Optimization, Characterization and Thermodynamic Studies on B. licheniformis ALW1 Keratinase
Hashem, A., Abdel-Fattah, A., Ismail, S., El-Gamal, M., Esawy, M., Emran, M. (2018). Optimization, Characterization and Thermodynamic Studies on B. licheniformis ALW1 Keratinase. EKB Journal Management System, 61(4), 591-607. doi: 10.21608/ejchem.2018.3379.1287
Amal Mohamed Hashem; Azza Abdel-Fattah; Siham Ismail; Mamdouh El-Gamal; Mona Esawy; Mohamed Abdelrahman Emran. "Optimization, Characterization and Thermodynamic Studies on B. licheniformis ALW1 Keratinase". EKB Journal Management System, 61, 4, 2018, 591-607. doi: 10.21608/ejchem.2018.3379.1287
Hashem, A., Abdel-Fattah, A., Ismail, S., El-Gamal, M., Esawy, M., Emran, M. (2018). 'Optimization, Characterization and Thermodynamic Studies on B. licheniformis ALW1 Keratinase', EKB Journal Management System, 61(4), pp. 591-607. doi: 10.21608/ejchem.2018.3379.1287
Hashem, A., Abdel-Fattah, A., Ismail, S., El-Gamal, M., Esawy, M., Emran, M. Optimization, Characterization and Thermodynamic Studies on B. licheniformis ALW1 Keratinase. EKB Journal Management System, 2018; 61(4): 591-607. doi: 10.21608/ejchem.2018.3379.1287

Optimization, Characterization and Thermodynamic Studies on B. licheniformis ALW1 Keratinase

Egyptian Journal of Chemistry
Article 3, Volume 61, Issue 4, July and August 2018, Page 591-607  XML PDF (1023.02 K)
Document Type: Original Article
DOI: 10.21608/ejchem.2018.3379.1287
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Authors
Amal Mohamed Hashem email orcid 1; Azza Abdel-Fattah1; Siham Ismail1; Mamdouh El-Gamal2; Mona Esawy1; Mohamed Abdelrahman Emran1
1Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki, Giza, Egypt.
2Department of Botany and Microbiology. Faculty of Science (Boys), Al-Azhar University, Cairo, Egypt
Abstract
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.
Keywords
Keratinase; B. licheniformis; Partial Purification; Thermodynamic; Kinetics
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