A CRITICAL STUDY OF CLINTON BENNETT’S THOUGHTS TOWARDS SIRAH OF THE HOLY PROPHET ﷺ

Sirah of the Holy Prophet ﷺ is the topic on which a lot of work has been done both in the Muslim and non-Muslim world. For Muslims it was the source of aspiration and adaptation for the practical purposes of social life while for the non-Muslims it was the source of inquisitiveness and understanding Islam as a successful religion in the past and present time. Therefore, Muslim enthusiastic interest in the biography of the Holy Prophet ﷺ developed and evolved into a regular science while the west has modified the knowledge of biography according to their own order of preference but within the same biographic precedents. Both have tried to reconstruct the biography of the Holy Prophet ﷺ historically, chronologically and logically. Clinton Bennett is one of the western scholars who has contributed not only in the Islamic literature but also the biographic field. His work consists of numerous issues in Islam. Whatever he has learned from Islam and the Sirah of Holy Prophet and thus concluded in the form of his own thoughts, he has expressed most of them in his famous five books for example ‘In Search of Muhammad’, ‘Muslims and Modernity’, ‘Studying Islam’, ‘Interpreting the Qur’an’, and ‘Victorian Images of Islam’ (doctoral thesis)’. This study focuses on Clinton Bennett’s work on Sirah specifically with his broader view of the subject. This research is descriptive and analytical in nature and presents a detailed analysis of the work it is based upon.

Kinetics and Thermodynamics of Proteases from Bacillus Sp.

Present project focuses on the study of protease from the indigenously isolated strain Bacillus. Effects of different substrate levels, ionic concentrations (MgCl2, CaCl2, K2HPO4, (NH4)2SO4, Urea), cane molasses and yeast sludge on the production of proteases by Bacillus subtilis. Various conditions like incubation period, mode of fermentation, pH, temperature etc. were optimized. After optimization of conditions, the proteases were produced on large scale. The proteases thus produced were subjected to the purification through various steps like ammonium sulphate precipitation, ion exchange chromatography and gel filtration. Kinetic study of proteases was also carried out in order to calculate Km and Vmax of the enzymes. Thermal inactivation was studied in order to calculate the Kd, energy of activation (Ea), Gibbs free energy (∆G), Enthalpy (∆H) and entropy (∆S). Activation or inhibition effect of different metal ions and chelating agents like EDTA, EGTA and PMSF on the protease was examined. Maximum activity of the crude proteases ( 502 U) was obtained at pH 7.5, temperature 45 °C after 48 hours of continuous shaking at 220 rpm using Bacillus subtilis cultured on skim milk (2%) in the optimized medium containing MgCl2 ( 0.01%), (NH4)2SO4 (0.3%) , CaCl2 ( 0.03%), K2HPO4 ( 0.5%), yeast sludge (300 μL) and cane molasses (0.03%). Specific activity of the purified protease was (80 U/mg), yield is 3.18 % and 3 folds increase in activity. Kinetic investigation revealed that that Km and Vmax were 0.2mg/mL and 60 U/mg. Energy of activation Ea , Free energy of activation ∆G , Activaton Enthalpy ∆H, Activation entropy (∆S) were -403 KJ/mol, 91.4 KJ/mol, -403.37 KJ/mol and -407.80 J/mol. Thermo stabilization of proteases is mostly accompanied by a decrease in ∆H and ∆S. A metal ions effect on the activity of the proteases was also studied. PMSF inhibited the enzyme activity, but EDTA and EGTA would not had much pronounced effect on the activity of enzyme. That proved the class of proteases to be the serine due to the inhibition of PMSF. It was concluded that Bacillus subtilis had significant potential for the production of proteases. With respect to the kinetic study of proteases, small vales of Km than the substrate concentration showed large affinity of the enzyme with the substrate and found good source of for the production on proteases on large scale. The nature of the reaction mechanism was found to be first order because [S] was much less than Km. Activation enthalpy had negative values indicates that the enzyme was of endothermic nature. Economically cheaper metals enhanced the enzyme activity. So the Bacillus subtilis was found good catalytic agent for the production of proteases.