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Fig. 6 | Biotechnology for Biofuels

Fig. 6

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

Fig. 6

Localization of the three substitutions, surface view, and charge distribution in RmMan5A and mRmMan5A. a Localization of three residues (Tyr233, Lys264, and Asn343) and active site (Glu175 and Glu293) in RmMan5A. b The protein surface charge of RmMan5A and mRmMan5A. The most negative and most positive electrostatic potentials are indicated by red and blue, respectively. c The location of Tyr233 and Lys264 in RmMan5A before mutation. d The location of His233 and Met264 in mRmMan5A after mutation. Tyr233, Lys264, and Asn343 were shown in red, blue, and purple, respectively. The active site and catalytic groove were colored in green and yellow, respectively

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