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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Structure-guided protein engineering increases enzymatic activities of the SGNH family esterases

Fig. 1

Enzymatic characterizations of CrmE10 and AlinE4. a Enzymatic activities toward substrates with various chain lengths of p-nitrophenyl (p-NP) esters. The value toward p-NP hexanoate and p-NP butyrate was 100% for CrmE10 and AlinE4, respectively. b Effects of different pH on enzyme activities. Enzymatic activities were determined at a series of pH. The value obtained at pH 7.5 was taken as 100%. The gap between different pH due to the buffer changing. c Effects of temperature on enzyme activities. Enzymatic activity was determined with a series of temperatures. The values obtained at 20 °C and 40 °C were taken as 100% for CrmE10 and AlinE4, respectively. d Effects of temperature on the stability of CrmE10 and AlinE4. The values obtained without heat treatment were taken as 100%. e Effects of temperature on AlinE4 enzyme stability after incubation for different times. The values obtained without heat treatment were taken as 100%. f Effects of NaCl concentration on the activities. The values obtained without NaCl in the reaction mixture were taken as 100%. g Effects of different metal ions on the activities. The values obtained without ions in the reaction mixture were taken as 100%. h Effects of organic solvents on the activities. The values obtained without organic solvent were taken as 100%

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