Anita Herawati Permana1,2, Fida Madayanti Warganegara1, Deana Wahyuningrumand Akhmaloka1,4*

1Biochemistry Research Group, Faculty of Mathematics and Natural Science,
Institut Teknologi Bandung, Indonesia.
2Study Program of Quality Assurance of Food Industry, Politeknik AKA Bogor, Indonesia.
3Organic Chemistry Research Group, Faculty of Mathematics and Natural Science,
Institut Teknologi Bandung, Indonesia.
4Department of Chemistry, Faculty of Science and Computer,
Universitas Pertamina, Indonesia.

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