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For these two substrates the enzyme has experimentally been shown to have the opposite enantioselectivity.
Therefore, these two substrates turned the biobutanol production far from being economically feasible.
Therefore, the P. excavatus proteases would have a different catalytic mechanism towards these two substrates than human plasminogen.
The lipase activities were different by using these two substrates because lipases in the organ extracts probably have different specificities towards these substrates (Gillmor et al. 1997).
But these two substrates are subject to the restrictions of the place of production and thus have not made gains in promotion and application.
However, diffusion limitations with these two substrates, especially for the higher vanadyl contents have led to the design of different mixed redox and acid solid catalysts.
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This is in agreement with the higher influence of these two substrate positions for the cleavage rates of the proteases.
These two substrate peptides of protein FTase have been suggested to have two different rate-determining transition states (TSs) in the chemical step of the enzyme.
Several experimental runs were also carried out with different mixtures of these three substrates.
The adhesive strength of Cu coatings on these three substrates was investigated.
All of these four substrates were used as sole tannin source for production of tannase under submerged fermentation.
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