Partial purification of monoterpene synthase extracted from the young leaf of Michelia alba, by using Mono-Q ion exchange chromatography
2004
Lee, Y. C. | Radzali M. | Mohd Arif S. | Mohd Yunus S.
This preliminary research work was conducted in order to partially purified monoterpene synthase from the young leaf of Michelia alba (Magnoliaceae family). Five stages of partial purification was needed, including crude leaf extraction, ultracentrifugation, dialysis, removal of phenol compounds and Mono-Q ion exchange chromatography. As the results of the experiment, the monoterpene synthase (MSase)enzyme was partially purified for 3.3 fold and the final recovery rate is 19.8 %. A SPME -GCFID technique was used to identify and quantify the end products of the reaction activity of the particular MSase enzyme. The substrate used in this experiment is Geranylpyrophosphate (GPP).The Vmax value of monoterpene synthase (MSase) is 6.7 ng product/min and its Km value is 83µM substrate. The study of this particular enzyme activity using different substrates (namely GGPP and IPP ) show no reaction at all. Inhibitors such as EGTA and EDTA show -50% of inhibition of enzyme reaction at the final concentration of 15mM.
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