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1.
Environ Res ; 259: 119527, 2024 Jul 06.
Artículo en Inglés | MEDLINE | ID: mdl-38977155

RESUMEN

The wastewater produced during coffee cherry pulping is known for containing harmful pollutants, particularly organic compounds containing carbon, which pose significant risks to the environment and human health. This research aimed to evaluate the effectiveness of Tamarindus indica L. seed polysaccharides in treating coffee effluent. Varying doses (ranging from 0.05 to 0.30 g) of the isolated polysaccharides were added to samples of the effluent to determine their ability to remove contaminants, especially those of organic carbon origin. Notably, a dosage of 0.10 g demonstrated optimal efficacy, resulting in a 55% decrease in total dissolved solids and an 80% decrease in chemical oxygen demand. Additionally, Fourier-transform infrared and zeta potential analysis of both the polysaccharides and the treated effluent samples revealed the presence of functional groups potentially pivotal for the pollutant removal activity of the isolated polysaccharides. This provides insights into the coagulation mechanism of Tamarindus indica L. seed polysaccharides in eliminating organic carbon-based pollutants. These findings highlight the potential of Tamarindus polysaccharides as a sustainable alternative to chemical agents for removing pollutants, thus promoting environmental sustainability and human well-being.

2.
Acta Crystallogr Sect E Struct Rep Online ; 70(Pt 12): 580-3, 2014 Dec 01.
Artículo en Inglés | MEDLINE | ID: mdl-25552997

RESUMEN

The title mol-ecular salt, C8H13N2 (+)·Br(-), crystallizes with two independent 3-amino-pyridinium cations and two bromide anions in the asymmetric unit (Z' = 2). In the pyridine ring, the N atom is alkyl-ated by a propyl group. The dihedral angle between the mean planes of the pyridinium ring and the propyl group is 84.84 (2)° in cation A, whereas the corresponding angle is 89.23 (2)° in cation B. In the crystal, the anions and cations are linked via N-H⋯Br and C-H⋯Br hydrogen bonds, forming chains propagating along [100].

3.
J Mol Biol ; 324(4): 755-62, 2002 Dec 06.
Artículo en Inglés | MEDLINE | ID: mdl-12460575

RESUMEN

Phospholipase A(2) catalyses hydrolysis of the ester bond at the C2 position of 3-sn-phosphoglycerides. Here we report the 1.9A resolution crystal structure of the triple mutant K56,120,121M of bovine pancreatic phospholipase A(2). The structure was solved by molecular replacement method using the orthorhombic form of the recombinant phospholipase A(2). The final protein model contains all the 123 amino acid residues, two calcium ions, 125 water molecules and one 2-methyl-2-4-pentanediol molecule. The model has been refined to a crystallographic R-factor of 19.6% (R(free) of 25.9%) for all data between 14.2A and 1.9A. The residues 62-66, which are in a surface loop, are always disordered in the structures of bovine pancreatic phospholipase A(2) and its mutants. It is interesting to note that the residues 62-66 in the present structure is ordered and the conformation varies substantially from those in the previously published structures of this enzyme. An unexpected and interesting observation in the present structure is that, in addition to the functionally important calcium ion in the active site, one more calcium ion is found near the N terminus. Detailed structural analyses suggest that binding of the second calcium ion could be responsible for the conformational change and the ordering of the surface loop. Furthermore, the results suggest a structural reciprocity between the k(cat)(*) allosteric site and surface loop at the i-face, which represents a newly identified structural property of secreted phospholipase A(2).


Asunto(s)
Calcio/química , Modelos Moleculares , Páncreas/enzimología , Fosfolipasas A/química , Fosfolipasas A/genética , Sitio Alostérico , Secuencia de Aminoácidos , Animales , Calcio/metabolismo , Bovinos , Cristalografía por Rayos X , Escherichia coli , Glicoles/química , Hidrólisis , Cuerpos de Inclusión/química , Mutagénesis Sitio-Dirigida , Fosfolipasas A/metabolismo , Fosfolipasas A2 , Conformación Proteica , Estructura Secundaria de Proteína , Proteínas Recombinantes/química , Proteínas Recombinantes/aislamiento & purificación , Porcinos , Agua/química
4.
Artículo en Inglés | MEDLINE | ID: mdl-16508077

RESUMEN

The enzyme phospholipase A2 catalyzes the hydrolysis of the sn-2 acyl chain of phospholipids, forming fatty acids and lysophospholipids. The crystal structure of a triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 in which the lysine residues at positions 53, 56 and 121 are replaced recombinantly by methionines has been determined at atomic resolution (0.97 A). The crystal is monoclinic (space group P2), with unit-cell parameters a = 36.934, b = 23.863, c = 65.931 A, beta = 101.47 degrees. The structure was solved by molecular replacement and has been refined to a final R factor of 10.6% (Rfree = 13.4%) using 63,926 unique reflections. The final protein model consists of 123 amino-acid residues, two calcium ions, one chloride ion, 243 water molecules and six 2-methyl-2,4-pentanediol molecules. The surface-loop residues 60-70 are ordered and have clear electron density.


Asunto(s)
Páncreas/enzimología , Fosfolipasas A/química , Animales , Secuencia de Bases , Bovinos , Cristalografía por Rayos X , Cartilla de ADN , Liofilización , Enlace de Hidrógeno , Modelos Moleculares , Mutagénesis Sitio-Dirigida , Fosfolipasas A/genética , Fosfolipasas A2 , Conformación Proteica , Proteínas Recombinantes/química
5.
J Synchrotron Radiat ; 11(Pt 4): 358-62, 2004 Jul 01.
Artículo en Inglés | MEDLINE | ID: mdl-15211044

RESUMEN

Data from the alkaline cellulase apo form were collected at a resolution of 1.9 A using an in-house X-ray source (Cu K alpha). By using different fragments of helices from the model solved by macromolecular crystallographic means, the direct-methods program ACORN was used to arrive at the complete model. Attempts have been made to use various percentages of input phasing information from these helices. The minimum input phasing required in feeding the fragments was about 14% of the whole structure. The phases obtained from ACORN were of superb quality, allowing automated model building to be carried out using ARP/wARP. Minimal manual model building was required and the structure determination was completed using the maximum-likelihood refinement program REFMAC. The whole process, starting from the running of ACORN and ending with the refined model, took nearly 15 h of CPU time using a Pentium III PC.


Asunto(s)
Algoritmos , Celulasa/análisis , Celulasa/química , Modelos Moleculares , Programas Informáticos , Difracción de Rayos X/métodos , Simulación por Computador , Sustancias Macromoleculares , Peso Molecular , Conformación Proteica , Reproducibilidad de los Resultados , Sensibilidad y Especificidad
6.
J Synchrotron Radiat ; 11(Pt 1): 64-7, 2004 Jan 01.
Artículo en Inglés | MEDLINE | ID: mdl-14646136

RESUMEN

One of the main interests in the molecular biosciences is in understanding structure-function relations and X-ray crystallography plays a major role in this. ACORN can be used as a comprehensive and efficient phasing procedure for the determination of protein structures when atomic resolution data are available. An initial model can automatically be built by ARP/wARP followed by REFMAC for refinement. The alpha helices and beta sheets occurring in many protein structures can be taken as starting fragments for structure solution in ACORN. ACORN, along with ARP/wARP followed by REFMAC, can be an ab initio method for solving protein structure for which data are better than 1.2 A (atomic resolution). Attempts are here made in extending its applications to real data at 1.45 A resolution and also to truncated data at 1.6 A resolution. Two previously known structures, congerin II and alkaline cellulase N257, were resolved using the above approach. Automatic structure solution, phasing and refinement for real data at still lower resolutions for proteins of various complexities are being carried out. Data mining of the secondary structural features using PDB is being carried out for this new approach for 'seed-phasing' to ACORN.


Asunto(s)
Algoritmos , Cristalografía por Rayos X/métodos , Bases de Datos de Proteínas , Modelos Moleculares , Proteínas/química , Análisis de Secuencia de Proteína/métodos , Programas Informáticos , Celulasas/química , Sistemas de Administración de Bases de Datos , Galectinas/química , Conformación Proteica , Estructura Secundaria de Proteína , Control de Calidad , Sensibilidad y Especificidad
7.
Acta Crystallogr D Biol Crystallogr ; 60(Pt 9): 1586-90, 2004 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-15333929

RESUMEN

The crystal structure of the triple mutant K53,56,120M of bovine pancreatic phospholipase A(2) has been redetermined using sulfur single-wavelength anomalous scattering. The synchrotron data were collected at lambda = 1.54 A and the crystal diffracted to 1.6 A resolution. The program SOLVE was used to locate the heavy atoms and to estimate the initial phases and the resulting map was then subjected to RESOLVE. The output of 455 non-H atoms, including 12 S atoms, one calcium ion and one chloride ion, were then subjected to ARP/wARP followed by REFMAC. With the improved phases, the automatic model building successfully built more than 85% of the 123 residues, excluding the N- and C-terminal residues. The final crystallographic R factor is 17.7% (R(free) = 21.7%). The refined model consists of 954 non-H protein atoms, 165 water O atoms, three 2-methyl-2,4-pentanediol (MPD) molecules, one calcium ion and one chloride ion. The present work is yet another example that shows the utility of single-wavelength anomalous scattering data for solving a protein structure.


Asunto(s)
Fosfolipasas A/química , Fosfolipasas A/genética , Animales , Bovinos , Cloruros/química , Cristalografía por Rayos X , Glicoles , Modelos Moleculares , Mutación/genética , Páncreas/enzimología , Fosfolipasas A2 , Dispersión de Radiación , Azufre/química , Agua/química , Difracción de Rayos X
8.
Acta Crystallogr C ; 58(Pt 3): o164-7, 2002 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-11870315

RESUMEN

N-(2-Chlorobenzyl)-1,2,3,4-tetrahydroisoquinoline-1,3-dione, C(16)H(12)ClNO(2), crystallizes in P2(1)/n with three crystallographically independent molecules in the asymmetric unit, which differ slightly in conformation, N-(2-bromo-4-methylphenyl)-1,2,3,4-tetrahydroisoquinoline-1,3-dione, C(16)H(12)BrNO(2), crystallizes in P2(1)/n with one molecule in the asymmetric unit and N-(2,3-dichlorophenyl)-1,2,3,4-tetrahydroisoquinoline-1,3-dione, C(15)H(9)Cl(2)NO(2), crystallizes in P2(1)/c with one molecule in the asymmetric unit. In all three structures, the heterocyclic rings adopt approximately planar conformations. The pyridine rings are orthogonal to the substituted phenyl rings. In all three structures, the crystal packing is stabilized by intermolecular C-H...O hydrogen bonds.


Asunto(s)
Isoquinolinas/química , Tetrahidroisoquinolinas , Enlace de Hidrógeno , Modelos Moleculares , Conformación Molecular
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