| Summary: | Enzyme immobilization was one effort to improve the operational stability of
enzymes against pH and temperature changes as well as provide the ability to be
reused. Silica was the potential matrix material for immobilization process. Silica
surface was coated by polyethyleneimine (PEI) to gives strength anion capacity,
while 2-phenypropinaldehyde addition cause hydrophobic interaction between
matrix and enzymes. Aspergillus niger 65I6 lipase that produced by Solid State
Fermentation (SSF) could catalyze sinthesis reaction of ethyl ester oleic. The aim
of this study was obtain stable and reuseable matrix for lipase A.niger 65I6
immobilization on ethyl ester oleic acid sinthesys and examine the affect of
immobilization used silica-polyethyleneimine (Si-PEI) and silicapolyethyleneimine-
2-phenylpropionaldehyde (Si-PEI-2PP) matrix for pH and
temperature stability and reusable of Aspergillus niger 65I6 lipase. Methods of
this research were consist of 3 stages (1) production of extracelluler lipase from
Aspergillus niger 65I6 by SSF, (2) lipase purification by ion exchange
chromatography and (3) lipase immobilization used Si-PEI and Si-PEI-2PP
matrix. Characterization of immobilized lipase was done by stability pH and
temperature assay, reuseable and storage stability assay. was
obtained has an activity 165,38 U/ml with protein content 8,02 mg/ml. The result
of ion exchange showed the activity of partial lipase was 105, 96 U/ml which has
fold purification 27. Characters of immobilized lipase as protein loading were
0,57 and 0,55 mg/g matrix. Immobilized lipase have pH stability pH range (5-7),
was stable at 400C, it could used on 6 times esterification reaction and have
storage stability on 40C during 6-8 days. Si-PEI and Si-PEI-2PP were potential for
A.niger 65I6 lipase immobilization. Immobilization of A.niger 65I6 lipase was
increased stability and reuseable A. niger 65I6 lipase for ethyl ester oleic acid
sinthesys.
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