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Fig. 5 | Biotechnology for Biofuels

Fig. 5

From: Molecular characterization of a novel chitinase CmChi1 from Chitinolyticbacter meiyuanensis SYBC-H1 and its use in N-acetyl-d-glucosamine production

Fig. 5

Effect of pH and temperature on the activity and stability of CmChi1. a Optimal pH and pH stability of the recombinant CmChi1. The optimal pH was determined in 50 mM solutions of various buffers within the pH range 3.5–10.0 (black line). To determine pH stability, the enzyme was incubated at 45 °C for 2 h with various pH buffers (gray line), and the residual activities were measured. b Optimal temperature and thermal stability of the recombinant CmChi1. The temperature optimum was determined at different temperatures (25–60 °C) in 50 mM sodium citrate (pH 5.2) (solid squares). To determine the thermostability, the residual activity was measured in 50 mM sodium citrate (pH 5.2) after the enzyme was treated for 2 h at different temperatures (open triangles)

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