L-glutamate dehydrogenase mutant and application thereof

Abstract

Provided are an L-glutamate dehydrogenase mutant and an application thereof, the mutant mutating the amino acid residue A at position 166 and/or the amino acid residue V at position 376 shown in SEQ ID NO. 1 into a hydrophilic or small sterically hindered amino acid residue, the application performing an amination reaction of 2-oxo-4-(hydroxymethylphosphinyl)butyrate in the presence of an L-amino acid dehydrogenase mutant, an inorganic amino donor, and a reduced coenzyme NADPH, and performing an acidification reaction on the obtained L-glufosinate salt to obtain L-glufosinate. Compared to wild L-glutamate dehydrogenase, the present L-glutamate dehydrogenase mutant has a higher concentration of substrates that can be catalysed when preparing L-glufosinate, thereby increasing the efficiency of the action of the enzyme and reducing reaction costs.

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