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Applied Biological Chemistry
Fig. 3 | Journal of the Korean Society for Applied Biological Chemistry

Fig. 3

From: Efficient secretory expression of gene encoding a broad pH-stable maltose-forming amylase from Lactobacillus plantarum S21 in food-grade lactobacilli host

Fig. 3

Characterization of purified recombinant α-amylase. The optimal pH of α-amylase determined at 37 °C in various buffer systems for 10 min with the activity at pH 6.5 set as 100 %; the buffers used included citrate–phosphate buffer (3.0–6.0), Na-phosphate buffer (6.0–8.0), and Tris–HCl (8.0–9.0) (A). The pH stability of α-amylase; the enzyme activity was determined at pH 6.5 and 37 °C for 10 min after incubation of the enzyme solution at different pH values (3.0–9.0) at 37 °C for 24 h. The activity at pH 6.5 without incubation was set to 100 % (B). The optimum temperature of α-amylase; the enzyme assay was conducted at different temperatures (25–65 °C) at pH 6.5 for 10 min, with the activity at 37 °C set as 100 % (C). Thermostability of α-amylase; the enzyme activity was determined at pH 6.5 and 37 °C for 10 min after incubation at different temperatures for 1 h. The activity without incubation was set to 100 % (D)

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