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Fig. 3 | Biotechnology for Biofuels

Fig. 3

From: Efficient hydrolysis of raw starch and ethanol fermentation: a novel raw starch-digesting glucoamylase from Penicillium oxalicum

Fig. 3

Effects of pH and temperature on enzymatic activity and the stability of the purified glucoamylase PoGA15A. Data given are mean ± standard deviation from three replicates. The results are from a representative experiment, and similar results were obtained in two other independent experiments. a The effect of pH on enzyme activity. The enzyme activity was assayed in a citrate–phosphate buffer (pH 3.0–7.0) at 37 °C. b The influence of temperature on enzyme activity. The enzyme activity was determined between 30 and 80 °C under optimum pH conditions. c The effect of pH on enzyme stability. The pH stability of PoGA15A was measured by pre-incubating the enzyme in various buffers for 24 h at 4 °C, and the residual enzyme activity was determined using the standard method. d The influence of temperature on enzyme stability. Temperature stability was determined by the standard method after pre-incubating the enzyme at pH 4.5 between 30 and 80 °C for 1 h

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