Figure 1.
Amino acid hydrophobicity profile of RML.
a: 3TGL, lid-closed form, b: 4TGL, lid-open form. Red, hydrophilic residues; blue, hydrophobic residues.
Figure 2.
CDocker energy of RML mutants and wild-type with different substrates.
a and b are separate because of discrepancies in the range of their Y-axes. a and b have the same legend. For comparison with the enzyme activity data, the energy value was converted to positive.
Figure 3.
Flow cytometry of whole cell RML catalysts.
a: Asn87Ile/Asp91Val, b: His108Leu/Lys109Ile, c: Asp256Ile/His257Leu, d: His108Leu/Lys109Ile/Asp256Ile/His257Leu, e: wild-type, f: negative control.
Figure 4.
Enzyme activity of RML wild-type and mutants.
a: hydrolytic activity, b: esterification activity.
Figure 5.
OA incorporation of whole cell catalyst and commercial lipase.
a: OA incorporation in a reaction of PPP with OA for 24 h; b: OA incorporation in a reaction of palm oil with OA for 3 h and 6 h.
Figure 6.
Profiles of RML mutants and wild-type docking with PPP.
a: Asn87Ile/Asp91Val, b: His108Leu/Lys109Ile, c: Asp256Ile/His257Leu, d: His108Leu/Lys109Ile/Asp256Ile/His257Leu, e: wild-type.