemicals tested and removed 31.4–62.3% of the 0.025–0.25 mg SMZ L<SUP>−1</SUP> and 27.7–46.8% of the 0.025–0.25 mg SMX L<SUP>−1</SUP> in the mixture after 12 days of cultivation. The greater biodegradation observed at higher SMZ and SMX concentrations indicates that microalgal degradation of SMZ and SMX could act as an efficient adaptive mechanism to antibiotics.</P> <P><B>Highlights</B></P> <P> <UL> <LI> <I>S. obliquus</I> can withstand high doses of SMZ and SMX. </LI> <LI> EC<SUB>50</SUB> of SMZ, SMX and their mixture for <I>S. obliquus</I> was 1.23, 0.12, and 0.15 mg L<SUP>−1</SUP>. </LI> <LI> <I>S. obliquus</I> removed 62.3 and 46.8% of SMZ and SMX, respectively. </LI> <LI> A greater biodegradation was observed in higher SMZ and SMX concentration. </LI> </UL> </P>
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Sushama S. Gomare,Jyoti P. Jadhav,Sanjay P. Govindwar 한국생물공학회 2008 Biotechnology and Bioprocess Engineering Vol.13 No.2
Lignin peroxidase (EC 1.11.1.14) was purified from the Brevibacillus laterosporus MTCC 2298 by ion exchange chromatography. The Km value of the purified lignin peroxidase (using n-propanol as substrate) was 1.6 mM. The MW of purified enzyme determined with the help of MW-standard markers was approximately 205 kDa. Purity of the enzyme was confirmed by native polyacrylamide gel electrophoresis (PAGE) and the activity staining using a substrate L-DOPA. Sulfonated azo dyes such as Methyl orange and Blue-2B were degraded by the purified lignin peroxidase. Degradation of the dyes was confirmed by HPLC, GC-MS, and FTIR spectroscopy. The mainly elected products of Methyl orange were 4-substituted hexanoic acid (m/z = 207), 4-cyclohexenone lactone cation (m/z = 191), and 4-isopropanal-2, 5-cyclohexa-dienone (m/z = 149) and for Blue-2B were 4-(2-hexenoic acid)-2, 5-cyclohexa-diene-one (m/z = 207; M - 1 = 206) and dehydro-acetic acid derivative (m/z = 223).
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Biological Conversion of Amino Acids to Higher Alcohols
El-Dalatony, Marwa M.,Saha, Shouvik,Govindwar, Sanjay P.,Abou-Shanab, Reda A.I.,Jeon, Byong-Hun Elsevier 2019 Trends in biotechnology Vol.37 No.8
<P>‘Higher’ alcohols, which contain more than two carbons, have a higher boiling point, higher cetane number, and higher energy density than ethanol. Blends of biodiesel and higher alcohols can be used in internal combustion engines as next-generation biofuels without any modification and are minimally corrosive over extensive use. Producing higher alcohols from biomass involves fermenting and metabolizing amino acids. In this review, we describe the pathways and regulatory mechanisms involved in amino acid bioprocessing to produce higher alcohols and the effects of amino acid supplementation as a nitrogen source for higher alcohol production. We also discuss the most recent approaches to improve higher alcohol production via genetic engineering technologies for three microorganisms: <I>Saccharomyces cerevisiae</I>, <I>Clostridium</I> spp., and <I>Escherichia coli</I>.</P> <P><B>Highlights</B></P> <P>Proteins are polymers of various amino acids, connected via peptide bonds and classified as a major feedstock for bioenergy production. Higher alcohols are high-density alternative fuels that increase the longevity of transportation fuels.</P> <P>Proteins have a significant role in the fermentation process by providing amino acids for the growth of microorganisms, and enhancement of sugar permeability, in carbohydrate-rich sources.</P> <P>Due to the environmental and economic advantages of recombinant DNA technology, fermentation is the most used process for industrial-scale alcohol production. Applying this technology to higher alcohols can significantly improve industrialization for advanced fuel production.</P> <P>Extraction techniques are used to separate and mitigate the toxicity of alcohols produced in the fermentation broth to maintain the microbial cell viability for longer.</P>
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Amar A. Telke,Avinash A. Kadam,Sujit S. Jagtap,Jyoti P. Jadhav,Sanjay P. Govindwar 한국생물공학회 2010 Biotechnology and Bioprocess Engineering Vol.15 No.4
In our study, we produced intracellular blue laccase by growing the filamentous fungus Aspergillus ochraceus NCIM-1146 in potato dextrose broth. The enzyme was then purified 22-fold to a specific activity of 4.81 U/mg using anion-exchange and size exclusion chromatography. The molecular weight of purified laccase was estimated as 68 kDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme showed maximum substrate specificity toward 2,2'-Azinobis, 3-ethylbenzothiazoline-6-sulfonic acid than any other substrate. The optimum pH and temperature for laccase activity were 4.0 and 60ºC, respectively. The purified enzyme was stable up to 50ºC, and high laccase activity was maintained at pH 5.0 ~ 7.0. Laccase activity was strongly inhibited by sodium azide, EDTA, dithiothreitol, and L-cysteine. Purified laccase decolorized various textile dyes within 4 h in the absence of redox mediators. HPLC and FTIR analysis confirmed degradation of methyl orange. The metabolite formed after decolorization of methyl orange was characterized as p-N,N'-dimethylamine phenyldiazine using GCMS.
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Umesh U. Jadhav,Vishal V. Dawkar,Dhawal P. Tamboli,Sanjay P. Govindwar 한국생물공학회 2009 Biotechnology and Bioprocess Engineering Vol.14 No.3
In the present work, we have purified veratryl alcohol oxidase (VAO) enzyme from Comamonas sp. UVS to evaluate its potential to decolorize textile dyes. VAO was purified (13.9 fold) by an ion exchange followed by the size exclusion chromatography. Molecular weight of the VAO was estimated to be about 66 kDa by SDS-PAGE. The optimum pH and temperature of oxidase were 30°C and 65°C, respectively. VAO showed maximum activity with n-propanol among the various substrates (n-propanol, veratryl alcohol, L-dopa, tryptophan, etc.). Under standard assay conditions, Km value of the enzyme was 2.5 mM towards veratrole. The enzyme activity was completely inhibited by 0.5 mM sodium azide. L-cysteine, dithiothreitol, and the metal chelator, EDTA had a slight inhibitory effect. The purified enzyme was able to decolorize textile dyes, Red HE7B (57.5%) and Direct Blue GLL (51.09%) within 15 h at 40 μg/mL concentration. GC-MS analysis of the metabolites suggested oxidative cleavage and desulphonation of these dyes In the present work, we have purified veratryl alcohol oxidase (VAO) enzyme from Comamonas sp. UVS to evaluate its potential to decolorize textile dyes. VAO was purified (13.9 fold) by an ion exchange followed by the size exclusion chromatography. Molecular weight of the VAO was estimated to be about 66 kDa by SDS-PAGE. The optimum pH and temperature of oxidase were 30°C and 65°C, respectively. VAO showed maximum activity with n-propanol among the various substrates (n-propanol, veratryl alcohol, L-dopa, tryptophan, etc.). Under standard assay conditions, Km value of the enzyme was 2.5 mM towards veratrole. The enzyme activity was completely inhibited by 0.5 mM sodium azide. L-cysteine, dithiothreitol, and the metal chelator, EDTA had a slight inhibitory effect. The purified enzyme was able to decolorize textile dyes, Red HE7B (57.5%) and Direct Blue GLL (51.09%) within 15 h at 40 μg/mL concentration. GC-MS analysis of the metabolites suggested oxidative cleavage and desulphonation of these dyes
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Kurade, Mayur B.,Waghmode, Tatoba R.,Xiong, Jiu-Qiang,Govindwar, Sanjay P.,Jeon, Byong-Hun Elsevier 2019 Journal of cleaner production Vol.213 No.-
<P><B>Abstract</B></P> <P>Textile dyes are xenobiotic contaminants which pose a potential risk on the ecosystem upon their disposal to the water bodies. This study evaluated the efficiencies of different immobilization matrices for its utilization in a reactor with continuous mode operation for decolorization of textile effluent. An effective consortium of bacteria (<I>Brevibacillus laterosporus</I>) and yeast (<I>Galactomyces geotrichum</I>) were immobilized in different support matrices including calcium alginate, polyvinyl alcohol, stainless steel sponge and polyurethane foam to investigate the decolorization of a model azo dye, Remazol red and textile industry effluent. The microbial consortia immobilized in stainless steel sponge and polyurethane foam exhibited 100% decolorization of 50 mg L<SUP>−1</SUP> Remazol red in 11 and 15 h, respectively; however, calcium alginate and polyvinyl alcohol required considerably more time (20 and 24 h, respectively) for complete decolorization. Among all the matrices, The calcium alginate, stainless steel sponge and polyurethane foam showed >95% decolorization of textile industry effluent within 48 h. The calcium alginate and polyvinyl alcohol exhibited stable performance of decolorization with its repeated use for 5 cycles with >76% decolorization. An upflow fixed bed reactor (total volume- 215 mL) packed with the immobilized cells of consortium onto stainless steel sponge attained ∼90% decolorization of textile industry effluent in continuous operation at 10 mL h<SUP>−1</SUP>. The decolorization efficiency of the reactor was well maintained (>90%) when the reactor was used repeatedly for three cycles. The overall results indicated that immobilized mixed consortium cells can be considered as an effective tool for its potential application in removal of xenobiotic textile dyes from the textile industry wastewater with >90% of decolorization efficiency.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Effective microbial consortium was immobilized in different support matrices. </LI> <LI> SS-sponge immobilized cells showed 100% decolorization of Remazol red in 11 h. </LI> <LI> Calcium alginate, polyvinyl alcohol showed stable decolorization of textile effluent. </LI> <LI> The upflow fixed bed reactor can be used for continuous decolorization of effluent. </LI> </UL> </P>
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( Mahesh Khot ),( Rohini Gupta ),( Kadambari Barve ),( Smita Zinjarde ),( Sanjay Govindwar ),( Ameeta Ravikumar ) 한국미생물 · 생명공학회 2015 Journal of microbiology and biotechnology Vol.25 No.4
This study evaluated the microbial conversion of coconut oil waste, a major agro-residue in tropical countries, into single cell oil (SCO) feedstock for biodiesel production. Copra cake was used as a low-cost renewable substrate without any prior chemical or enzymatic pretreatment for submerged growth of an oleaginous tropical mangrove fungus, Aspergillus terreus IBB M1. The SCO extracted from fermented biomass was converted into fatty acid methyl esters (FAMEs) by transesterification and evaluated on the basis of fatty acid profiles and key fuel properties for biodiesel. The fungus produced a biomass (8.2 g/l) yielding 257 mg/g copra cake SCO with ~98% FAMEs. The FAMEs were mainly composed of saturated methyl esters (61.2%) of medium-chain fatty acids (C12-C18) with methyl oleate (C18:1; 16.57%) and methyl linoleate (C18:2; 19.97%) making up the unsaturated content. A higher content of both saturated FAMEs and methyl oleate along with the absence of polyunsaturated FAMEs with ≥4 double bonds is expected to impart good fuel quality. This was evident from the predicted and experimentally determined key fuel properties of FAMEs (density, kinematic viscosity, iodine value, acid number, cetane number), which were in accordance with the international (ASTM D6751, EN 14214) and national (IS 15607) biodiesel standards, suggesting their suitability as a biodiesel fuel. The low cost, renewable nature, and easy availability of copra cake, its conversion into SCO without any thermochemical pretreatment, and pelleted fungal growth facilitating easier downstream processing by simple filtration make this process cost effective and environmentally favorable.
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Peroxidase from Bacillus sp. VUS and Its Role in the Decolorization of Textile Dyes
Vishal V. Dawkar,Umesh U. Jadhav,Amar A. Telke,Sanjay P. Govindwar 한국생물공학회 2009 Biotechnology and Bioprocess Engineering Vol.14 No.3
Peroxidase was purified by an ion exchange chromatography followed by gel filtration chromatography from dye degrading Bacillus sp. strain VUS. The optimum pH and temperature of the enzyme activity was 3.0 and 65°C, respectively. This enzyme showed more activity with n-propanol than other substrates tested viz. xylidine, 3-(3,4-dihydroxy phenyl) Lalanine (L-DOPA), hydroxyquinone, ethanol, indole, and veratrole. Km value of the enzyme was 0.076 mM towards n-propanol under standard assay conditions. Peroxidase was more active in presence of the metal ions like Li²+ , Co²+ , K²+ , Zn²+, and Cu²+ where as it showed less activity in the presence of Ca²+ and Mn²+ . Inhibitors like ethylenediamine tetraacetic acid (EDTA), glutamine, and phenylalanine inhibited the enzyme partially, while sodium azide (NaN3) completely. The crude as well as the purified peroxidase was able to decolourize different industrial dyes. This enzyme decolourized various textile dyes and enhanced percent decolourization in the presence of redox mediators. Aniline was the most effective redox mediator than other mediators tested. Gas chromatography-Mass spectrometry (GC-MS) confirmed the formation of 7-Acetylamino-4-hydroxy-naphthalene-2-sulphonic acid as the final product of Reactive Orange 16 indicating asymmetric cleavage of the dye Peroxidase was purified by an ion exchange chromatography followed by gel filtration chromatography from dye degrading Bacillus sp. strain VUS. The optimum pH and temperature of the enzyme activity was 3.0 and 65°C, respectively. This enzyme showed more activity with n-propanol than other substrates tested viz. xylidine, 3-(3,4-dihydroxy phenyl) Lalanine (L-DOPA), hydroxyquinone, ethanol, indole, and veratrole. Km value of the enzyme was 0.076 mM towards n-propanol under standard assay conditions. Peroxidase was more active in presence of the metal ions like Li²+ , Co²+ , K²+ , Zn²+, and Cu²+ where as it showed less activity in the presence of Ca²+ and Mn²+ . Inhibitors like ethylenediamine tetraacetic acid (EDTA), glutamine, and phenylalanine inhibited the enzyme partially, while sodium azide (NaN3) completely. The crude as well as the purified peroxidase was able to decolourize different industrial dyes. This enzyme decolourized various textile dyes and enhanced percent decolourization in the presence of redox mediators. Aniline was the most effective redox mediator than other mediators tested. Gas chromatography-Mass spectrometry (GC-MS) confirmed the formation of 7-Acetylamino-4-hydroxy-naphthalene-2-sulphonic acid as the final product of Reactive Orange 16 indicating asymmetric cleavage of the dye
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Kurade, Mayur B.,Saha, Shouvik,Salama, El-Sayed,Patil, Swapnil M.,Govindwar, Sanjay P.,Jeon, Byong-Hun Elsevier Applied Science 2019 Bioresource Technology Vol. No.
<P><B>Abstract</B></P> <P>Fats, oil and grease (FOG) are energy-dense wastes that substantially increase biomethane recovery. Shifts in the microbial community during anaerobic co-digestion of FOG was assessed to understand relationships between substrate digestion and microbial adaptations. Excessive addition of FOG inhibited the methanogenic activity during initial phase; however, it enhanced the ultimate methane production by 217% compared to the control. The dominance of Proteobacteria was decreased with a simultaneous increase in Firmicutes, Bacteriodetes, Synergistetes and Euryarchaeota during the co-digestion. A significant increase in <I>Syntrophomonas</I> (0.18–11%), <I>Sporanaerobacter</I> (0.14–6%) and <I>Propionispira</I> (0.02–19%) was observed during co-digestion, which substantiated their importance in acetogenesis. Among methanogenic Archaea, the dominance of <I>Methanosaeta</I> (94%) at the beginning of co-digestion was gradually replaced by <I>Methanosarcina</I> (0.52–95%)<I>.</I> The absence/relatively low abundance of syntrophic acetate oxidizers and hydrogenotrophic methanogens, and dominance of acetoclastic methanogens suggested that methane generation during co-digestion of FOG was predominantly conducted through acetoclastic pathway led by <I>Methanosarcina</I>.</P> <P><B>Highlights</B></P> <P> <UL> <LI> The addition of fats, oil and grease enhanced ultimate methane production by 217%. </LI> <LI> Firmicutes, Bacteriodetes, Synergistetes and Euryarchaeota were greatly increased. </LI> <LI> Dominance of <I>Methanosaeta</I> was replaced by <I>Methanosarcina</I> at the end of digestion. </LI> <LI> Methane was predominantly generated through acetoclastic pathway by <I>Methanosarcina</I>. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
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