Now showing items 1-6 of 6
| Abstract: | An alkaline protease from marine Engyodontium album was characterized for its physicochemical properties towards evaluation of its suitability for potential industrial applications. Molecular mass of the enzyme by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) analysis was calculated as 28.6 kDa. Isoelectric focusing yielded pI of 3–4. Enzyme inhibition by phenylmethylsulfonyl fluoride (PMSF) and aprotinin confirmed the serine protease nature of the enzyme.Km, Vmax, and Kcat of the enzyme were 4.727 9 10-2 mg/ml, 394.68 U, and 4.2175 9 10-2 s-1, respectively. Enzyme was noted to be active over a broad range of pH (6–12) and temperature (15–65 C), withmaximumactivity at pH 11 and 60 C. CaCl2 (1 mM), starch (1%), and sucrose (1%) imparted thermal stability at 65 C. Hg2?, Cu2?, Fe3?, Zn2?, Cd?, and Al3? inhibited enzyme activity, while 1 mMCo2? enhanced enzyme activity. Reducing agents enhanced enzyme activity at lower concentrations. The enzyme showed considerable storage stability, and retained its activity in the presence of hydrocarbons, natural oils, surfactants, and most of the organic solvents tested. Results indicate that the marine protease holds potential for use in the detergent industry and for varied applications. |
| Description: | J Ind Microbiol Biotechnol (2011) 38:743–752 DOI 10.1007/s10295-010-0914-3 |
| URI: | http://dyuthi.cusat.ac.in/purl/4264 |
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| Characterizatio ... odontium album BTMFS10.pdf | (382.3Kb) |
| Abstract: | Inthis paper,we define partial moments for a univariate continuous random variable. A recurrence relationship for the Pearson curve using the partial moments is established. The interrelationship between the partial moments and other reliability measures such as failure rate, mean residual life function are proved. We also prove some characterization theorems using the partial moments in the context of length biased models and equilibrium distributions |
| Description: | METRON - International Journal of Statistics 2004, vol. LXII, n. 3, pp. 353-362 |
| URI: | http://dyuthi.cusat.ac.in/purl/4277 |
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| Characterizatio ... using partial moments.pdf | (96.08Kb) |
| Abstract: | Bacillus smithii BTMS 11, isolated from marine sediment, produced alkaline and thermostable lipase. The enzyme was purified to homogeneity by ammonium sulfate precipitation and ion exchange chromatography which resulted in 0.51 % final yield and a 4.33 fold of purification. The purified enzyme was found to have a specific activity of 360 IU/mg protein. SDS-PAGE analyses, under non-reducing and reducing conditions, yielded a single band of 45 kDa indicating the single polypeptide nature of the enzyme and zymogram analysis using methylumbelliferyl butyrate as substrate confirmed the lipolytic activity of the protein band. The enzyme was found to have 50 C and pH 8.0 as optimum conditions for maximal activity. However, the enzyme was active over wide range of temperatures (30–80 C) and pH (7.0–10.0). Effect of a number of metal salts, solvents, surfactants, and other typical enzyme inhibitors on lipase activity was studied to determine the novel characteristics of the enzyme. More than 90 % of the enzyme activity was observed even after 3 h of incubation in the presence of commercial detergents Surf, Sunlight, Ariel, Henko, Tide and Ujala indicating the detergent compatibility of B. smithii lipase. The enzyme was also found to be efficient in stain removal from cotton cloths. Further it was observed that the enzyme could catalyse ester synthesis between fatty acids of varying carbon chain lengths and methanol with high preference for medium to long chain fatty acids showing 70 % of esterification. Results of the study indicated scope for application of this marine bacterial lipase in various industries |
| Description: | World J Microbiol Biotechnol (2013) 29:1349–1360 DOI 10.1007/s11274-013-1298-0 |
| URI: | http://dyuthi.cusat.ac.in/purl/4262 |
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| Detergent compa ... cillus smithii BTMS 11.pdf | (531.4Kb) |
| Abstract: | A continuous cell line (SISK) from kidney of sea bass, Lates calcarifer, has been established and characterized. The cell line was maintained in Leibovitz' L-15 supplemented with 15% fetal bovine serum. This cell line has been subcultured more than 100 times over a period of 2 years. The SISK cell line consists of predominantly of epithelial-like cells. These cells showed strong positive for epithelial markers such as cytokeratin 19 and pancytokeratin. The cells were able to grow at temperature between 25 and 32 °C with optimum temperature of 28 °C. The growth rate of sea bass kidney cells increased as the FBS proportion increased from 2% to 20% at 28 °C with optimum growth at the concentrations of 15% or 20% FBS. The distribution of chromosome number was 30 to 56 with a modal peak at 48 chromosomes. Polymerase chain reaction products were obtained from SISK cells and tissues of sea bass with primer sets of microsatellite markers of sea bass. Five fish viruses were tested on this cell line to determine its susceptibility to these viruses and this was found to be susceptible to MABV NC1 and nodavirus, and the infection was confirmed by RT-PCR and CPE. This suggests that the SISK cell line has good potential for the isolation of various fish viruses. This cell line has been shown to be susceptible to bacterial extracellular products. The SISK cell line is the India's first marine fish cell line. |
| Description: | Aquaculture 257 (2006) 92–103 |
| URI: | http://dyuthi.cusat.ac.in/purl/4025 |
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| Establishment a ... ass (Lates calcarifer).pdf | (1.207Mb) |
| Abstract: | Protease inhibitors have great demand in medicine and biotechnology. We report here the purification and characterization of a protease inhibitor isolated from mature leaf extract of Moringa oleifera that showed maximum inhibitor activity. The protease inhibitor was purified to 41.4-fold by Sephadex G75 and its molecular mass was calculated as 23,600 Da. Inhibitory activity was confirmed by dot-blot and reverse zymogram analyses. Glycine, glutamic acid, alanine, proline and aspartic acid were found as the major amino acids of the inhibitor protein. Maximal activity was recorded at pH 7 and at 40 ◦C. The inhibitor was stable over pH 5–10; and at 50 ◦C for 2 h. Thermostability was promoted by CaCl2, BSA and sucrose. Addition of Zn2+ and Mg2+, SDS, dithiothreitol and -mercaptoethanol enhanced inhibitory activity, while DMSO and H2O2 affected inhibitory activity. Modification of amino acids at the catalytic site by PMSF and DEPC led to an enhancement in the inhibitory activity. Stoichiometry of trypsin–protease inhibitor interaction was 1:1.5 and 0.6 nM of inhibitor effected 50% inhibition. The low Ki value (1.5 nM) obtained indicated scope for utilization of M. oliefera protease inhibitor against serine proteases |
| Description: | Process Biochemistry 46 (2011) 2291–2300 |
| URI: | http://dyuthi.cusat.ac.in/purl/4257 |
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| Protease inhibi ... , and characterisation.pdf | (797.7Kb) |
| Abstract: | Recently, reciprocal subtangent has been used as a useful tool to describe the behaviour of a density curve. Motivated by this, in the present article we extend the concept to the weighted models. Characterization results are proved for models viz. gamma, Rayleigh, equilibrium, residual lifetime, and proportional hazards. An identity under weighted distribution is also obtained when the reciprocal subtangent takes the form of a general class of distributions. Finally, an extension of reciprocal subtangent for the weighted models in the bivariate and multivariate cases are introduced and proved some useful results |
| Description: | Communications in Statistics—Theory and Methods, 41: 1397–1410, 2012 |
| URI: | http://dyuthi.cusat.ac.in/purl/4286 |
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| Some Results on ... ext of Weighted Models.pdf | (170.9Kb) |
Now showing items 1-6 of 6
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