Enzymatic degradation and bioactivity evaluation of C-6 oxidized chitosan

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• 作者：Guillaume Pierre ; Rym Salah ; Christine Gardarin ; Mounir Traikia ; Emmanuel Petit ; Anne-Marie Delort ; Nabil Mameri ; Farida Moulti-Mati ; Philippe Michaud
• 关键词：Chitosan ; TEMPO oxidation ; Leishmania
• 刊名：International Journal of Biological Macromolecules
• 出版年：2013
• 出版时间：September, 2013
• 年：2013
• 卷：60
• 期：Complete
• 页码：383-392
• 全文大小：1520 K

文摘

C-6 oxidized chitosan was produced from chitosan by performing selective oxidation with NaOCl and NaBr using 2,2,6,6-tetramethylpiperidine-1-oxy radical (TEMPO) as catalyst. Endocellulase, Celluclast 1.5 L, Glucanex^?, Macerozyme R-10, hyaluronidase, hyaluronate lyase, red scorpionfish chitinase, glucuronan 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 enzymatic degradation 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 antileishmanial activity of the derivative was evaluated against Leishmania infantum LIPA 137. The antibacterial activities against Escherichia coli ATCC 25922 and Pseudomonas aeruginosa ATCC 27853 were also tested. Results showed an antileishmanial activity (IC₅₀: 125 ¦Ìg/mL) of the obtained derivatives against L. infantum LIPA 137.