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Water Soluble Polyaniline as Biocide
Kumar, K. K. Satheesh,Ponmariappan, S.,Geetha, S.,Trivedi, D. C. 한국부식방식학회 2002 Corrosion Science and Technology Vol.31 No.3
The microbial fouling of a submerged object is a complex phenomenon and its control requires the use of potentially hazardous chemicals. The effective control of microbial films on a submerged object is essential to prevent its corrosion. The microbial fouling not only accelerates the rate of corrosion due to imbalance of oxygen by creating electrochemical cell. The currently available biocides are for the control of planktonic microorganisms is based on tri-organic tin compounds, which are not friendly to aquatic life. Our preliminary study indicates that polyaniline doped with fhctionalized dopan? at concentration of 4×10^-6 g/ml is able to control the growth of microorganism in the area of 140㎜². In this paper we present our study on synthesis and use of water-soluble polyaniline as a biocide to control bio fouling.
Enhanced Production and Partial Purification of Glucoamylase from Mutated Bacillus sp. FME
Kumar, Gudi Satheesh,Chandra, Muni Ramanna Gari Subhosh,Sujana, Yakasiri Nagasai,Reddy, Bontha Rajasekhar,Choi, Yong-Lark The Korean Society for Applied Biological Chemistr 2009 Applied Biological Chemistry (Appl Biol Chem) Vol.52 No.5
In this study, a potent newly-isolated glucoamylase producing actively growing cells of Bacillus sp. FME was subjected to UV irradiation and ethidium bromide (EtBr) mutagenesis. The promising colonies were further screened for glucoamylase production via plate assays and submerged enzyme production at the flask level. Amongst all of the tested colonies, the best mutant, Bacillus sp. FME 2, selected from UV irradiation (20 min) and EtBr (1 mg/mL), was shown to be the most promising. The yield of glucoamylase generated by the mutant strain was approximately 3.0 fold and 1397 U/mL with an incubation period of 24 h, which was larger than the yield generated by the wild-type strain. The glucoamylase was partially purified using ammonium sulphate precipitation followed by gel exclusion chromatography. The enzyme was partially purified 3.0-fold to homogeneity with a final recovery of 66% and a specific activity of 1145 U/mg protein for the mutant strain. The molecular mass was approximately 67.1 kDa, as determined by SDS-PAGE. The active band was observed as a clear colorless area on zymogram analysis, which indicated an absence of glucoamylase isoforms. The results of thin-layer chromatography identified this enzyme as a glucoamylase.
Kumar, G. Satheesh,Chandra, M. Subhosh,Sumanth, M.,Vishnupriya, A.,Reddy, B. Rajasekhar,Choi, Yong-Lark The Korean Society for Applied Biological Chemistr 2009 Journal of Applied Biological Chemistry (J. Appl. Vol.52 No.1
Newly isolated strains Bacillus sp. FME 1 and FME 2 were evaluated for the cellulolytic enzymes production during submerged fermentation (SmF) of different substrates including rice husk, Whatman filter paper and cellulose powder CF 11. Extracellular enzyme assays for CMCase, FPase and ${\beta}$-glucosidase were examined up to 8 days of submerged fermentation. Among the three substrates, rice husk was the most suitable substrate for higher production of cellulolytic enzymes. Maximum titers of 100, 45, and 3.5 U/mL in respect of CMCase, FPase and ${\beta}$-glucosidase in Bacillus sp. FME 2 were recovered as against 45, 12, and 0.39 U/mL in Bacillus sp. FME 1 respectively, at their respective peak time intervals. Bacillus sp. FME 2 was found to produce higher cellulolytic enzyme activities than Bacillus sp. FME 1.
SOME PROPERTIES OF BIVARIATE GENERALIZED HYPERGEOMETRIC PROBABILITY DISTRIBUTIONS
Kumar, C. Satheesh The Korean Statistical Society 2007 Journal of the Korean Statistical Society Vol.36 No.3
In this paper we study some important properties of the bivariate generalized hypergeometric probability (BGHP) distribution by establishing the existence of all the moments of the distribution and by deriving recurrence relations for raw moments. It is shown that certain mixtures of BGHP distributions are again BGHP distributions and a limiting case of the distribution is considered.
Satheesh Kumar Gudi,최용락,Chandrasekhar Gurramkonda,Gulam Rather,Muniramanna Gari Subohsh Chandra,Usha Kiranmayi Mangamuri,Shdhakar Podha 한국응용생명화학회 2013 Applied Biological Chemistry (Appl Biol Chem) Vol.56 No.4
Glucoamylase (EC 3.2.1.3) is an important group of enzymes in starch processing, also referred to as amyloglucosidases,which are exo-acting amylases that release glucose from the nonreducing end of starch and related oligosaccharides. The glucoamylase newly isolated from the Aspergillus niger FME)was reported for the first time. This enzyme was produced by detergent-mediated release and purified to ~9.11 fold using Sephadex-G 100 and ion-exchange chromatography. Molecular mass of the glucoamylase was ~36 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The product of starch hydrolysis, analysed by thin-layer chromatography, showed the presence of glucose. The optimum pH and temperature for glucoamylase activity was 5.0 and 45oC,respectively. The Km and Vmax values of the enzyme were also determined using soluble starch as substrate as 94 μg/mL and 39.02 U/mg, respectively. Moreover, glucoamylase was slightly activated by presence of Na and K ions and 10–20% inhibition was observed in presence of Zn2+, Sn2+, Mg2+, Ni2+, Mn2+, and almost 80% with Cu2+ ions, whereas the presence of ethylene diamine tetra acetic acid (EDTA) did not show significant inhibition. Glucoamylase, also assayed for surfactant property, shows significant surfactant tolerance at high concentrations of detergent and can retain 90% of its activity. Finally, secondary structure analysis of glucoamylase by circular dichroism spectroscopy showed the presence of 48% α-helix, 11% β-sheet, and 41%random structure.
On Estimating the Parameters of an Extended Form of Logarithmic Series Distribution
Kumar, C. Satheesh,Riyaza, A. The Korean Statistical Society 2013 Communications for statistical applications and me Vol.20 No.5
We consider an extended version of a logarithmic series distribution and discuss the estimation of its parameters by the method of moments and the method of maximum likelihood. Test procedures are suggested to test the significance of the additional parameter of this distribution and all procedures are illustrated with the help of real life data sets. In addition, a simulation study is conducted to assess the performance of the estimators.
G. Satheesh Kumar(사티시 쿠마르),M. Subhosh Chandra(수보쉬 찬드라),K. V. Mallaiah(브이 말라이아),P. Sreenivasulu(스리니바슐루),Yong Lark Choi(최용락) 한국생명과학회 2012 생명과학회지 Vol.22 No.4
고온성 α-아밀라제를 생산하는 내열성 Alicyclobacillus acidocaldarius 균을 인도 Tirupati, Andhra Pradesh 지역의 가열한 미강 열수 추출물에서 분리하였다. 분리균인 내열성 Alicyclobacillus acidocaldarius가 생산하는 세포 외 α-아밀라제의 생산과 성장에 미치는 배양조건을 실험실 규모로 조사하였다. 그 결과 α-amylase의 고생산 최적 조건은 온도 60oC, pH 6.0 및 배지의 전분농도 1.0%, yeast extract와 tryptone은 0.2%를 나타냈다. Surfactantslike Tween-20과 SDS 같은 계면활성제는 0.02%까지 균주의 성장과 효소 생산을 증가 시켰으나, 그 이상의 농도에서는 α-amylase 효소의 생산이 현저하게 감소하였다. A thermophilic Alicyclobacillus acidocaldarius, which produces thermostable α-amylase, was isolated from the hot water effluent of a boiled rice mill near Tirupati, Andhra Pradesh, India. The effect of different culture conditions on the growth and production of extracellular α-amylase by thermophilic A. acidocaldarius was investigated in laboratory scale. The results showed that the optimum conditions for the production of α-amylase are a temperature of 60°C, pH of 6.0, and medium starch concentration of 1.0%, and yeast extract and tryptone of 0.2%. Surfactants, like Tween-20 and SDS, up to 0.02%, were found to increase the bacterial growth and enzymes. Further increase in their concentration resulted in significantly decreased enzyme production.
G. Satheesh kumar,P. Sreenivasulu,M. Subhosh Chandra,Yong-Lark Choi,K. V. Mallaiah 한국생물공학회 2010 Biotechnology and Bioprocess Engineering Vol.15 No.3
In this study, the production of extracellular thermostable α-amylase by newly isolated thermophilic Alicyclobacillus acidocaldarius was detected on LB agar plates containing 1.0% soluble potato starch and incubated at 60oC. This extracellular α-amylase was purified to homogeneity by ammonium sulphate precipitation followed by Sephadex and ion-exchange chromatography. The α-amylase was purified to 8.138 fold homogeneity with a final recovery of 58% and a specific activity of 3,239 U/mg proteins. The purified α-amylase appeared as a single protein band on SDS-PAGE with a molecular mass of 94.5 kDa. Non-denaturing PAGE analysis showed one major band associated with enzyme activity, indicating the absence of isoenzymes. A TLC analysis showed maltose as major end product of the enzyme. The optimum assay temperature and pH for enzyme activity were 60oC and 6.0respectively; however, the enzyme activity was stable over a wide range of pH and temperatures. The α-amylase retained its activity in the presence of the denaturing agents - SDS, Triton X-100, Tween-20, Tween-80, and was significantly inhibited by EDTA and urea. Calcium ions increased the enzyme activity, while Hg2+, Zn2+, and Co2+had inhibitory effects. The Km and Vmax values were found to be 2.9 mg/mL and 7936 U/mL respectively.
Some Properties of Bivariate Generalized HypergeometricProbability Distributions
C. Satheesh Kumar 한국통계학회 2007 Journal of the Korean Statistical Society Vol.36 No.3
In this paper we study some important properties of the bivariate gener-alized hypergeometric probability (BGHP) distribution by establishing theexistence of all the moments of the distribution and by deriving recurrencerelations for raw moments. It is shown that certain mixtures of BGHP distri-butions are again BGHP distributions and a limiting case of the distributionis considered.
Gudi, Satheesh Kumar,Gurramkonda, Chandrasekhar,Rather, Gulam,Chandra, Muniramanna Gari Subohsh,Mangamuri, Usha Kiranmayi,Podha, Shdhakar,Choi, Yong-Lark 한국응용생명화학회 2013 Applied Biological Chemistry (Appl Biol Chem) Vol.56 No.4
Glucoamylase (EC 3.2.1.3) is an important group of enzymes in starch processing, also referred to as amyloglucosidases, which are exo-acting amylases that release glucose from the non-reducing end of starch and related oligosaccharides. The glucoamylase newly isolated from the Aspergillus niger FME) was reported for the first time. This enzyme was produced by detergent-mediated release and purified to ~9.11 fold using Sephadex-G 100 and ion-exchange chromatography. Molecular mass of the glucoamylase was ~36 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The product of starch hydrolysis, analysed by thin-layer chromatography, showed the presence of glucose. The optimum pH and temperature for glucoamylase activity was 5.0 and $45^{\circ}C$, respectively. The $K_m$ and $V_{max}$ values of the enzyme were also determined using soluble starch as substrate as $94{\mu}g/mL$ and 39.02 U/mg, respectively. Moreover, glucoamylase was slightly activated by presence of Na and K ions and 10-20% inhibition was observed in presence of $Zn^{2+}$, $Sn^{2+}$, $Mg^{2+}$, $Ni^{2+}$, $Mn^{2+}$, and almost 80% with $Cu^{2+}$ ions, whereas the presence of ethylene diamine tetra acetic acid (EDTA) did not show significant inhibition. Glucoamylase, also assayed for surfactant property, shows significant surfactant tolerance at high concentrations of detergent and can retain 90% of its activity. Finally, secondary structure analysis of glucoamylase by circular dichroism spectroscopy showed the presence of 48% ${\alpha}$-helix, 11% ${\beta}$-sheet, and 41% random structure.