Fig. 4
From: Computational design of highly stable and soluble alcohol dehydrogenase for NADPH regeneration
Characterization of CbADH mutants compared with the wild type. a Enzyme activity in shake-flask fermentation at 25 ℃ with 0.5 mM IPTG dosage. The green column represents the crude enzyme activity, while the beige column represents OD600. The red square represents the proportion of soluble protein to total protein. b Thermal stability of the wild CbADH and the mutants. c SDS-PAGE analysis of protein expression of the wild-type CbADH-WT and mutant CbADH-6M: Lane M: molecular weight marker; Lane W: whole cell protein; Lane S: supernatant; Lane P: precipitation