Enzymatic degradation and bioactivity evaluation of C-6 oxidized chitosan

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Pierre, Guillaume | Salah, Rym | Gardarin, Christine | Traïkia, Mounir | Petit, Emmanuel | Delort, A.M. | Mameri, Nabil | Moulti-Mati, Farida | Michaud, Philippe

Edité par HAL CCSD ; Elsevier

International audience. C-6 oxidized chitosan was produced from chitosan by performing selective oxidation with NaOCl andNaBr using 2,2,6,6-tetramethylpiperidine-1-oxy radical (TEMPO) as catalyst. Endocellulase, Celluclast1.5 L, Glucanex®, Macerozyme R-10, hyaluronidase, hyaluronate lyase, red scorpionfish chitinase, glu-curonan lyase and a protein mix from Trichoderma reesei were used to degrade the C-6 oxidized chitosan.Glucanex®, the crude extract from T. reesei IHEM 4122 and Macerozyme R-10 validated the enzymaticdegradation through final hydrolysis yields of the derivative respectively close to 36.4, 20.3 and 12.9%(w/w). The best initial reaction velocity (2.41 U/mL) was observed for Glucanex®. The antileishmanialactivity of the derivative was evaluated against Leishmania infantum LIPA 137. The antibacterial activitiesagainst Escherichia coli ATCC 25922 and Pseudomonas aeruginosa ATCC 27853 were also tested. Resultsshowed an antileishmanial activity (IC50: 125 g/mL) of the obtained derivatives against L. infantum LIPA137.

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