1) Yes, at optimal conditions you'd get that. Mind though, if you have less, then the enzyme just produces less proportionately, per minute. HOwever
you can't scale this up forever, you may get substrate or product inhibition (both which are subject to vast analyses in the literature). So it
depends on the enzyme. But at those low concentrations, I'm sure you can scale this up for a fair bit.
2) Whether it's economical or not, it depends on the price of urease compared to other industrial methods. For trials at home, it certainluy is
economical. You could even attempt to purify the urease yourself. I can help you on this, providing you got a source that contains a fair bit.
3) It is odd that they use K2HPO4 as a buffer, but yet they say it's an inhibitor. I don't think it's a very strong inhibitor. Otherwise, you can
always make a buffer with some other ions, i.e. Tris HCl or something. Li is likely to be better then, yes. Also note the temperature max activity is
at 60 deg C. You may not want that because you are likely going to inactivate protein. So I'd rather keep it at i.e. 30 deg C and save the protein.
4) There you have it, the main caveat. As the reaction proceeds in water, you will mainly get ammonium carbonate. So you won't have any gas bubbles
appearing reagardless. You'll just get an increasingly concentrated solution of (NH4)2CO3. This you can of course extract later by crystallisation.
Other than that, there isn't much to maintain - just check the ammonium carbonate doesnt change the ph significantly,
Never Stop to Begin, and Never Begin to Stop...
Tolerance is good. But not with the intolerant! (Wilhelm Busch)
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