The Experts below are selected from a list of 306 Experts worldwide ranked by ideXlab platform

J C Tarafdar - One of the best experts on this subject based on the ideXlab platform.

  • tio2 nanoparticle biosynthesis and its Physiological Effect on mung bean vigna radiata l
    Biotechnology Reports, 2015
    Co-Authors: Ramesh Raliya, Pratim Biswas, J C Tarafdar
    Abstract:

    A B S T R A C T TiO2 nanoparticle (NPs) biosynthesis is a low cost, ecofriendly approach developed using the fungi Aspergillus flavus TFR 7. To determine whether TiO2 NPs is suitable for nutrient, we conducted a two part study; biosynthesis of TiO2 NP and evaluates their influence on mung bean. The characterized TiO2 NPs were foliar sprayed at 10 mgL � 1 concentration on the leaves of 14 days old mung bean plants. A significant improvement was observed in shoot length (17.02%), root length (49.6%), root area (43%), root nodule (67.5%), chlorophyll content (46.4%) and total soluble leaf protein (94%) as a result of TiO2NPs application. In the rhizosphere microbial population increased by 21.4–48.1% and activity of acid phosphatase (67.3%), alkaline phosphatase (72%), phytase (64%) and dehydrogenase (108.7%) enzyme was observed over control in six weeks old plants owing to application of TiO2 NPs. A possible mechanism has also been hypothesized for TiO2 NPs biosynthesis. a 2014 Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://

Ludmila Chistoserdova - One of the best experts on this subject based on the ideXlab platform.

  • Physiological Effect of xoxg 4 on lanthanide dependent methanotrophy
    Mbio, 2018
    Co-Authors: Yue Zheng, Jing Huang, Feng Zhao, Ludmila Chistoserdova
    Abstract:

    ABSTRACT A recent surprising discovery of the activity of rare earth metals (lanthanides) as enzyme cofactors as well as transcriptional regulators has overturned the traditional assumption of biological inertia of these metals. However, so far, examples of such activities have been limited to alcohol dehydrogenases. Here we describe the Physiological Effects of a mutation in xoxG, a gene encoding a novel cytochrome, XoxG(4), and compare these to the Effects of mutation in XoxF, a lanthanide-dependent methanol dehydrogenase, at the enzyme activity level and also at the community function level, using Methylomonas sp. strain LW13 as a model organism. Through comparative phenotypic characterization, we establish XoxG as the second protein directly involved in lanthanide-dependent metabolism, likely as a dedicated electron acceptor from XoxF. However, mutation in XoxG caused a phenotype that was dramatically different from the phenotype of the mutant in XoxF, suggesting a secondary function for this cytochrome, in metabolism of methane. We also purify XoxG(4) and demonstrate that this protein is a true cytochrome c, based on the typical absorption spectra, and we demonstrate that XoxG can be directly reduced by a purified XoxF, supporting one of its proposed Physiological functions. Overall, our data continue to suggest the complex nature of the interplay between the calcium-dependent and lanthanide-dependent alcohol oxidation systems, while they also suggest that addressing the roles of these alternative systems is essential at the enzyme and community function level, in addition to the gene transcription level. IMPORTANCE The lanthanide-dependent biochemistry of living organisms remains a barely tapped area of knowledge. So far, only a handful of lanthanide-dependent alcohol dehydrogenases have been described, and their regulation by lanthanides has been demonstrated at the transcription level. Little information is available regarding the concentrations of lanthanides that could support sufficient enzymatic activities to support specific metabolisms, and so far, no other redox proteins involved in lanthanide-dependent methanotrophy have been demonstrated. The research presented here provides enzyme activity-level data on lanthanide-dependent methanotrophy in a model methanotroph. Additionally, we identify a second protein important for lanthanide-dependent metabolism in this organism, XoxG(4), a novel cytochrome. XoxG(4) appears to have multiple functions in methanotrophy, one function as an electron acceptor from XoxF and another function remaining unknown. On the basis of the dramatic phenotype of the XoxG(4) mutant, this function must be crucial for methanotrophy.

  • Physiological Effect of XoxG(4) on Lanthanide-Dependent Methanotrophy
    American Society for Microbiology, 2018
    Co-Authors: Yue Zheng, Jing Huang, Feng Zhao, Ludmila Chistoserdova, Stephen Giovannoni
    Abstract:

    A recent surprising discovery of the activity of rare earth metals (lanthanides) as enzyme cofactors as well as transcriptional regulators has overturned the traditional assumption of biological inertia of these metals. However, so far, examples of such activities have been limited to alcohol dehydrogenases. Here we describe the Physiological Effects of a mutation in xoxG, a gene encoding a novel cytochrome, XoxG(4), and compare these to the Effects of mutation in XoxF, a lanthanide-dependent methanol dehydrogenase, at the enzyme activity level and also at the community function level, using Methylomonas sp. strain LW13 as a model organism. Through comparative phenotypic characterization, we establish XoxG as the second protein directly involved in lanthanide-dependent metabolism, likely as a dedicated electron acceptor from XoxF. However, mutation in XoxG caused a phenotype that was dramatically different from the phenotype of the mutant in XoxF, suggesting a secondary function for this cytochrome, in metabolism of methane. We also purify XoxG(4) and demonstrate that this protein is a true cytochrome c, based on the typical absorption spectra, and we demonstrate that XoxG can be directly reduced by a purified XoxF, supporting one of its proposed Physiological functions. Overall, our data continue to suggest the complex nature of the interplay between the calcium-dependent and lanthanide-dependent alcohol oxidation systems, while they also suggest that addressing the roles of these alternative systems is essential at the enzyme and community function level, in addition to the gene transcription level

Yue Zheng - One of the best experts on this subject based on the ideXlab platform.

  • Physiological Effect of xoxg 4 on lanthanide dependent methanotrophy
    Mbio, 2018
    Co-Authors: Yue Zheng, Jing Huang, Feng Zhao, Ludmila Chistoserdova
    Abstract:

    ABSTRACT A recent surprising discovery of the activity of rare earth metals (lanthanides) as enzyme cofactors as well as transcriptional regulators has overturned the traditional assumption of biological inertia of these metals. However, so far, examples of such activities have been limited to alcohol dehydrogenases. Here we describe the Physiological Effects of a mutation in xoxG, a gene encoding a novel cytochrome, XoxG(4), and compare these to the Effects of mutation in XoxF, a lanthanide-dependent methanol dehydrogenase, at the enzyme activity level and also at the community function level, using Methylomonas sp. strain LW13 as a model organism. Through comparative phenotypic characterization, we establish XoxG as the second protein directly involved in lanthanide-dependent metabolism, likely as a dedicated electron acceptor from XoxF. However, mutation in XoxG caused a phenotype that was dramatically different from the phenotype of the mutant in XoxF, suggesting a secondary function for this cytochrome, in metabolism of methane. We also purify XoxG(4) and demonstrate that this protein is a true cytochrome c, based on the typical absorption spectra, and we demonstrate that XoxG can be directly reduced by a purified XoxF, supporting one of its proposed Physiological functions. Overall, our data continue to suggest the complex nature of the interplay between the calcium-dependent and lanthanide-dependent alcohol oxidation systems, while they also suggest that addressing the roles of these alternative systems is essential at the enzyme and community function level, in addition to the gene transcription level. IMPORTANCE The lanthanide-dependent biochemistry of living organisms remains a barely tapped area of knowledge. So far, only a handful of lanthanide-dependent alcohol dehydrogenases have been described, and their regulation by lanthanides has been demonstrated at the transcription level. Little information is available regarding the concentrations of lanthanides that could support sufficient enzymatic activities to support specific metabolisms, and so far, no other redox proteins involved in lanthanide-dependent methanotrophy have been demonstrated. The research presented here provides enzyme activity-level data on lanthanide-dependent methanotrophy in a model methanotroph. Additionally, we identify a second protein important for lanthanide-dependent metabolism in this organism, XoxG(4), a novel cytochrome. XoxG(4) appears to have multiple functions in methanotrophy, one function as an electron acceptor from XoxF and another function remaining unknown. On the basis of the dramatic phenotype of the XoxG(4) mutant, this function must be crucial for methanotrophy.

  • Physiological Effect of XoxG(4) on Lanthanide-Dependent Methanotrophy
    American Society for Microbiology, 2018
    Co-Authors: Yue Zheng, Jing Huang, Feng Zhao, Ludmila Chistoserdova, Stephen Giovannoni
    Abstract:

    A recent surprising discovery of the activity of rare earth metals (lanthanides) as enzyme cofactors as well as transcriptional regulators has overturned the traditional assumption of biological inertia of these metals. However, so far, examples of such activities have been limited to alcohol dehydrogenases. Here we describe the Physiological Effects of a mutation in xoxG, a gene encoding a novel cytochrome, XoxG(4), and compare these to the Effects of mutation in XoxF, a lanthanide-dependent methanol dehydrogenase, at the enzyme activity level and also at the community function level, using Methylomonas sp. strain LW13 as a model organism. Through comparative phenotypic characterization, we establish XoxG as the second protein directly involved in lanthanide-dependent metabolism, likely as a dedicated electron acceptor from XoxF. However, mutation in XoxG caused a phenotype that was dramatically different from the phenotype of the mutant in XoxF, suggesting a secondary function for this cytochrome, in metabolism of methane. We also purify XoxG(4) and demonstrate that this protein is a true cytochrome c, based on the typical absorption spectra, and we demonstrate that XoxG can be directly reduced by a purified XoxF, supporting one of its proposed Physiological functions. Overall, our data continue to suggest the complex nature of the interplay between the calcium-dependent and lanthanide-dependent alcohol oxidation systems, while they also suggest that addressing the roles of these alternative systems is essential at the enzyme and community function level, in addition to the gene transcription level

Ramesh Raliya - One of the best experts on this subject based on the ideXlab platform.

  • tio2 nanoparticle biosynthesis and its Physiological Effect on mung bean vigna radiata l
    Biotechnology Reports, 2015
    Co-Authors: Ramesh Raliya, Pratim Biswas, J C Tarafdar
    Abstract:

    A B S T R A C T TiO2 nanoparticle (NPs) biosynthesis is a low cost, ecofriendly approach developed using the fungi Aspergillus flavus TFR 7. To determine whether TiO2 NPs is suitable for nutrient, we conducted a two part study; biosynthesis of TiO2 NP and evaluates their influence on mung bean. The characterized TiO2 NPs were foliar sprayed at 10 mgL � 1 concentration on the leaves of 14 days old mung bean plants. A significant improvement was observed in shoot length (17.02%), root length (49.6%), root area (43%), root nodule (67.5%), chlorophyll content (46.4%) and total soluble leaf protein (94%) as a result of TiO2NPs application. In the rhizosphere microbial population increased by 21.4–48.1% and activity of acid phosphatase (67.3%), alkaline phosphatase (72%), phytase (64%) and dehydrogenase (108.7%) enzyme was observed over control in six weeks old plants owing to application of TiO2 NPs. A possible mechanism has also been hypothesized for TiO2 NPs biosynthesis. a 2014 Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://

Chunyang Zhang - One of the best experts on this subject based on the ideXlab platform.

  • Physiological Effect of anatase tio2 nanoparticles on lemna minor
    Environmental Toxicology and Chemistry, 2012
    Co-Authors: Guanling Song, Yuan Gao, Wenhua Hou, Chunyang Zhang
    Abstract:

    Manufactured metal oxide nanoparticles (NPs) are being used on a large scale, and these particles will inevitably reach a body of water through wastewater and urban runoff. The ecotoxicological study of these NPs on hydrophyte is limited at present. Lemna minor was exposed to media with different concentrations of titanium dioxide (TiO(2)) NPs or bulk TiO(2) for 7 d. The changes in plant growth, chlorophyll, antioxidant defense enzymes (peroxidase [POD], catalase [CAT], and superoxide dismutase [SOD] activities), and malondialdehyde (MDA) content were measured in the present study. The particle size of TiO(2) NPs and the zeta potential of TiO(2) NPs and of bulk TiO(2) in the culture media were also analyzed to complementally study the toxicity of these materials on duckweed. The results showed that the Effect of TiO(2) NPs on plant growth was more obvious than bulk TiO(2.) Titanium dioxide NPs stimulated plant growth in low concentrations, but inhibited plant growth at high concentrations. The POD, SOD, and CAT activity of Lemna minor increased when TiO(2) NP concentration was lower than 200 mg/L to eliminate accumulated reactive oxygen species in plant cells. The SOD activity decreased when the TiO(2) NP concentration was higher than 200 mg/L, and the plant cell membrane encountered serious damage from 500 mg/L TiO(2) NP concentration in the culture media.