This
is the first study on improving lactobionic acid
(LBA) production capacity in Pseudomonas taetrolens by genetic engineering. First, quinoprotein glucose dehydrogenase
(GDH) was identified as the lactose-oxidizing enzyme of P. taetrolens. Of the two types of GDH genes in P. taetrolens, membrane-bound (GDH1) and soluble
(GDH2), only GDH1 showed lactose-oxidizing activity. Next, the genetic
tool system for P. taetrolens was developed
based on the pDSK519 plasmid for the first time, and GDH1 gene was
homologously expressed in P. taetrolens. Recombinant expression of the GDH1 gene enhanced intracellular
lactose-oxidizing activity and LBA production of P.
taetrolens in flask culture. In batch fermentation
of the recombinant P. taetrolens using
a 5 L bioreactor, the LBA productivity of the recombinant P. taetrolens was approximately 17% higher (8.70
g/(L h)) than that of the wild type (7.41 g/(L h)). The LBA productivity
in this study is the highest ever reported using bacteria as production
strains for LBA.
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