Badillo-Zeferino_2017_Biotechnol.Appl.Biochem_64_62

Production of recombinant thermo-alkali-stable lipase LipMatCCR11, expressed in Escherichia coli BL21 (DE3), was investigated via response surface methodology by using a face-centered design with three levels of each factor. Additionally, improvement of the catalytic performance of expressed lipase was assessed by immobilization on microporous polypropylene. Results showed that inducer (isopropyl beta-d-1-thiogalactopyranoside [IPTG]) concentration and temperature were found to be the significant factors (P < 0.05). The maximum lipase expression was obtained at IPTG 0.6 mM, 16 degrees C, and 18 H, with a specific lipase activity of 7.29 x 106 U/mg, which was 36.4 times higher (over 1,300-fold increase) than lipase activity measured under nonoptimized conditions. On the other hand, immobilized lipase showed a high biocatalytic activity, particularly in the synthesis of aroma esters.