2011/01/01 by Kana Ishisaki, Sachiko Arai, Tatsuro Hamada +2 · 1 citation
Agricultural and Biological Sciences · Arts and Humanities · Biochemistry, Genetics and Molecular Biology · #Historical Art and Architecture Studies #Historical Studies on Spain #Plant Parasitism and Resistance #Plant and Biological Electrophysiology Studies #Plant tissue culture and regeneration
paper · doi:10.1016/j.carres.2012.09.001
openalex publication_date 2011/01/01 · openalex created_date 2016/06/24 · openalex updated_date 2026/04/28
A class III chitinase belonging to the GH18 family from Nepenthes alata (NaCHIT3) was expressed in Escherichia coli. The enzyme exhibited hydrolytic activity toward colloidal chitin, ethylene glycol chitin, and (GlcNAc)(n) (n=5 and 6). The enzyme hydrolyzed the fourth glycosidic linkage from the non-reducing end of (GlcNAc)(6). The anomeric form of the products indicated it was a retaining enzyme. The colloidal chitin hydrolytic reaction displayed high activity between pH 3.9 and 6.9, but the pH optimum of the (GlcNAc)(6) hydrolytic reaction was 3.9 at 37 °C. The optimal temperature for activity was 65 °C in 50 mM sodium acetate buffer (pH 3.9). The pH optima of NaCHIT3 and NaCHIT1 might be related to their roles in chitin degradation in the pitcher fluid.