title: Laccase mediated-synthesis of hydroxycinnamoyl-peptide from ferulic acid and carnosine.
abstract: Carnosine (CAR) dipeptide was functionalized with ferulic acid (FA) as substrate using laccase from Myceliophtora thermophila as biocatalyst. The enzymatic reaction was performed in aqueous medium under mild conditions (pH 7.5, 30°C) as an eco-friendly procedure. Results showed that this enzymatic process led to the synthesis of two new derivatives (P1, P2), from the coupling between CAR and FA derived products. Conditions allowing a high production of P1, P2 derivatives were determined with an optimal ratio of (FA: CAR) of (1:1.6) at optimal time reaction of 8h. Under these optimal conditions, the coupling between CAR and FA-products was demonstrated, resulting in the decrease of -NH2 groups (almost 50%) as quantified via derivatization. Due to the presence of FA in the structure of these new derivatives, they exhibited higher hydrophobic property than carnosine. Structural analyses by mass spectrometry showed that P1 and P2 (FA-CAR) derivatives exhibited the same molecular mass (MM 770g/mol) containing one CAR-molecule and three FA-molecules but with different chemical structures. Furthermore, these derivatives presented improved antioxidant (almost 10 times) and anti-proliferative (almost 18 times) properties in comparison with CAR. Moreover, P1 derivative exhibited higher antioxidant and anti-proliferative activities than P2 derivative, which confirmed the different structures of P1 and P2. These results suggested that the oxidized phenols coupling with carnosine is a promising process to enhance the CAR-properties.
authors.affiliation: Lorraine University, Laboratory of Biomolecules Engineering (LIBio), 2 Avenue de la Forêt de Haye, TSA40602, F-54518 Vandœuvre-lès-Nancy, France.
authors.forename: Abdulhadi
authors.initials: A
authors.lastname: Aljawish
authors.affiliation: Lorraine University, Laboratory of Reactions and Process Engineering (LRGP-CNRS UMR 7274), 2 Avenue de la Forêt de Haye, TSA40602, F-54518 Vandœuvre-lès-Nancy, France. Electronic address: isabelle.chevalot@univ-lorraine.fr.
authors.forename: Isabelle
authors.initials: I
authors.lastname: Chevalot
authors.affiliation: Lorraine University, Laboratory of Biomolecules Engineering (LIBio), 2 Avenue de la Forêt de Haye, TSA40602, F-54518 Vandœuvre-lès-Nancy, France.
authors.forename: Nidal
authors.initials: N
authors.lastname: Madad
authors.affiliation: Lorraine University, Laboratory of Biomolecules Engineering (LIBio), 2 Avenue de la Forêt de Haye, TSA40602, F-54518 Vandœuvre-lès-Nancy, France.
authors.forename: Cédric
authors.initials: C
authors.lastname: Paris
authors.affiliation: Lorraine University, Laboratory of Biomolecules Engineering (LIBio), 2 Avenue de la Forêt de Haye, TSA40602, F-54518 Vandœuvre-lès-Nancy, France.
authors.forename: Lionel
authors.initials: L
authors.lastname: Muniglia
mesh_terms: D052160:Benzothiazoles / Q000378:metabolism; D055162:Biocatalysis / Q000187:drug effects; D018938:Caco-2 Cells; D002336:Carnosine / Q000378:metabolism* / Q000494:pharmacology; D049109:Cell Proliferation / Q000187:drug effects; D002851:Chromatography, High Pressure Liquid; D003373:Coumaric Acids / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D020128:Inhibitory Concentration 50; D007700:Kinetics; D042845:Laccase / Q000378:metabolism*; D013058:Mass Spectrometry; D010084:Oxidation-Reduction / Q000187:drug effects; D010455:Peptides / Q000378:metabolism*; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet; D013451:Sulfonic Acids / Q000378:metabolism; D013997:Time Factors
chemical_list: D052160:Benzothiazoles; D003373:Coumaric Acids; D010455:Peptides; D013451:Sulfonic Acids; C002502:2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid; D002336:Carnosine; C004999:ferulic acid; D042845:Laccase
keywords: Antioxidant activity; Caco2 cells; Carnosine; Ferulic acid; Laccase