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1.
Polymers (Basel) ; 15(15)2023 Jul 31.
Article in English | MEDLINE | ID: mdl-37571156

ABSTRACT

The present study involves the synthesis of photocatalytic composite nanofibers (NFs) comprising ilmenite nickel titanite-supported carbon nanofibers (NiTiO3/TiO2@CNFs) using an electrospinning process. The photocatalytic composite NFs obtained were utilized in hydrogen (H2) production from the photohydrolysis of ammonia borane (AB). The experimental findings show that the photocatalytic composite NFs with a loading of 25 mg had a good catalytic performance for H2 generation, producing the stoichiometric H2 in 11 min using 1 mmol AB under visible light at 25 °C and 1000 rpm. The increase in catalyst load to 50, 75, and 100 mg leads to a corresponding reduction in the reaction time to 7, 5, and 4 min. The findings from the kinetics investigations suggest that the rate of the photohydrolysis reaction is directly proportional to the amount of catalyst in the reaction system, adhering to a first-order reaction rate. Furthermore, it was observed that the reaction rate remains unaffected by the concentration of AB, thereby suggesting a reaction of zero order. Increasing the reaction temperature results in a decrease in the duration of the photohydrolysis reaction. Furthermore, an estimated activation energy value of 35.19 kJ mol-1 was obtained. The composite nanofibers demonstrated remarkable and consistent effectiveness throughout five consecutive cycles. The results suggest that composite NFs possess the capacity to function as a feasible substitute for costly catalysts in the process of H2 generation from AB.

2.
Prep Biochem Biotechnol ; 38(1): 24-39, 2008.
Article in English | MEDLINE | ID: mdl-18080908

ABSTRACT

Optimized Synthetic human insulin gene was preferred to easy of cloning, plasmid stability, and protein expression away from the native sequence and its rare codons. Two steps to obtain the insulin, so we assembled the gene of 293 bp using a battery of overlapped synthetic oligos, then cloned into pET101directional TOPO expression vector downstream to the T7 promoter. The proinsulin products were produced as inclusion bodies in E. coli at a level of 10%. The batch cultivation of the strain yielded 6 g/L, while the high cell density of fed-batch cultivation yielded 46 g/L. The proinsulin purification yielded 110 mg/gram cell weight, and 1.3 mg/gram of a bioactive insulin. The native insulin was generated by enzymatic conversion of chemically processed proinsulin. The produced insulin was matched with that of a commercial aqueous version at a level of enzyme immunoassys, SDS-PAGE, RP-HPLC, and bioactivity. The present results showed that the produced insulin has a comparable biochemical and potency similar to that of commercial one.


Subject(s)
Gene Expression Regulation , Insulin/metabolism , Chromatography, High Pressure Liquid , Cloning, Molecular , Culture Media , Electrophoresis, Polyacrylamide Gel , Escherichia coli/genetics , Escherichia coli/metabolism , Humans , Immunoassay , Insulin/genetics , Kinetics , Plasmids/genetics , Promoter Regions, Genetic
3.
Hum Antibodies ; 15(3): 95-102, 2006.
Article in English | MEDLINE | ID: mdl-17065740

ABSTRACT

Polymeric immunoglobulin (dimeric IgA and pentameric IgM) molecules can assembly by using the immunoglobulin J (joining) chain and across the epithelial cell layers. Based on its amino acid and gene sequences data, disulfide bond (2 bonds) assignment secondary structure predictions, and chemical properties, a model for J-chain folding has been proposed. However, the crystal structure of the J-chain protein is still far from obtained, because the J-chain expression and its protein downstream has a permanent aggregation problems, due to its two free thiol groups. Our work focused on the chemical blocking of free cysteines-SH or to mutate these cysteines into serine residues. The chemical blocking yielded partially soluble proteins with new structures (carboxyamidomethyl cysteine and carboxyamidomethyl methionine) at cysteine and methionine residues. While mutate the cysteines into serine has been yielded a complete soluble (11.5 mg/l) J-chain protein which migrate (SDS-PAGE) at 27 KDa. We were used pET22b expression vector and E. coli BL21 (DE3) to produce the J-chain protein. For maximization the production yield of j-chain foreign protein, the batch culture was developed. We described the scaling-up production in term of kinetic behavior to the recombinant E.coli and optimization of cultivation parameters in 3-L bench-top bioreactor. The process was automated through a computer aided data bioprocessing system AFS-BioCommand multi-process management program to regulate the cell growth rate, temperature, pH and agitation speed based on dissolved oxygen. The results showed an obvious increasing in biomass by 5.98 g/L after about 27 h [corrected]


Subject(s)
Immunoglobulin J-Chains/chemistry , Recombination, Genetic , Base Sequence , DNA Primers , Electrophoresis, Polyacrylamide Gel , Humans , Immunoglobulin J-Chains/genetics , Mutagenesis, Site-Directed , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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