The effect of temperature on the inhibition mechanism of candida rugosa lipase
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Date
2019-06
Authors
Nurul Afini Binti Fuad
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Abstract
Enzyme inhibition by the inhibitor is a common issue in the bio-catalysis. In this
work, the effect of temperature on the inhibition mechanism was investigated.
Lipase-catalyzed hydrolysis of 4-nitrophenol butyrate (4NPB) was used as a model
reaction. Prior to the investigation, the effect of substrate concentration and
temperature were studied. Finally, the effect of methanol as an inhibitor to Candida
rugosa lipase and mechanism of inhibition as well as its kinetics at different
temperatures were compared. Rate of reaction increased proportionally with
substrate concentration from 1.0 M to 5.0 M. When substrate concentration increased
from 10.0 M to 15.0 M, the reaction velocity was constant. The ideal temperature
was found to be at 40 ℃ when the pH of 7.2 was used. Lastly, it was found that the
mechanism of inhibition of Candida rugosa lipase at 30 ℃ and 40 ℃ were
uncompetitive inhibition. Whereas at temperature 50 ℃, the mechanism of inhibition
is competitive inhibition. For enzyme kinetics at 40 ℃, the maximum velocity is
higher, product easy to form while the inhibitory effect is significant compared to at
temperature 30 ℃. When the kinetics is compared based on the concentration of
inhibitor, for uncompetitive inhibition, Vmax*, Km* and KI were decreased. For the
competitive inhibition, the Vmax* remained constant, Km* increased while the KI was
decreased.