0973-7510 Journal of Pure and Applied Microbiology 2581-690X DR. M.N. Khan 10.22207/JPAM.12.2.10 The Effect of Different Matrix Bound on the Transesterification Activity of Immobilized PPD2 Lipase Herawati Permana Anita Madayanti Warganegara Fida Wahyuningrum Deana Akhmaloka Biochemistry Research Group, Faculty of Mathematics and Natural Science, Institut Teknologi Bandung, Indonesia. Study Program of Quality Assurance of Food Industry, Politeknik AKA Bogor, Indonesia. Organic Chemistry Research Group, Faculty of Mathematics and Natural Science, Institut Teknologi Bandung, Indonesia. Department of Chemistry, Faculty of Science and Computer, Universitas Pertamina, Indonesia. 30 06 2018 12 2 513 519 Copyright © 2018 The Author(s) 2018 This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International License which permits unrestricted use, sharing, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.https://creativecommons.org/licenses/by/4.0/

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 xyz