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Industrial Biotransformations

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d-Amino acid transaminase<br />

Bacillus sp.<br />

1 = aspartate<br />

2 = glutamate<br />

3 = 2-oxo-aspartate<br />

4 = 2-oxo-glutamate<br />

Fig. 2.6.1.21 – 1<br />

1) Reaction conditions<br />

pH: 8.0<br />

T: 42 °C<br />

medium: aqueous<br />

reaction type: amino group transfer<br />

catalyst: whole cell<br />

enzyme: d-alanine; 2-oxoglutarate aminotransferase (d-aspartase transaminase)<br />

strain: Bacillus sp.<br />

CAS (enzyme): [37277–85–3]<br />

2) Remarks<br />

O<br />

R CO 2 -<br />

+ H3N CO 2 -<br />

D-1<br />

CO 2 -<br />

alternative amine donor:<br />

+ H3N CO 2 -<br />

D-2<br />

CO2 -<br />

E<br />

O CO 2 -<br />

O CO 2 -<br />

EC 2.6.1.21<br />

NSC Technologies,<br />

Monsanto<br />

● The main drawback of transaminases is the equilibrium conversion of about 50 %.<br />

● Therefore in commercial application l-aspartate is often used as the amino donor for l-amino<br />

acid transaminase. The product decarboxylates to pyruvic acid and carbon dioxide. Pyruvic acid<br />

itself is also an α-keto acid and is converted by dimerisation using acetolactate synthase to acetolactate.<br />

The latter undergoes spontaneous decarboxylation to acetoin that can be easily<br />

removed and does not participate in other reactions.<br />

3<br />

4<br />

CO 2 -<br />

CO2 -<br />

NH3 +<br />

R CO 2 -<br />

267

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