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Figure 3 | Biotechnology for Biofuels

Figure 3

From: An acidic, thermostable exochitinase with β-N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin to N-acetyl glucosamine

Figure 3

Optimal pH (a) and pH stability (b) of the purified PbChi74 from P. barengoltzii . The optimal pH was determined in 50 mM of various buffers within pH 2.0-12.0. The buffers used were: glycine-HCl (solid squares) (pH 2.0-3.5), sodium citrate (open diamonds) (pH 3.0-6.0), acetate (solid diamonds) (pH 4.0-5.5), sodium phosphate (open triangles) (pH 6.0-7.5), Tris-HCl (solid circles) (pH 6.5-8.0), CHES (open squares) (pH 7.5-9.0), MOPS (open circles) (pH 8.0-10.0), and glycine-NaOH (solid triangles) (pH 10.0-12.0). To determine pH stability, the enzyme aliquots were incubated in different buffers mentioned above at 30°C for 30 min and then the residual activities were measured.

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