Azza M. Abdel‐Fattah

National Research Centre

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Reactions, Anti-Alzheimer and Anti COX-2 Activities of the Newly Synthesized 2-Substituted Thienopyridines

Current Organic Chemistry (2009)

Fawzy A. Attaby Azza M. Abdel‐Fattah Labeeb M. Shaif Mohamed A. Elsayed

3-Amino-4-(phenyl or p-methoxyphenyl)-6-pyridin-3-ylthieno[2,3-b]-pyridine-2-carboxamide and 3-amino-4- (phenyl or p-methoxyphenyl)-6-pyridin-3-ylthieno[2,3-b]pyridine-2-carbonitrile were used as the starting materials aiming to obtain the newly synthesized pyridothieno-pyrimidines, pyridothienotriazines and pyridothienoxazines via their reactions with several reagents e.g. CS2, HCOOH, CH(OEt)3, Ac2O and HNO2. These newly synthesized heterocyclic compounds were tested as anti-Alzheimer and anti COX-2 agents and their structures were elucidated by considering the data of IR, 1H NMR, mass spectra and elemental analyses.

Carboxamide

10.2174/138527209789578135

Cite

Citations (11)

ChemInform Abstract: Synthesis, Reactions, Characterization and Biological Evaluation of 2,3′‐Bipyridine Derivatives (III).

ChemInform (2015)

Fawzy A. Attaby Azza M. Abdel‐Fattah Labeeb M. Shaif Mohamed M. Elsayed

Abstract This describes the syntheses of a series of target compounds (V) and (VI) (selected examples shown).

Characterization

10.1002/chin.201504155

Cite

Citations (0)

Synthesis, reactions and characterization of 2-methylthionicotino-nitrile, pyrazolopyridine and pyridopyrazolotriazine derivatives

Afinidad (2008)

Azza M. Abdel‐Fattah Mohamed A. A. Elneairy M. N. Gouda Fawzy A. Attaby

4,6-Diaryl-1H-pyrazolo[3,4-b]pyridin-3-amines 4a-c were obtained in very pure state and used as the good starting materials for the present study. Compound 4a diazotized to give the corresponding diazonium salt 11 and also, reacted with 2-bromo-1-phenylethanone to give the corresponding pyrazolo[3,4-b]pyridin-2-yl)-1-phenylethanone derivative 7 which in turn, used for the preparation of the hydrazone and formamide derivatives 8 and 10 respectively through its reaction with hydrazine hydrate and formic acid respectively. Compound 11 was used for the preparation of pyridopyrazolotriazine derivatives via its coupling with several active –CH2- containing compounds. Considering the data from IR, 1H NMR, the mass spectra and elemental analyses the chemical structures of the newly synthesized heterocyclic compounds were elucidated.

Hydrazone

Hydrazine (antidepressant)

Derivative (finance)

Proton NMR

Coupling reaction

Source

Cite

Citations (1)

Preparation and some properties of immobilized Penicillium funiculosum 258 dextranase

Process Biochemistry (1999)

Mohamed A. Abdel–Naby A. M. Ismail Azza M. Abdel‐Fattah Ahmed F. Abdel‐Fattah

Dextranase

Glutaraldehyde

Michaelis–Menten kinetics

Specific activity

10.1016/s0032-9592(98)00127-7

Cite

Citations (52)

Levansucrase optimization using solid state fermentation and levan biological activities studies

Carbohydrate Polymers (2013)

Mona A. Esawy Azza M. Abdel‐Fattah Mamdouh M. Ali Wafaa A. Helmy Bassem M. Salama

Levansucrase

Yeast extract

Solid-State Fermentation

10.1016/j.carbpol.2013.03.089

Cite

Citations (29)

The potential industrial application of Bacillus amyloliquefaciens EGY3 keratinolytic protease: optimization, characterization and application as eco-friendly sustainable alternative in leather and detergent industry

Egyptian Journal of Chemistry (2024)

Shaimaa A. Nour Shaymaa A. Ismail El-Shhat Nashy Azza M. Abdel‐Fattah

Keratinolytic proteases are proteolytic enzymes specifically catalyse keratin hydrolysis that have been seen as efficient eco-friendly bio-catalysts for various industrial processes. In this study, an isolated keratinolytic bacterial strain namely Bacillus amyloliquefaciens EGY3 (Genbank accession number PP038117) was used for the enzyme production under submerged fermentation of feather in which the addition of corn steep liquor possessed a positive impact on the enzyme productivity. Furtherly, the fermentation conditions was statistically optimized and the optimized enzyme activity (391.5 ± 3.50 U/ml) was increased by 5.5-fold. Moreover, the partially purified enzyme was estimated to be alkalophilic (optimum activity at pH 9), thermophilic (optimum activity at 70°C) and surfactant stable enzyme. By examining the generated enzyme's suitability for dehairing bovine hide, complete dehairing was achieved after 2 h with the production of smooth clean surface and without the estimation of any negative impact on the skin structure manifested by scanning electron microscopy. Finally, the enzyme's possible application in getting rid of a stain made of proteins (chocolate-flavored milk stain) from cotton fabrics was examined in which the enzyme addition to a thermally-inactivated commercial detergent restored the whiteness index of the treated fabric by 86.28 % in compare to 65.26% for the use of the commercial detergent.

Environmentally Friendly

Bacillus amyloliquefaciens

Alkaline protease

10.21608/ejchem.2024.328542.10633

Cite

Citations (0)

Biodegradation of feather waste by keratinase produced from newly isolated Bacillus licheniformis ALW1

Journal of Genetic Engineering and Biotechnology (2018)

Azza M. Abdel‐Fattah Mamdouh S. El-Gamal Siham Ismail Mohamed A. Emran Amal M. Hashem

Keratinase are proteolytic enzymes which have gained much attention to convert keratinous wastes that cause huge environmental pollution problems. Ten microbial isolates were screened for their keratinase production. The most potent isolate produce 25.2 U/ml under static condition and was primarily identified by partial 16s rRNA gene sequence as Bacillus licheniformis ALW1. Optimization studies for the fermentation conditions increased the keratinase biosynthesis to 72.2 U/ml (2.9-fold). The crude extracellular keratinase was optimally active at pH 8.0 and temperature 65 °C with 0.7% soluble keratin as substrate. The produced B. licheniformis ALW1 keratinase exhibited a good stability over pH range from 7 to 9 and over a temperature range 50–60 °C for almost 90 min. The crude enzyme solution was able to degrade native feather up to 63% in redox free system.

Keratinase

Bacillus licheniformis

Feather meal

Bacillus (shape)

Bacillus sphaericus

10.1016/j.jgeb.2018.05.005

Cite

Citations (114)

Purification and characterization of a new thermophilic collagenase from Nocardiopsis dassonvillei NRC2aza and its application in wound healing

International Journal of Biological Macromolecules (2018)

Amira Abood Asmaa Salman Azza M. Abdel‐Fattah Amr E. El-Hakim Azza M. Abdel‐Aty

10.1016/j.ijbiomac.2018.05.030

Cite

Citations (19)

Optimization, characterization and thermodynamic studies on B. licheniformis ALW1 keratinase

Egyptian Journal of Chemistry (2018)

Amal M. Hashem Azza M. Abdel‐Fattah Siham Ismail Mamdouh S. El-Gamal Mona A. Esawy

Optimization of B. licheniformis ALW1 keratinase was investigated by using a Plackett – Burman design (PBD) and Central Composite Design (CCD). PBD showed that galactose, inoculum size and corn steep liquorwere the most effectivevariables played a rolein improving the enzyme productivity (87.65U/mL). CCD results recorded an increase in enzyme productivity to about1.4-fold compared to the basal medium (99.1 U/mL). The optimum activity for the partial purified enzyme was obtained at pH 8.5 and 70˚C. The activation and deactivation energy were calculated to be25.37 kJmol-1 and73.38 kJmol-1 respectively. The half-life time was 1380,690,530, and383 min. at 50˚C,55˚C,60˚C and 65˚C respectively. Also, D values were 4600,2300,1769, 1277min. at the same degree respectively. ∆G° (kJmol-1) kept relatively constant between 50-60˚C (191.49 kJmol-1-193.31 kJmol-1) and noticeably increase at 65˚C (212.86 kJmol-1). ∆H° (kJmol-1) recorded minor decrease by the increase of temperature. Approximately, most of the tested metals ions have stimulation effect in enzyme activityand MgSO4.H2O was the best (146%). Among all the tested detergents tween 80 retained 97% of original enzyme activity. DMSO increased the enzyme activity about 11%, while propanol and acetonitrile reduced the enzyme activity to about 14% and 10% respectively. All the reducing agents had a stimulating effect on enzyme activity with variable degrees. The enzyme (980 U) had the ability to hydrolyze 74% of the feather to nutritional valuable protein.

Keratinase

Central composite design

Bacillus licheniformis

10.21608/ejchem.2018.3379.1287

Cite

Citations (11)

Pyrazolo[3,4-b]pyridine in heterocyclic synthesis: synthesis of new pyrazolo[3,4-b]pyridines, imidazo[1',2':1,5]pyrazolo[3,4-b]pyridines, and pyrido[2',3':3,4]pyrazolo[1,5-a]pyrimidines

Canadian Journal of Chemistry (2007)

Mohamed A. M. Gad‐Elkareem Azza M. Abdel‐Fattah Mohamed A. A. Elneairy

Pyrazolo[3,4-b]pyridine derivatives 7 and 9 were synthesized via the reaction of 3-amino-1H-pyrazolo-[3,4-b]pyridine derivative 2 with ω-bromoacetophenones. Reaction of 7 and 9 with Ac 2 O afforded the imidazo[1',2':1,5]py razolo[3,4-b]pyridine derivative 8 and pyrazolo[3,4-b]pyridine derivative 10, respectively. Reaction of 2 with chloroacetonitrile followed by DMF-DMA gave imidazo[1',2':1,5]pyrazolo[3,4-b]pyridines 4 and 5, respectively. Acetyl acetone and 1,1-dicyano-2,2-dimethylthioethene were reacted with 2 to afford the pyrido[2',3':3,4]pyrazolo-[1,5-a]-pyrimidines 11 and 14, respectively. Also, 2 reacted with DMF-DMA to yield the formamidine 15, which in turn, reacted with active methylene reagents, yielding the corresponding pyrido[2',3':3,4]pyrazolo[1,5-a]pyrimidines 18 and 23a-23d.Key words: 1H-pyrazolo[3,4-b]pyridines, imidazo[1',2':1,5]pyrazolo[3,4-b]pyridines, pyrido[2',3':3,4]pyrazolo[1,5-a]pyrimidines.

Derivative (finance)

Methylene

10.1139/v07-089

Cite

Citations (19)