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%).
Geobacillus thermoleovorans PPD2, thermostable lipase, immobilization, Ni-NTA agarose, carboxmethyl chitosan, transesterification
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