caa a22 4500 605506639 CHVBK 20210128100628.0 cr unu---uuuuu 210128e20150801xx s 000 0 eng 10.1007/s00253-015-6392-9 doi (NATIONALLICENCE)springer-10.1007/s00253-015-6392-9 Enzyme fusion for whole-cell biotransformation of long-chain sec -alcohols into esters [Elektronische Daten] [Eun-Yeong Jeon, A-Hyong Baek, Uwe Bornscheuer, Jin-Byung Park] 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. Springer-Verlag Berlin Heidelberg, 2015 Enzyme fusion nationallicence Whole-cell biocatalysis nationallicence Baeyer-Villiger monooxygenase nationallicence Alcohol dehydrogenase nationallicence Jeon Eun-Yeong Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea aut Baek A-Hyong Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea aut Bornscheuer Uwe Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, Greifswald University, 17487, Greifswald, Germany aut Park Jin-Byung Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/15(2015-08-01), 6267-6275 0175-7598 99:15<6267 2015 99 253 https://doi.org/10.1007/s00253-015-6392-9 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6392-9 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Jeon Eun-Yeong Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea aut NATIONALLICENCE 700 1- Baek A-Hyong Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea aut NATIONALLICENCE 700 1- Bornscheuer Uwe Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, Greifswald University, 17487, Greifswald, Germany aut NATIONALLICENCE 700 1- Park Jin-Byung Department of Food Science & Engineering, Ewha Womans University, 120-750, Seoul, Republic of Korea aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/15(2015-08-01), 6267-6275 0175-7598 99:15<6267 2015 99 253