Growth and biochemical characterization of associations between cyanobionts and wheat seedlings in co-culturing experiments

Biologia ◽  
2011 ◽  
Vol 66 (1) ◽  
Author(s):  
Anjuli Sood ◽  
Pawan Singh ◽  
Arun Kumar ◽  
Rajendra Singh ◽  
Radha Prasanna
Keyword(s):  
Amino Acids ◽  
Indoleacetic Acid ◽  
Biochemical Characterization ◽  
Shoot Biomass ◽  
Wheat Seedlings ◽  
Symbiotic Associations ◽  
Plant Groups ◽  
Wide Range ◽  
Root And Shoot Biomass

AbstractN2-fixing cyanobacteria are unique in their capacity to form symbiotic associations with a wide range of eukaryotic hosts belonging to different plant groups. The present study was undertaken to analyze the interactions of the cyanobiont PI 01 (from Azolla pinnata) and Nostoc PCC 9229 (from Gunnera monoika) with wheat seedlings, in co-culturing experiments. Each of the cyanobionts enhanced significantly the volume of root and shoot biomass in the experimental cultures. The transverse sections of roots in the co-cultured seedlings revealed the presence of aseriate packets of cyanobionts below the root epidermis. The investigated cyanobionts excreted amino acids (His, Met, Val) and sugars into the medium, while indoleacetic acid was detected when the cyanobionts were grown in a tryptophan containing medium. During the co-culturing, sugars and proline were detected in the extracellular filtrates. It can be hypothesized that these sugars and amino acids may serve as signal substances in the development of functional associations between the relevant cyanobionts and the wheat seedlings.

scholarly journals Phenotypic, Genetic and Biochemical Characterization of Five Tunisian Varieties of Chickpea

2017 ◽  
Vol 5 (1) ◽  
pp. 77 ◽  
Author(s):  
Mongi Melki ◽  
Abir Gsouri ◽  
Mariem Bouhadida ◽  
Hnya Chograni ◽  
Mohsen Rezgui
Keyword(s):  
Amino Acids ◽  
Biochemical Characterization ◽  
Block Design ◽  
Field Trials ◽  
Morphological Characters ◽  
Yield Potential ◽  
Polymorphism Analysis ◽  
Sulfur Amino Acids ◽  
Semi Arid Region

Five Tunisian varieties of Kabuli chickpea were characterized based on agro morphological, molecular and biochemical parameters to investigate their genetic variability and yield potential. Randomized complete block design field trials were carried out in the upper semi-arid region of Kef in Tunisia during the 2013-2014 seasons. Data analysis showed significant differences between genotypes for several parameters. The results indicated that these genotypes could be set into two different groups. The first group composed of Bochra and Chetoui genotypes. Kasseb, Neyer and Beja1 were in the second group. Genotypes in each group were closely related to each other according to their common morphological characters such as pod number, one hundred seeds weight and yield.  Chetoui and Kasseb varieties are later in comparison to other varieties. Genetic diversity was studied using simple sequence repeat (SSR) markers. Four loci (TA64, TA71, TA96, TA194) were multiallelic. Whereas while two loci (TA72, GAA47) were monomorphic. Polymorphism analysis showed a phylogeny related to genotypes differentiation according to their relatives, origin and several morphological characters. Bochra variety had high amino acids content followed by Chetoui variety. All the varieties were deficient in sulfur amino acids. Chickpeas protein contents were variable and high ranging from 18% to 25%.

Biochemical Characterization of Branched Chain Amino Acids Uptake in Trypanosoma cruzi

2015 ◽  
Vol 63 (3) ◽  
pp. 299-308 ◽  
Author(s):  
Nubia C. Manchola ◽  
Ludmila N. Rapado ◽  
María J. Barisón ◽  
Ariel M. Silber
Keyword(s):  
Amino Acids ◽  
Trypanosoma Cruzi ◽  
Biochemical Characterization ◽  
Branched Chain Amino Acids ◽  
Branched Chain

scholarly journals Genetic and Biochemical Characterization of OXA-535, a Distantly Related OXA-48-Like β-Lactamase

2018 ◽  
Vol 62 (10) ◽  
Author(s):  
L. Dabos ◽  
A. B. Jousset ◽  
R. A. Bonnin ◽  
N. Fortineau ◽  
A. Zavala ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Content Type ◽  
Sequence Identity

ABSTRACT OXA-535 is a chromosome-encoded carbapenemase of Shewanella bicestrii JAB-1 that shares only 91.3% amino acid sequence identity with OXA-48. Catalytic efficiencies are similar to those of OXA-48 for most β-lactams, except for ertapenem, where a 2,000-fold-higher efficiency was observed with OXA-535. OXA-535 and OXA-436, a plasmid-encoded variant of OXA-535 differing by three amino acids, form a novel cluster of distantly related OXA-48-like carbapenemases. Comparison of blaOXA-535 and blaOXA-436 genetic environments suggests that an ISCR1 may be responsible for blaOXA-436 gene mobilization from the chromosome of Shewanella spp. to plasmids.

Discovery and Biocatalytic Application of a PLP-Dependent Amino Acid γ-Substitution Enzyme that Catalyzes C-C Bond Formation

2020 ◽  
Author(s):  
Mengbin Chen ◽  
Chun-Ting Liu ◽  
Yi Tang
Keyword(s):  
Amino Acids ◽  
Biosynthetic Pathway ◽  
Pyridoxal Phosphate ◽  
Biochemical Characterization ◽  
Indole Alkaloid ◽  
Building Blocks ◽  
Nucleophilic Attack ◽  
Keto Esters ◽  
Key Enzyme

Pyridoxal phosphate (PLP)-dependent enzymes can catalyze various transformations of amino acids at alpha, beta, and gamma positions. These versatile enzymes are prominently involved in the biosynthesis of nonproteinogenic amino acids as building blocks of natural products, and are attractive biocatalysts. Here, we report the discovery of a two-step enzymatic synthesis of (2<i>S, </i>6<i>S</i>)-6-methyl pipecolate <b>1</b>, from the biosynthetic pathway of indole alkaloid citrinadin. The key enzyme CndF is PLP-dependent and catalyzes synthesis of (<i>S</i>)-2-amino-6-oxoheptanoate <b>3</b> that is in equilibrium with the cyclic Schiff base. The second enzyme CndE is a stereoselective imine reductase that gives <b>1</b>. Biochemical characterization of CndF showed this enzyme performs gamma-elimination of <i>O</i>-acetyl L-homoserine to generate the vinylglycine ketimine, which is subjected to nucleophilic attack by acetoacetate to form the new C<sub>gamma</sub>-C<sub>delta</sub> bond in <b>3 </b>and complete the gamma-substitution reaction. CndF displays substrate promiscuity towards different beta-keto carboxylate and esters. Using a recombinant <i>Aspergillus </i>strain expressing CndF and CndE, feeding various alkyl-beta-keto esters led to the biosynthesis of 6-substituted L-pipecolates. The discovery of CndF expands the repertoire of reactions that can be catalyzed by PLP-dependent enzymes.

Plant ABC transporters: time for biochemistry?

2015 ◽  
Vol 43 (5) ◽  
pp. 931-936 ◽  
Author(s):  
François Lefèvre ◽  
Amandine Baijot ◽  
Marc Boutry
Keyword(s):  
Abc Transporters ◽  
Biochemical Characterization ◽  
Direct Methods ◽  
Membrane Transporters ◽  
Current Status ◽  
Isolated Cells ◽  
Abc Proteins ◽  
Physiological Processes ◽  
Wide Range

ATP-binding cassette (ABC) proteins form a large and ubiquitous family, most members of which are membrane-associated primary transporters. Plant genomes code for a particularly large number of these ABC proteins, with more than 120 genes present in both Arabidopsis thaliana and Oryza sativa (rice). Although plant ABC transporters were initially identified as detoxifiers, sequestering xenobitotics into the vacuole, they were later found to be involved in a wide range of essential physiological processes. Currently, the exact substrates transported by most of these transporters are still unknown and we therefore cannot exclude that a single substrate (e.g. a hormone) is responsible for the diversity of physiological roles. This gap in our knowledge is mainly due to the fact that only a few studies have used direct methods to identify the substrates of these membrane transporters. To address this issue, transport assays involving isolated cells, vesicular membranes or reconstituted liposomes are essential. In this review, we will highlight the importance of the direct biochemical characterization of plant ABC transporters and give some insights into the current status of the homologous and heterologous expression of such proteins.

scholarly journals A multifunctional GH39 glycoside hydrolase from the anaerobic gut fungus Orpinomyces sp. strain C1A

2016 ◽  
Author(s):  
Jessica M Morrison ◽  
Mostafa S Elshahed ◽  
Noha Youssef
Keyword(s):  
Active Site ◽  
Glycoside Hydrolase ◽  
Biochemical Characterization ◽  
Xylanase Activity ◽  
Comparative Modeling ◽  
Glycoside Hydrolase Family ◽  
Wide Range ◽  
Promising Source ◽  
Substrate Competition

Background. The anaerobic gut fungi (phylum Neocallimastigomycota) represent a promising source of novel lignocellulolytic enzymes. Here, we report on the cloning, expression, and characterization of a glycoside hydrolase family 39 (GH39) enzyme (Bgxg1) that is highly transcribed by the anaerobic fungus Orpinomyces sp. strain C1A under different growth conditions. This represents the first study of a GH39-family enzyme from the anaerobic fungi. Methods. Using enzyme activity assays, we performed a biochemical characterization of Bgxg1 on a variety of substrates over a wide range of pH and temperature values to identify the optimal enzyme conditions and the specificity of the enzyme. In addition, substrate competition studies and comparative modeling efforts were completed. Results. Contrary to the narrow range of activities (β-xylosidase or α-L-iduronidase) observed in previously characterized GH39 enzymes, Bgxg1 is unique in that it is multifunctional, exhibiting strong β-xylosidase, β-glucosidase, β-galactosidase activities (11.5 ± 1.2, 73.4 ± 7.15, and 54.6 ± 2.26 U/mg, respectively) and a weak xylanase activity (10.8 ± 1.25 U/mg), strength determined as compared to previously characterized enzymes. Physiological characterization revealed that Bgxg1 is active over a wide range of pH (3-8, optimum 6) and temperatures (25-60°C, optimum 39°C), and possesses excellent temperature and thermal stability. Substrate competition assays suggest that all observed activities occur at a single active site. Using comparative modeling and bioinformatics approaches, we putatively identified ten amino acid differences between Bgxg1 and previously biochemically characterized GH39 β-xylosidases that we speculate could impact active site architecture, size, charge, and/or polarity. The putative contributions of these changes to the observed relaxed specificities in Bgxg1 are discussed. Discussion. Collectively, the unique capabilities and multi-functionality of Bgxg1 render it an excellent candidate for inclusion in enzyme cocktails mediating cellulose and hemicellulose saccharification from lignocellulosic biomass.

scholarly journals BIOCHEMICAL CHARACTERIZATION OF Ferula rutbaensis MEDICINAL PLANT IN IRAQI WESTERN DESERT

2020 ◽  
Vol 17 (36) ◽  
pp. 831-844
Author(s):  
Kutayba Farhan DAWOOD ◽  
Ayoob Obaid ALFALAHI ◽  
Shamil Ismail NEAMAH ◽  
Omar Mahmood DHANNOON
Keyword(s):  
Fatty Acids ◽  
Bioactive Compounds ◽  
Unsaturated Fatty Acids ◽  
Biochemical Characterization ◽  
Western Desert ◽  
Morphological Identification ◽  
Plant Parts ◽  
Methanolic Extracts ◽  
Wide Range

Plants used in folk medicine not only represent rich sources for therapeutic materials, but it also plays a crucial role in developing completely or partially novel synthesized drugs. Mharut plant (Ferula rutbaensis) is an integral part of Bedouin therapeutic practices in the western desert of Anbar province-Iraq. Still, to date, this is the first study describing its phytochemical constituents. The plant was growing near the Iraq-Saudi Arabia borders and adapted to a wide range of soils. Traditionally, F. rutbaensis has been widely used to treat acne, stomach and bowel disorders, food poisoning and respiratory problems. Fresh plant samples were collected and morphologically characterized. Likewise, the ITS-based DNA barcoding technique was efficiently used to approve the morphological identification of F. rutbaensis. The GC-MS spectrum was adopted in the phytochemical characterization of aqueous and methanol extracts of fresh and dry plant parts. The aqueous extract of dry roots was the richest source for bioactive compounds than fresh or methanolic extracts of either fresh or dry plant parts. In general, the detected phytochemicals falling into fatty acids, terpenes, hydrocarbon alkanes, and esters. Notably, fatty acids in Oleic and Palmitic acids were the two most abundant bioactive compounds in both aqueous and methanolic extracts of plant fresh and dry roots. The detected unsaturated fatty acids and/or other bioactive components are laying behind the therapeutic properties of F. rutbaensis that can be useful ingredients to prepare Mharut-based cosmetics such as medical soaps, body lotions, skin conditioners and sunscreens. Additionally, some other components were found to have anti-inflammatory, antioxidants, and antimicrobial properties. Further investigations will be necessary to confirm the antimicrobial activity of F. rutbaensis extracts.

Biochemical characterization of thermostable ω-transaminase from Sphaerobacter thermophilus and its application for producing aromatic β- and γ-amino acids

2016 ◽  
Vol 87-88 ◽  
pp. 52-60 ◽  
Author(s):  
Sam Mathew ◽  
Saravanan Prabhu Nadarajan ◽  
Taeowan Chung ◽  
Hyun Ho Park ◽  
Hyungdon Yun
Keyword(s):  
Amino Acids ◽  
Biochemical Characterization

scholarly journals Adsorption to soils and biochemical characterization of purified phytases

2019 ◽  
Author(s):  
Maria Marta Caffaro ◽  
Karina Beatriz Balestrasse ◽  
Gerardo Rubio
Keyword(s):  
Phytic Acid ◽  
Crop Production ◽  
Biochemical Characterization ◽  
Solid Phase ◽  
Organic P ◽  
E Coli ◽  
Nitrophenyl Phosphate ◽  
Wide Range ◽  
Temperature Ranges

Abstract. Four purified phytases isolated from Aspergillus niger and Escherichia coli were characterized biochemically and in terms of their adsorption to soils belonging to the Mollisol order. Three different organic P substrates were used to measure enzyme activity in a wide range of pH (2.3 to 9) and temperatures (−10° to 70 °C): p-nitrophenyl-phosphate, glyceraldehyde-3-phosphate and phytic acid. Phytases from A. niger showed a higher capacity to release P (36 to 50 % of P contained in the substrates, 44 to 62 μg P), than phytases from E. coli (24 to 36 %, 20 to 44 μg P). The amount of P released from organic P substrates by A. niger phytases followed the following range: p-nitrophenyl-phosphate > glyceraldehyde-3-phosphate > phytic acid whereas in E. coli phytases the order was p-nitrophenyl-phosphate/glyceraldehyde-3-phosphate > phytic acid. All phytases were active throughout the pH and temperature ranges for optimum crop production. The proportion of phytases found in the solid phase of the soil 60 minutes after addition was lower than that found in the liquid phase (23–34 % vs. 66–77 %). Obtained results are promising in terms of the use of phytases as a complement to P fertilization in agricultural settings and encourages further studies under field conditions.

scholarly journals Isolation and preliminary biochemical characterization of the gonococcal H.8 antigen.

1986 ◽  
Vol 164 (6) ◽  
pp. 2038-2048 ◽  
Author(s):  
W Strittmatter ◽  
P J Hitchcock
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Preliminary Analysis ◽  
Chemical Nature ◽  
Biochemical Characterization ◽  
Sulfur Containing ◽  
Lipid Components

We have presented a method for the extraction and isolation of the gonococcal H.8 antigen. There was no evidence of contamination by other gonococcal proteins, phospholipids, or LPS. The purified H.8 antigen was subjected to preliminary analysis and appeared to be a proteolipid consisting of both protein and lipid components. The amino acid composition was unusual; the peptide portion of the antigen was an alanine and proline-rich molecule that lacked aromatic and sulfur-containing amino acids. The overall amino acid composition is hydrophobic. A lipid constituent was also identified; it was made up of at least two lipid components, which were unique to the H.8 molecule. The chemical nature of the association of the protein and lipid is presently unknown, but it is clearly a tenacious one.

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