Rajkot, India
Rajkot, India

The Saurashtra University is one of the significant universities in Gujarat state in India. This university was established on 23 May 1967 in Rajkot city, the administrative headquarters at Rajkot. Presently, 272 colleges in Amreli, Jamnagar, Junagadh, Porbandar, Rajkot and Surendranagar districts are affiliated with the Saurashtra University. Wikipedia.

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Sheth B.P.,Saurashtra University | Thaker V.S.,Saurashtra University
Planta | Year: 2014

Plants dwelling at the base of biological food chain are of fundamental significance in providing solutions to some of the most daunting ecological and environmental problems faced by our planet. The reductionist views of molecular biology provide only a partial understanding to the phenotypic knowledge of plants. Systems biology offers a comprehensive view of plant systems, by employing a holistic approach integrating the molecular data at various hierarchical levels. In this review, we discuss the basics of systems biology including the various 'omics' approaches and their integration, the modeling aspects and the tools needed for the plant systems research. A particular emphasis is given to the recent analytical advances, updated published examples of plant systems biology studies and the future trends. © 2014 Springer-Verlag Berlin Heidelberg.

Gohel S.D.,Saurashtra University | Singh S.P.,Saurashtra University
International Journal of Biological Macromolecules | Year: 2013

An alkaline serine protease from a newly isolated salt-tolerant alkaliphilic actinomycetes, Brachystreptospora xinjiangensis OM-6 was purified with 35- and 26-fold purification and 47% and 22% yield employing two steps and one step methods, respectively. The enzyme was quite stable at 80°C in 30% Na-glutamate with the deactivation rate constant (Kd) 8.66 and half life (t1/2) 80.04min. The activation energies (E), enthalpy (ΔH*), entropy (ΔS*) and change in free energy (ΔG*) for the protease deactivation were calculated in the presence of 30% Na-glutamate and correlated with the enzyme stability. The thermodynamic analysis corresponded the trends of the enzyme stability and inactivation. The enzyme retained high activity and significant stability at higher salt, temperature, range of pH and metal ions. The enzyme was extremely resistant against urea denaturation, oxidizing and reducing agents and surfactants, a finding which is rather unique and restricted to only few proteins. © 2013 Elsevier B.V.

The protective effect of Lactobacillus rhamnosus 231 (Lr 231) against potent carcinogen N-Methyl-N'-Nitro-N-Nitrosoguanidine (MNNG) in the rat model is studied. Daily feeding with Lr 231 improved the body weight of male Wistar rats compared with control groups. Fecal azoreductase (p < 0.001) and nitroreductase (p < 0.01) enzyme activity decreased significantly in Lr 231 group in comparison with control groups that received only phosphate buffer or MNNG. Oral administration of MNNG led to a significant increase in Glutathione transferase (GST) while Glutathione reductase (GSH) showed decreased activity. Conversely, feeding Lr 231 showed significantly increased GSH and decreased GST activity in comparison to the MNNG group, emphasizing the protection provided by Lr 231 against MNNG. Histopathological analysis of liver, spleen and colon showed decreased signs of inflammation in the Lr 231 group. The present study highlights that inclusion of active Lr 231 in regular diets could be used to prevent MNNG induced colon carcinoma.

Chauhan C.K.,Saurashtra University | Joshi M.J.,Saurashtra University
Journal of Crystal Growth | Year: 2013

The formation of urinary stones, known as nephrolithiasis or urolithiasis, is a serious, debilitating problem throughout the world. Struvite - NH 4MgPO4·6H2O, ammonium magnesium phosphate hexahydrate, is one of the components of urinary stones (calculi). Struvite crystals with different morphologies were grown by in vitro single diffusion gel growth technique with different growth parameters. The crystals were characterized by powder XRD, FT-IR, thermal analysis and dielectric study. The powder XRD results of struvite confirmed the orthorhombic crystal structure. The FT-IR spectrum proved the presence of water of hydration, metal-oxygen bond, N-H bond and P-O bond. For thermal analysis TGA, DTA and DSC were carried out simultaneously. The kinetic and thermodynamic parameters of dehydration/decomposition process were calculated. Vickers micro-hardness and related mechanical parameters were also calculated. The in vitro growth inhibition studies of struvite by the juice of Citrus medica Linn as well as the herbal extracts of Commiphora wightii, Boerhaavia diffusa Linn and Rotula aquatica Lour were carried out and found potent inhibitors of struvite. © 2011 Elsevier B.V.

Anoxybacillus beppuensis TSSC-1 (GenBank Number, EU710556), a thermophilic bacterium isolated from a hot spring reservoir, was found to optimally secrete a monomeric α-amylase at 55 °C and pH 7. The enzyme was purified to homogeneity by a single-step purification on phenyl sepharose 6FF, achieving a 58% yield, 10,000 U/mg specific activity and 19.5 fold purification. The molecular weight, Km and Vmax were 43 kD, 0.5 mg ml -1 and 3571.42 μmol ml-1 m-1, respectively. The enzymatic catalysis of soluble starch was optimum at 80 °C and pH 7. The thermodynamic parameters, Kd, t1/2, ΔH*, ΔS*, E and ΔG*, were consistent. The very compact structure of the enzyme and the transitional enzyme-substrate complex resisted denaturation at extreme temperatures and alkaline pH. The Kd and t1/2 measurements were consistent with the high thermostability and pH tolerance observed. The structural stability of the enzyme was also reflected by the values of ΔH*, ΔS*, E and ΔG*. While the enzyme did not exhibit metal ion dependency, it was resistant to chemical denaturation. The broad thermo- and pH-tolerance of this enzyme suggests potential commercial opportunities. © 2012 Elsevier Ltd.

Bhalodia J.A.,Saurashtra University | Mankadia S.R.,Saurashtra University
Solid State Phenomena | Year: 2014

A systematic investigation of neodymium-based manganite, Nd0.7Sr0.3MnO3 (NSMO), was undertaken with a view to understand the influence of sintering temperature on various physical properties. The materials were prepared by the a soft chemical approach of co-precipitation method by sintering at four different temperatures starting from 700 to 1000 °C, with an interval of 100 °C. X-ray diffraction (XRD), transmission electron microscopy (TEM) and D. C. four-probe resistivity were employed to study the crystal structure, average particle size and electrical property respectively. Analysis of XRD patterns shows that all the samples exhibit single phase orthorhombic crystal structure. We followed William-son Hall approach to calculate the lattice stain (ε).These materials were found to exhibit different metal-insulator transition temperature (TMI) for the different sintering temperature. The value of TMI increases, as the sintering temperature increases, whereas ε decreases. TEM results show that with the increment of sintering temperature, the particle size of the NSMO samples also increases, which plays a key role on electrical transport. To understand the conduction mechanism in metallic and insulating regions of resistivity, various theoretical models are discussed in this communication. © (2014) Trans Tech Publications, Switzerland.

Kumar S.,Saurashtra University
International Journal of Pharma and Bio Sciences | Year: 2011

In this study, chlorpyrifos degrading capability of four bacterial monocultures (RCC-2, GCC-1, GCC-3 and JCC-3) and two bacterial mixed-cultures (GCE345 and GCC134) was investigated in terms of treatment duration and culture volume, using soil slurry medium. Among the bacterial mono-cultures, RCC-2 was found to be most efficient with 21, 37, 54 and 77% of chlorpyrifos degradation in 5, 10, 15 and 30 days of treatment duration, respectively. Out of two bacterial mixed-cultures, GCC134 was more effective and resulted in 24, 38, 56 and 85% degradation of chlorpyrifos in 5, 10, 15 and 30 days of treatment, respectively. Chlorpyrifos degradation was higher by increasing the culture volume of respective bacterial cultures, from 10% to 25% (v/v), for 10 days of treatment at room temperature. The Pearson correlation between treatment duration and % degradation of chlorpyrifos were 0.953 and 0.988 with bacterial mono- and mixed-cultures, respectively.

Gohel S.D.,Saurashtra University | Singh S.P.,Saurashtra University
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences | Year: 2012

An alkaline protease from salt tolerant alkaliphilic actinomycetes, Nocardiopsis alba strain OK-5 was purified to homogeneity by 27 and 13 fold with a yield of 35 and 13% using two-steps and one-step method, respectively. The purification methods involved hydrophobic interaction on phenyl sapharose matrix. The apparent molecular mass was 20kDa. The temperature optimum shifted from 70 to 80°C in 4M NaCl and 30% Na-glutamate, with significant stability at 60-80°C in Na-glutamate. Deactivation rate constant (K d) increased and half life (t 1/2) decreased with the increasing temperatures from 37 to 80°C. The order of stability was: 30% Na-glutamate>4M NaCl>2M NaCl>0M NaCl. The enzyme was stable even at 80°C in 30% Na-glutamate with K d 4.11 and t 1/2 168.64min. The activation energies (E), enthalpy (ΔH*) and entropy (ΔS*) for protease deactivation in with Na-glutamate were 31.97kJ/mole, 29.23kJ/mole and -211.83J/mole, respectively. The change in free energy (ΔG*) for protease deactivation at 60°C in 30% Na-glutamate was 101.70kJ/mole. Protease had the highest activity and stability at pH 10-11. While the enzyme was highly resistant against chemical denaturation, it had varied responses to metal ions. Complete inhibition by PMSF confirmed serine nature of the protease. Na-glutamate, H 2O 2, β-mercaptoethanol and different surfactants enhanced the activity. © 2012 Elsevier B.V.

Gohel S.D.,Saurashtra University | Singh S.P.,Saurashtra University
International Journal of Biological Macromolecules | Year: 2015

An alkaline protease from salt-tolerant alkaliphilic actinomycetes, Nocardiopsis alba OK-5 was purified by a single-step hydrophobic interaction chromatography and characterized. The purified protease with an estimated molecular mass of 20kDa was optimally active at 70°C in 0-3M NaCl and 0-100mM Ca2+ displaying significant stability at 50-80°C. The enzyme was stable at 80°C in 100mM Ca2+ with Kd of 17×10-3 and t1/2 of 32min. The activation energy (Ea), enthalpy (δH*), and entropy (δS*) for the protease deactivation calculated in the presence of 200mM Ca2+ were 38.15kJ/mol, 35.49kJ/mol and 183.48J/mol, respectively. The change in free energy (δG*) for protease deactivation at 60°C in 200mM Ca2+ was 95.88kJ/mol. Decrease in δH* reflected reduced cooperativity of deactivation and unfolding. The enzyme was intrinsically stable that counteracted heat denaturation by a weak cooperativity during the unfolding. Further, the enzyme was highly stable in the presence of various cations, surfactants, H2O2, β-mercaptoethanol, and commercial detergents. The compatibility of the enzyme with various cations, surfactants, and detergent matrices suggests its suitability as an additive in the detergents and peptide synthesis. © 2014 Elsevier B.V.

Kikani B.A.,Saurashtra University | Singh S.P.,Saurashtra University
International Journal of Biological Macromolecules | Year: 2011

A thermophilic bacteria, identified and designated as Bacillus amyloliquifaciens TSWK1-1 (16S rRNA gene sequence, GenBank: GQ121033), was isolated from a hot water reservoir located at Tulsi Shyam, Gujarat, India. The optimum temperature and pH for amylase production were 50°C and 7.0, respectively. The crude enzyme was partially purified by ammonium sulphate fractionation followed by dialysis. However, single step purification was achieved on Phenyl Sepharose 6FF affinity column with 45.71% yield, 8000U/mg specific activity and 13.33 fold purification. The molecular weight of the purified α-amylase was 43kD. The optimal temperature and pH for amylase activity were 70°C and 7.0, respectively; however, the purified amylase was stable at broad temperature and pH range. The purified amylase did not require Ca++ and K+; however, it was moderately affected by Mg++ and Cu++ and significantly inhibited by Na+ and Fe++. The amylase was highly thermostable and remained active for 24h at 60°C, for 12h at 70°C and up to 3h even at 90°C. Other unique features of the enzyme were calcium independent nature and resistance against chemical denaturation by Urea and Guanidine-HCl. The data on the enzymatic stability at different levels of purity would add significantly to the knowledge of amylases. © 2011 Elsevier B.V.

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