Cloning and characterization of gluconolactone oxidase of Penicillium cyaneo-fulvum ATCC 10431 and evaluation of its use for production of D-erythorbic acid in recombinant Pichia pastoris

Article Abstract:

The gluconolactone oxidase (GLO) of Penicillium cyaneo-fulvum was purified, the corresponding gene was cloned and sequenced, the recombinant enzyme was characterized and the feasibility of producing glucode-D-erythorbic acid is demonstrated. The results suggest that unlike other known lactone oxidases, GLO is synthesized in the form of a preprotein having a 20-amino-acid N-terminal secretion signal.

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Inactivation of lys7 gene, encoding saccharopine reductase in Penicillium chrysogenum, leads to accumulation of the secondary metabolite precursors Piperdine-6-Carboxylic acid and Pipecolic acid from alpha-aminoadipic acid

Article Abstract:

Pipecolic acid, a product of lysine, is an important compound that acts as a precursor to the biosynthesis of alkaloids slfamine and swainsomine. Penicillium chrysogenum has an active alpha-aminoadipic acid pathway, which is used for synthesis of this precursor to penicillin and it was found that P.chrysogenum lys7 disruption mutants have the ability to produce Pipecolic acid in large quantities.

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Uptake of the beta-lactam precursor alpha-aminoadipic acid in Penicillium chrysogenum is mediated by the acidic and the general amino acid permease

Article Abstract:

The analysis of the uptake of alpha-AAA by Penicillium chrysogenum and the two major uptake routes (the acidic amino acid permease and the general amino acid permease) are described. The results suggested that both systems contribute to the uptake of alpha-AAA by P. chrysogenum under conditions in which beta-lactams are formed.

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