Dear All,
I have enzymatic crud extract from Actinobacteria , I d like to extract and purify Tyrosinase, and when I use L dopa i found a heigh activity and for 2,6 DMP substrat there were no activity but for syrngaldazine there were low activity , how do you interpret this results ?
best regrads
Dear Harir,
It will be difficult to draw conclusions on the experiment you have conducted since you have used a crude extract of actinobacteria. As you might know that oxidative enzymes laccase, peroxidase, phenoxazinone synthase and tyrosinase are produced by actinobacteria and each of them has optimal pH and different characteristics.
Therefore, I suggest that you make the necessary purification and then conduct the enzymatic activity on a pure enzyme.
I am attaching a publication which I believe will be helpful and fruitful for your study.
Hoping this will be helpful,
Rafik
Same enzyme can have different activities for different substrates. Optimal pH for them can also change. Check literature to see which substrate is dominantly used for activity and reaction conditions. If all of them are then determine pH optimum for each of them. You can do this in a microtiter plate by performing reaction in different buffers. That should give you some starting ideas of you enzyme. Good luck.
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