Enhancement of Lactobionic Acid Productivity by Homologous Expression of Quinoprotein Glucose Dehydrogenase in Pseudomonas taetrolens

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-...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2020-11, Vol.68 (44), p.12336-12344
Main Authors: Oh, Yu-Ri, Jang, Young-Ah, Lee, Seung Soo, Kim, Jang-Ho, Hong, Soon Ho, Han, Jeong Jun, Eom, Gyeong Tae
Format: Article
Language:English
Subjects:
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biotechnology and Biological Transformations
Disaccharides - biosynthesis
Gene Expression
Glucose Dehydrogenases - genetics
Glucose Dehydrogenases - metabolism
Lactose - metabolism
Metabolic Engineering
Pseudomonas - genetics
Pseudomonas - metabolism
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Summary: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.
ISSN:0021-8561
1520-5118
DOI:10.1021/acs.jafc.0c04246