Citation
Lee Y. C., . and Radzali M., . and Mohd Arif S., . and Mohd Yunus S., . (2004) Partial purification of monoterpene synthase extracted from the young leaf of Michelia alba by using Mono-Q ion exchange chromatography. [Proceedings Paper]
Abstract
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 MSaseenzyme 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 83M 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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Abstract
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 MSaseenzyme 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 83M 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.
Additional Metadata
| Item Type: | Proceedings Paper |
|---|---|
| Additional Information: | Available at Perpustakaan Sultan Abdul Samad Universiti Putra Malaysia 43400 UPM Serdang Selangor Malaysia. QK710.2 M239 2004 Call Number |
| AGROVOC Term: | Magnoliaceae |
| AGROVOC Term: | Michelia |
| AGROVOC Term: | Leaves |
| AGROVOC Term: | Flower extracts |
| AGROVOC Term: | Ion exchange chromatography |
| AGROVOC Term: | Enzymatic activity |
| AGROVOC Term: | Monoterpenes |
| AGROVOC Term: | Ultracentrifugation |
| AGROVOC Term: | Dialysis |
| AGROVOC Term: | Purification |
| Geographical Term: | MALAYSIA |
| Depositing User: | Ms. Suzila Mohamad Kasim |
| Last Modified: | 24 Apr 2025 05:15 |
| URI: | http://webagris.upm.edu.my/id/eprint/12812 |
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