Sandbox323: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 121: | Line 121: | ||
[[Image:Enzyme units percentage increase.png|700px|left|thumb|4 degrees C yields 42.2% increase in Units of Enzyme Activity цmol/minute ]] | [[Image:Enzyme units percentage increase.png|700px|left|thumb|4 degrees C yields 42.2% increase in Units of Enzyme Activity цmol/minute ]] | ||
===Discussion and Conclusion=== | |||
42.2% increase in units of enzyme activity was a considerable gain. No replicates were done for this study. A future experiment would include replicates so t-test can be run to determine significance of the increase. Overall the temperature decrease had an effect on the conversion of PNPA to PNP. | |||
A comparison model is the thermostable esterase from the moderate thermophile Bacillus circulans. Esterase activity was associated with a protein of molecular mass 95 kDa, composed of three identical subunits of 30 kDa. The esterase activity was thermostable with a maximum activity at 55 °C using PNPA assay. Literature reported units of enzyme activity in umol/minute at rate 790% greater than 4q7q. Taken as a comparison model, 4q7q rate is quite slow.<ref name="Thermo">Kademi, A.; Ait-Abdelkader, N.; Fakhreddine, L.; Baratti, J. Purification and characterization of a thermostable esterase from the moderate thermophile Bacillus circulans. Appl. Microbiol. Biotechnol., 2000, 54(1), 173-179, https://doi.org/10.1007/s002530000353</ref> | |||
The role of the chloride cofactor was not investigated thoroughly. Chloride ion was present in all reaction conditions, so it's independence was not tested. A future experiment would be testing the functionality of the enzyme without chloride in solution compared to with chloride ion. | |||
== References == | == References == | ||
<references/> | <references/> | ||
