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Fig. 3 | Biotechnology for Biofuels

Fig. 3

From: Directed evolution of a β-mannanase from Rhizomucor miehei to improve catalytic activity in acidic and thermophilic conditions

Fig. 3

Biochemical properties of RmMan5A (filled square) and mRmMan5A (filled circle). a The effect of pH on β-mannanase activity in 50 mmol L−1 different buffers at 55 °C (for RmMan5A) or 65 °C (for mRmMan5A). b The pH stability of each enzyme in various pH ranges. c The influence of temperature on β-mannanase activity in 50 mmol L−1 McIlvaine buffer (pH 7.0 for RmMan5A and pH 4.5 for mRmMan5A). d The thermostability of each enzyme at different temperatures. For pH stability and thermostability, the residual activities of RmMan5A were measured at pH 7.0 and 55 °C, and those of mRmMan5A were measured at pH 4.5 and 65 °C. The specific activities of RmMan5A (10,756.3 U mg−1) and mRmMan5A (9671.4 U mg−1) were considered as 100% to determinate the optimal pH, pH stability, optimal temperature, and thermostability

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