Mechanism and kinetics modeling of the enzymatic hydrolysis of [alpha]1-32 antibacterial peptide

• Published in: Bioprocess and biosystems engineering Vol. 37; no. 7; p. 1315
• Main Authors: Hedhili, K, Vauchel, P, Dimitrov, K, Kriaa, K, Chataigné, G, Hani, K, Dhulster, P, Nedjar-arroume, N
• Format: Journal Article
• Language: English
• Published: Heidelberg Springer Nature B.V 01.07.2014
• Subjects: Antimicrobial agents; Hydrologic sciences; Hydrolysis; Kinetics; Peptides
• ISSN: 1615-7591; 1615-7605
• DOI: 10.1007/s00449-013-1101-5

Several antibacterial peptides can be obtained by enzymatic hydrolysis of the [alpha] chain of bovine hemoglobin. The kinetics of [alpha]1-32 peptide hydrolysis by pepsin was studied at several temperatures (15, 23 and 37 °C). Intermediate and final peptides were identified, and their antibacterial activity was assessed against four bacterial species. Evolution of generated peptides concentration enabled to propose a reaction pathway describing the parallel and consecutive reactions taking place during the hydrolysis. A mathematical model, based on the proposed mechanism, was developed to describe the kinetics of generated peptides during [alpha]1-32 hydrolysis. The constants of the main reactions were identified based on the experimental data, and their dependence on temperature was established using Arrhenius-type equations. Validation of the proposed model was performed by predicting kinetics of [alpha]1-32 peptide hydrolysis at 30 °C (all other experimental conditions being unchanged) with a good accuracy. This mathematical model could allow defining the optimal conditions for the production of various intermediate peptides with antibacterial activity from peptic hydrolysis of [alpha]1-32 peptide.[PUBLICATION ABSTRACT]