The Effect of Different Matrix Bound on the Transesterification Activity of Immobilized PPD2 Lipase

Abstract

Immobilization of thermostable lipase from Geobacillus thermoleovorans PPD2 (Lip-A) were carried out on Ni-NTA agarose and carboxymethyl chitosan. Free enzyme was obtained by heterologous expression in Escherichia coli as a host cell. The enzyme showed catalytic activity for transesterification reaction. Transesterification activity of immobilized lipase on Ni-NTA agarose was increased by three fold (75.04% conversion) compared to that the free enzyme (24.65%), while the activity of immobilized lipase on carboxymethyl chitosan was slightly decreased (19.86%).

Keywords

• geobacillus thermoleovorans ppd2
• thermostable lipase
• immobilization
• ni-nta agarose
• carboxmethyl chitosan
• transesterification.