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Expression Levels of Chaperones Influence Biotransformation Activity of Recombinant Escherichia Coli Expressing Micrococcus Luteus Alcohol Dehydrogenase and Pseudomonas Putida Baeyer-Villiger Monooxygenase

Title
Expression Levels of Chaperones Influence Biotransformation Activity of Recombinant Escherichia Coli Expressing Micrococcus Luteus Alcohol Dehydrogenase and Pseudomonas Putida Baeyer-Villiger Monooxygenase
Authors
Baek, A-HyongJeon, Eun-YeongLee, Sun-MeePark, Jin-Byung
Ewha Authors
박진병
SCOPUS Author ID
박진병scopus
Issue Date
2015
Journal Title
BIOTECHNOLOGY AND BIOENGINEERING
ISSN
0006-3592JCR Link1097-0290JCR Link
Citation
vol. 112, no. 5, pp. 889 - 895
Keywords
chaperonesgamma-prefoldinthermosomewhole-cell biocatalysisBaeyer-Villiger monooxygenasealcohol dehydrogenasericinoleic acidEscherichia coli
Publisher
WILEY-BLACKWELL
Indexed
SCI; SCIE; SCOPUS WOS
Abstract
We demonstrated for the first time that the archaeal chaperones (i.e., -prefoldin and thermosome) can stabilize enzyme activity in vivo. Ricinoleic acid biotransformation activity of recombinant Escherichia coli expressing Micrococcus luteus alcohol dehydrogenase and the Pseudomonas putida KT2440 Baeyer-Villiger monooxygenase improved significantly with co-expression of -prefoldin or recombinant themosome originating from the deep-sea hyperthermophile archaea Methanocaldococcus jannaschii. Furthermore, the degree of enhanced activity was dependent on the expression levels of the chaperones. For example, whole-cell biotransformation activity was highest at 12 mu mol/g dry cells/min when -prefoldin expression level was approximately 46% of the theoretical maximum. This value was approximately two-fold greater than that in E. coli, where the -prefoldin expression level was zero or set to the theoretical maximum. Therefore, it was assumed that the expression levels of chaperones must be optimized to achieve maximum biotransformation activity in whole-cell biocatalysts. Biotechnol. Bioeng. 2015;112: 889-895. (c) 2014 Wiley Periodicals, Inc.
DOI
10.1002/bit.25521
Appears in Collections:
엘텍공과대학 > 식품공학전공 > Journal papers
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