The effect of temperature on the inhibition mechanism of candida rugosa lipase
| dc.contributor.author | Nurul Afini Binti Fuad | |
| dc.date.accessioned | 2021-03-10T03:53:58Z | |
| dc.date.available | 2021-03-10T03:53:58Z | |
| dc.date.issued | 2019-06 | |
| dc.description.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. | en_US |
| dc.identifier.uri | http://hdl.handle.net/123456789/11952 | |
| dc.language.iso | en | en_US |
| dc.title | The effect of temperature on the inhibition mechanism of candida rugosa lipase | en_US |
| dc.type | Other | en_US |
Files
License bundle
1 - 1 of 1
Loading...
- Name:
- license.txt
- Size:
- 1.71 KB
- Format:
- Item-specific license agreed upon to submission
- Description: