Mono, Bi and Trihetercyclic Compounds: Synthesis, Characterization, Physicochemical, Structural and Biological Properties | Book Publisher International

The synthesis of new mono-, bi- and tri-heterocyclic carboxylic and phosphonic acid models are attracting the interest of research teams around the world due to the broad spectrum of activity they present. Indeed, these biomolecules constitute a class of compounds active in biochemistry, enzymology, medicine, agrochemical industry, and pharmacology. The Professors and Researchers, members of the Organic Chemistry Laboratory, aware of the importance of integrating the University into its socio-economic environment and of the interest in linking their fundamental research axes to the world of industry, have turned to themes, at the chemistry-biology interface, focused on the search for molecules with agrochemical, pharmaceutical, and therapeutic potential. In addition to these properties, these molecules have several reactive centers and can be involved in different reactions, very important steps in the formation of the organic chemist. This book covers key areas of heterocyclic chemistry. It is based on four pillars: (1) the extension of our previous work on heterocyclic alkylation and cycloaddition reactions to the preparation of new models of heterocyclic and phosphonic amino acids by the substitution reaction of O-tosyl group and azide derivatives by different amino acids with heterocyclic and non-heterocyclic chains (glycine, proline, histidine, tryptophan…); (2) the application of the synthesis strategy provided for in the first part to the synthesis of new mono-, bi- and tri-heterocyclic carboxylic and phosphonic models; (3) the use of spectroscopic methods (NMR 1H, 13C, 14N, 1D, 2D, IR) and analytical techniques (X-ray diffraction, mass, elemental analysis) for the characterization of the synthesized molecules, (4) the search for an application to the synthesized molecules.

Author (s) Details

Anouar Alami
Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, FES, Morocco.

Younas Aouine
Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco and Department of Chemistry, Faculty of Sciences, Ibn Zohr University, P.B. 8106, Cité Dakhla, Agadir 80060, Morocco.

Brahim Labriti
Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco.

Hassane Faraj
Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco.

Abdelilah El Hallaoui
Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco.

Salaheddine Boukhssas
Doctoral Training “Bioactive Molecules, Health and Biotechnology”, Center of Doctoral Studies “Sciences and Technology”, Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco and Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco.

Khadim Dioukhane
Doctoral Training “Bioactive Molecules, Health and Biotechnology”, Center of Doctoral Studies “Sciences and Technology”, Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco and Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco.

Sara Hajib
Doctoral Training “Bioactive Molecules, Health and Biotechnology”, Center of Doctoral Studies “Sciences and Technology”, Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco and Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco.

Oumaima Karai
Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco.

Abdou Khadir Fall
Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco.

Khalid Boukallaba
Laboratory of Organic Chemistry (LCO), Faculty of Sciences Dhar El Mahraz, Sidi Mohamed Ben Abdellah University, P.B. 2626, Fez 30000, Morocco.

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Purification and Characterization of Pectin Methylesterase Produced in Solid State Fermentation by Aspergillus tubingensis | Chapter 03 | Advances and Trends in Biotechnology and Genetics Vol. 2

Aim: Purification and characterization of pectin methylesterase produced by Aspergillus tubingensis in solid state fermentation.

Study Design:  Pectin methylesterase enzyme produced by A. tubingensis was extracted from the fermented solid medium and purified using chromatographic techniques. The purified enzyme was characterized for physico-chemical and kinetic properties.

Place and Duration of Study: Experiments were performed at the School of Biotechnology, Devi Ahilya University, Indore, INDIA and Maharaja Ranjit Singh College of Professional Sciences, Indore, INDIA, between October, 2014 and August, 2015.

Methodology: The enzyme was extracted and purified using ammonium sulphate fractionation, ion exchange chromatography (IEC) using CM- cellulose and gel filtration chromatography (GFC) using Sephadex G-100. The molecular weight of the purified enzyme was determined using native polyacrylamide gel electrophoresis (Native PAGE) and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS–PAGE). The purified enzyme was characterized to determine the pH and temperature optima. Thermostability, pH stability and substrate kinetics were studied for purified pectin methylesterase.

Results: The acidic pectin methylesterase of Aspergillus tubingensis was purified to 20.3 fold with a 47.7% recovery through IEC on CM- cellulose and GFC using Sephadex G-100. The purified enzyme had a specific activity, 112.6 U/mg. The SDS-PAGE revealed that the enzyme was monomeric with a molecular weight of 45.7 kDa. The optimum pH and temperature were 4.6 and 50°C, respectively. This enzyme was stable over a wide pH range (3.0–8.0) and at relatively high temperature at 50°C for 1 h. The Km and Vmax values of pectin methylesterase towards citrus pectin were 33.3 mg/l and 251.2 µmol/ml/min, respectively. In addition, the enzyme activity increased by about 16% in the presence of 5 mM Mg2+.

Conclusion: The pectin methylesterase enzyme of A. tubingensis has been purified up to homogeneity and found to be monomeric on SDS-PAGE. Enzyme characterization revealed that purified enzyme worked optimally in acidic conditions and was stable at wider pH range.

Author(s) Details

Dr. Mukesh Kumar Patidar
Department of Biosciences, Maharaja Ranjit Singh College of Professional Sciences, Indore, India.

Dr. Anand Nighojkar
Department of Biosciences, Maharaja Ranjit Singh College of Professional Sciences, Indore 452001, India.

Dr. Sadhana Nighojkar
Department of Biotechnology, Mata Gujri College of Professional Studies, Indore 452001 India.

Dr. Anil Kumar
School of Biotechnology, Devi Ahilya University, Khandwa Road, Indore 452001, India.

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View Volume: https://doi.org/10.9734/bpi/atbg/v2