Enzyme fusion for whole-cell biotransformation of long-chain sec -alcohols into esters
Gespeichert in:
Verfasser / Beitragende:
[Eun-Yeong Jeon, A-Hyong Baek, Uwe Bornscheuer, Jin-Byung Park]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/15(2015-08-01), 6267-6275
Format:
Artikel (online)
Online Zugang:
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| 024 | 7 | 0 | |a 10.1007/s00253-015-6392-9 |2 doi |
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| 245 | 0 | 0 | |a Enzyme fusion for whole-cell biotransformation of long-chain sec -alcohols into esters |h [Elektronische Daten] |c [Eun-Yeong Jeon, A-Hyong Baek, Uwe Bornscheuer, Jin-Byung Park] |
| 520 | 3 | |a Enzyme fusion was investigated as a strategy to improve productivity of a two-step whole-cell biocatalysis. The biotransformation of long-chain sec-alcohols into esters by an alcohol dehydrogenase (ADH) and Baeyer-Villiger monooxygenases (BVMOs) was used as the model reaction. The recombinant Escherichia coli, expressing the fusion enzymes between the ADH of Micrococcus luteus NCTC2665 and the BVMO of Pseudomonas putida KT2440 or Rhodococcus jostii RHA1, showed significantly greater bioconversion activity with long-chain sec-alcohols (e.g., 12-hydroxyoctadec-9-enoic acid (1a), 13-hydroxyoctadec-9-enoic acid (2a), 14-hydroxyicos-11-enoic acid (4a)) when compared to the recombinant E. coli expressing the ADH and BVMOs independently. For instance, activity of the recombinant E. coli expressing the ADH-Gly-BVMO, in which glycine-rich peptide was used as the linker, with 1a was increased up to 22μmolg dry cells−1min−1. This value is over 40% greater than the recombinant E. coli expressing the ADH and BVMO independently. The substantial improvement appeared to be driven by an increase in the functional expression of the BVMOs and/or an increase in mass transport efficiency by localizing two active sites in close proximity. | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2015 | ||
| 690 | 7 | |a Enzyme fusion |2 nationallicence | |
| 690 | 7 | |a Whole-cell biocatalysis |2 nationallicence | |
| 690 | 7 | |a Baeyer-Villiger monooxygenase |2 nationallicence | |
| 690 | 7 | |a Alcohol dehydrogenase |2 nationallicence | |
| 700 | 1 | |a Jeon |D Eun-Yeong |u Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea |4 aut | |
| 700 | 1 | |a Baek |D A-Hyong |u Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea |4 aut | |
| 700 | 1 | |a Bornscheuer |D Uwe |u Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, Greifswald University, 17487, Greifswald, Germany |4 aut | |
| 700 | 1 | |a Park |D Jin-Byung |u Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea |4 aut | |
| 773 | 0 | |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/15(2015-08-01), 6267-6275 |x 0175-7598 |q 99:15<6267 |1 2015 |2 99 |o 253 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00253-015-6392-9 |q text/html |z Onlinezugriff via DOI |
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| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00253-015-6392-9 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Jeon |D Eun-Yeong |u Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Baek |D A-Hyong |u Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Bornscheuer |D Uwe |u Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, Greifswald University, 17487, Greifswald, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Park |D Jin-Byung |u Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/15(2015-08-01), 6267-6275 |x 0175-7598 |q 99:15<6267 |1 2015 |2 99 |o 253 | ||