Screening and characterization of an Agrobacterium tumefaciens mutant strain producing high level of coenzyme Q10

•We select a mutant of Agrobacterium tumefaciens producing high levels of coenzyme Q10.•The mutant is resistant to sodium azide and menadione and shows an eight-fold increase in CoQ10 production.•The activities of GAPDH and glucosaminitol dehydrogenase increase eight-fold and three-fold, respectivel...

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Bibliographic Details
Published in:Process biochemistry (1991) 2015, Vol.50 (1), p.33-39
Main Authors: Kim, Tae-Su, Yoo, Ji-Hyun, Kim, Sang-Yong, Pan, Cheol-Ho, Kalia, Vipin C., Kang, Yun Chan, Lee, Jung-Kul
Format: Article
Language:English
Subjects:
2-Dimensional electrophoresis
Coenzyme Q10
Mutagenesis
Production
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Summary:•We select a mutant of Agrobacterium tumefaciens producing high levels of coenzyme Q10.•The mutant is resistant to sodium azide and menadione and shows an eight-fold increase in CoQ10 production.•The activities of GAPDH and glucosaminitol dehydrogenase increase eight-fold and three-fold, respectively, in the mutant. A mutant of Agrobacterium tumefaciens (S02-13) producing high levels of coenzyme Q10 (CoQ10), was selected by high-throughput screening after repeated NTG mutagenesis. Mutant S02-13 was resistant to sodium azide and menadione and showed an eight-fold increase in CoQ10 production, as compared to that of the parent strain. The amount of CoQ10 produced by this mutant reached 350mgl−1 in pH-stat fed-batch culture. Mutant S02-13 differed from wild-type in morphology, biochemical properties, and proteome profiles. Scanning electron microscopy results revealed a remarkable change in morphology: the wild-type strain had a rod shape, whereas the mutant S02-13 was coccoid. In contrast to wild-type, the mutant S02-13 strain showed a negative reaction to tryptophan deaminase and N2 reduction, and a positive reaction to nitrate production in API kit assays. The spots representing proteins that were increased in the proteome expression of the mutant S02-13 strain were identified as glyceraldehyde-3-phosphate dehydrogenase (GAPDH), glucosaminitol dehydrogenase (GlcNOH), and superoxide dismutase (SOD). In particular, the enzyme activities of GAPDH and GlcNOH increased eight-fold and three-fold, respectively, in the mutant, as compared to the wild-type.
ISSN:1359-5113
1873-3298
DOI:10.1016/j.procbio.2014.10.024