Conceptual Study Of Enzymatic Sugar Ester Synthesis In The PBR At Steady-State And Isothermal Conditions
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Date
2021-06-01
Authors
Mohamed Firaz, Mohamed Zarif Wazif
Journal Title
Journal ISSN
Volume Title
Publisher
Universiti Sains Malaysia
Abstract
Lipase was used widely in the production of sugar ester especially in food processing
which used PBR as the reactor. The amount of yield produce is affected by the
enzymatic activity which also effected by binding energy, temperature and amount of
concentration of the substrate used. Ideal parameters based on experimental and also
simulation path are the major problem in order to produce higher amount of sugar
esters. The equation used for simulation were obtained based on the design equation
for PBR and based on the two substrate reaction(Varde & Fogler, 2001). Two
parameters were compared to obtain an optimum yield of sugar ester which are the
temperature and the molar ratio of substrate. This parameters are validate and
compared between the results obtained from Sebatini experiment in the literature with
the simulation by using POLYMATH. From the comparison, Simulation result are
much more accurate based on the validation of R2 methods as it can improve the data
that used by the experimental. In agreement with Harwell and Co-workers, The result
that obtained by the experimental can be modify by using the simulation methods
(Harwell et al., 2017). The trend of the graph for the effect of temperature against yield
of sugar ester shows the similar shape which the yield obtained was the highest at 40
⁰C but slightly different for the effect of substrate concentration molar ratio against
yield of sugar ester as the as it stated that the molar ratio of sugar: fatty acid for
simulation should be 1:1 while for the experimental was 1:2 respectively. After
obtaining the optimum and ideal parameters and constant for the sugar ester based on
the comparison of both sources, the effect of kinetic parameter and thermodynamic
parameter were discussed. From what obtained in kinetic parameter, the higher
activation energy of substrate bind to enzyme and the lower the inhibition activation
energy will increase rate of reaction. While for the thermodynamic parameters, the
higher the activation energy of catalysis process, △Gcat, activation energy during
equilibrium, △Heq and equilibrium temperature, Teq and the lower the activation
energy of thermal inactivation process, △Ginact, will yield lower rate of reaction. This
shows that the enzyme can act ideally if the activation energy of substrate binding
higher while the inhibition activation energy is lower. Beside that, enzyme also can act
ideally if the activation energy of catalysis, activation energy during equilibrium, and
equilibrium temperature are lower while if the activation energy of thermal
inactivation process is higher.