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Kinetic , generally stability limit

High temperatures are generally needed in solid state synthesis to improve reaction rates and to facilitate solid state diffusion. Solid state diffusion is typically very slow. Thus, mechanical grinding steps are important to homogenize the sample and encourage complete reaction. It is important to realize, however, that some phases decompose at elevated temperatures. For example, Ba CujOy is unstable above about 1050°C (1) and the related phase, BajYCUjOg is only stable to 860°C in one atmosphere of oxygen (2). Thus, efforts to prepare these phases require a balance between the heat put in to speed the reaction kinetics and the stability limits of the desired phase. [Pg.226]

We have seen ( 6.2.3) hat there is a close relationship between the rates of electrophilic substitutions and the stabilities of tr-complexes, and facts already quoted above suggest that no such relationship exists between those rates and the stabilities of the 7r-complexes of the kind discussed here. These two contrasting situations are further illustrated by the data given in table 6.2. As noted earlier, the parallelism of rate data for substitutions with stability data for o"-complexes is not limited to chlorination ( 6.2.4). Clearly, rr-complexes have no general mechanistic or kinetic significance in electrophilic substitutions. [Pg.118]

The optimum yield of a condensation product is obtained at the pH where Ka has a maximum. For peptide synthesis with serine proteases this coincides with the pH where the enzyme kinetic properties have their maxima. For the synthesis of penicillins with penicillin amidase, or esters with serine proteases or esterases, the pH of maximum product yield is much lower than the pH optimum of the enzymes. For penicillin amidase the pH stability is also markedly reduced at pH 4-5. Thus, in these cases, thermodynamically controlled processes for the synthesis of the condensation products are not favorable. When these enzymes are used as catalysts in thermodynamically controlled hydrolysis reactions an increase in pH increases the product yield. Penicilhn hydrolysis is generally carried out at pH about 8.0, where the enzyme has its optimum. At this pH the equiUbrium yield of hydrolysis product is about 97%. It could be further increased by increasing the pH. Due to the limited stability of the enzyme and the product 6-aminopenicillanic acid at pH>8, a higher pH is not used in the biotechnological process. [Pg.369]

Tetracycline antibiotics are generally considered relatively unstable compounds. Oxytetracycline posseses limited stability in aqueous solutions and shows specific and base catalysis, with overall hydrolysis observed to follow pseudo-first-order kinetics. The maximum stability of this drug is exhibited at pH 2, whereas the optimum stability ranges from pH 1 to 3, which accounts for the recent finding (70) that oxytetracycline has greater heat stability at pH 3 than at pH 6.9. [Pg.526]


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Kinetic , generally

Kinetic stability

Kinetic stabilization

Kinetics limitations

Stability limits

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