<p>The objective of this research was to modify the matrix surfaces to obtain both hydrophobic matrix (HM) and hydrophilic-hydrophobic matrix (HHM) for enzymatic synthesis of fructose oleic ester (FOE). The modification was performed by the attachment of 2-phenylpropionaldehyde (PPA) and PPA followed by polyethyleneimine (PEI) for HM and HHM, respectively. The results from FT-IR analysis showed that the peak of stretching vibration of NH<sub>2</sub> bond decreased and it was followed by an increase of the peak vibration of –C=N– bond at wave number 1667 cm<sup>-1</sup>. The peak of bending vibrations of the C=C bond also increased. It indicated that PPA was successfully attached on matrix. For HHM, an increase in the peak area of NH<sub>2</sub> bond indicated that PEI was also successfully attached on the matrix. The optimum conditions of lipase adsorption were obtained at buffer pH 7 containing 0.5 M NaCl (9.27 mg protein/g matrix) and without NaCl (9.23 mg protein/g matrix) for HM and HHM, respectively. For FOE synthesis, the best immobilized lipase concentration was about 8% and 6% for HM and HHM, respectively. The optimum time of esterification was 24 h and 18 h for HM and HHM, respectively, in which the yields were 75.96% and 85.29%, respectively. The immobilized lipase could be used up to 3 cycles of esterification reaction. Copyright © 2016 BCREC GROUP. All rights reserved</p><p><em>Received: 21<sup>st</sup> December 2015; Revised: 23<sup>rd</sup> February 2016; Accepted: 14<sup>th</sup> April 2016</em></p><p><strong>How to Cite</strong>: Hilmanto, H., Hidayat, C., Hastuti, P. (2016). Surface Modification of Macroporous Matrix for Immobilization of Lipase for Fructose Oleic Ester Synthesis. <em>Bulletin of Chemical Reaction Engineering & Catalysis</em>, 11 (3): 339-345 (doi:10.9767/bcrec.11.3.573.339-345)</p><p><strong>Permalink/DOI:</strong> <a href="http://doi.org/10.9767/bcrec.11.3.573.339-345">http://doi.org/10.9767/bcrec.11.3.573.339-345</a></p>