Abstract
The aim of these research was the optimize in the support hydrophobic octadecilo-sepabead
by interfacial adsorption, for which the experimental design was used Box-Behnken 3 factors
and 3 levels with a total of 12 experiments and 3 replicas on the central point. The variables
and their levels selected were: force Ionic (2.5, 5.0 and 10.0 mM), time (30, 60 and 120
min) and pH (6.0; 7.0 and 8.0) and them variable answers were the activity of the enzyme
immobilized (U/g support) and the percentage immobilization. The optimum parameters of
the immobilization process were: pH 6.62, 30 min and ionic strength 10 Mm. After adjust
the parameters to the model polynomial quadratic, is obtained 11,16 U/g support for the activity of lipase immobilized, with 81.50% and 74.0% of activity relative and performance
of immobilization respectively.
by interfacial adsorption, for which the experimental design was used Box-Behnken 3 factors
and 3 levels with a total of 12 experiments and 3 replicas on the central point. The variables
and their levels selected were: force Ionic (2.5, 5.0 and 10.0 mM), time (30, 60 and 120
min) and pH (6.0; 7.0 and 8.0) and them variable answers were the activity of the enzyme
immobilized (U/g support) and the percentage immobilization. The optimum parameters of
the immobilization process were: pH 6.62, 30 min and ionic strength 10 Mm. After adjust
the parameters to the model polynomial quadratic, is obtained 11,16 U/g support for the activity of lipase immobilized, with 81.50% and 74.0% of activity relative and performance
of immobilization respectively.
Translated title of the contribution | Optimization of the process of immobilization of lipase produced by marinobacter sp ch27 in octadecilo – sepabead |
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Original language | Spanish (Peru) |
Number of pages | 11 |
Journal | Revista de la Sociedad Química del Perú |
Volume | 82 |
Issue number | 4 |
State | Published - 2016 |
Keywords
- Lipase
- Marinobacter sp
- inmovilization
- octadecyl - sepabead
- response surface methodology