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Fig. 5 | Biotechnology for Biofuels

Fig. 5

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

Fig. 5

Determination of optimal pH (a) and optimal temperature (b) of mRmMan5A and the variants derived using site-directed mutagenesis. The effect of pH on β-mannanase activity was determined in 50 mmol L−1 of different buffers at optimal temperature of each enzyme. For optimal temperature, activity was measured at different temperatures in 50 mmol L−1 McIlvaine buffer (optimal pH of each enzyme). The specific activities of mRmMan5A (9671.4 U mg−1), variant Tyr233His (9834.6 U mg−1), variant Lys264Met (10,139.5 U mg−1), variant Asn343Ser (10,849.1 U mg−1), and variant Tyr233His/Lys264Met (9942.8 U mg−1) were considered as 100% in determinate the optimal pH and optimal temperature

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