title: Controlled Enzymatic Hydrolysis: A New Strategy for the Discovery of Antimicrobial Peptides.
abstract: The use of antimicrobial peptides (AMPs) is an alternative to traditional antibiotics. AMPs are obtained using different methods such as bacterial synthesis, chemical synthesis and controlled enzymatic hydrolysis. The later is an interesting approach that deserves our attention because of the yields gathered and peptides engineered. Usually, activities of AMPs obtained in such a way are tightly dependent on the hydrolysis mechanism used. This paper deals with the hydrolysis of hemoglobin mechanism as a potential source of AMPs. Production of AMPs from hemoglobin using enzymatic controlled system is linked to hemoglobin structure. Further, we show that bovine hemoglobin, which is sensitive to peptic hydrolysis, results upon enzymatic digestion as a great source of AMPs. The hemoglobin in native and denatured states was hydrolyzed by "one-by-one" and "zipper" mechanisms, respectively. Nevertheless, a new mechanism named "semi-zipper" mechanism is obtained when protein is in molten globule structural state, constituting an original strategy for AMPs production. Seventy seven percentage of the peptides obtained by this new strategy showed antibacterial activity against nine strains.
authors.affiliation: Laboratoire de Procédés Biologiques, Génie Enzymatique et Microbien (ProBioGEM), UPRES-EA 1026, Polytech'Lille/IUT «A», Université Lille I Sciences et Technologies, BP 179, 59655, Villeneuve d'Ascq Cedex, France.
authors.forename: Estelle Yaba
authors.initials: EY
authors.lastname: Adje
authors.affiliation: Laboratoire de Procédés Biologiques, Génie Enzymatique et Microbien (ProBioGEM), UPRES-EA 1026, Polytech'Lille/IUT «A», Université Lille I Sciences et Technologies, BP 179, 59655, Villeneuve d'Ascq Cedex, France. rafikbalti1981@gmail.com.
authors.forename: Rafik
authors.initials: R
authors.lastname: Balti
authors.affiliation: Laboratoire de Procédés Biologiques, Génie Enzymatique et Microbien (ProBioGEM), UPRES-EA 1026, Polytech'Lille/IUT «A», Université Lille I Sciences et Technologies, BP 179, 59655, Villeneuve d'Ascq Cedex, France.
authors.forename: Didier
authors.initials: D
authors.lastname: Lecouturier
authors.affiliation: Laboratoire d'Application de Spectrométrie de Masse (LASM), Faculté des Sciences Pharmaceutiques et Biologiques, Université Lille II Droit et Santé, Service Commun de Physicochimie, BP 83, 59006, Lille Cedex, France.
authors.forename: Mostafa
authors.initials: M
authors.lastname: Kouach
authors.affiliation: Laboratoire de Procédés Biologiques, Génie Enzymatique et Microbien (ProBioGEM), UPRES-EA 1026, Polytech'Lille/IUT «A», Université Lille I Sciences et Technologies, BP 179, 59655, Villeneuve d'Ascq Cedex, France.
authors.forename: Pascal
authors.initials: P
authors.lastname: Dhulster
authors.affiliation: Laboratoire de Procédés Biologiques, Génie Enzymatique et Microbien (ProBioGEM), UPRES-EA 1026, Polytech'Lille/IUT «A», Université Lille I Sciences et Technologies, BP 179, 59655, Villeneuve d'Ascq Cedex, France.
authors.forename: Didier
authors.initials: D
authors.lastname: Guillochon
authors.affiliation: Laboratoire de Procédés Biologiques, Génie Enzymatique et Microbien (ProBioGEM), UPRES-EA 1026, Polytech'Lille/IUT «A», Université Lille I Sciences et Technologies, BP 179, 59655, Villeneuve d'Ascq Cedex, France.
authors.forename: Naïma
authors.initials: N
authors.lastname: Nedjar-Arroume
keywords: Antimicrobial peptides; Bovine hemoglobin; Hydrolysis mechanism; Protein structure