Journal
PROCESS BIOCHEMISTRY
Volume 45, Issue 2, Pages 147-152Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2009.08.018
Keywords
(S)-styrene oxide; Styrene epoxidation; Styrene monooxygenase; Chaperone; Escherichia coli
Categories
Funding
- Korea Science and Engineering Foundation (KOSEF) [R01-2006-000-10893-0]
- Ministry of Education, Science and Technology, Korea
- National Research Foundation of Korea [R01-2006-000-10893-0] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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A highly active recombinant whole-cell biocatalyst, Escherichia coli pETAB2/pG-KJE1, was developed the efficient production of (S)-styrene oxide from styrene. The recombinant E. coli overexpressed styAB the genes of styrene monooxygenase of Pseudomonas putida SN1 and coexpressed the genes encoding chaperones (i.e., GroEL-GroES and DnaK-DnaJ-GrpE). The styrene monooxygenases were produced to ca. 40% of the total soluble proteins. enabling the whole-cell activity of the recombinant of 180 U/g CDW. The high StyAB activity in turn appeared to direct cofactors and molecular oxygen to styrene epoxidation. The product yield on energy source (i.e., glucose) reached ca. 40%. In addition, biotransformation in an organic/aqueous two-liquid phase system allowed the product to accumulate to 400 mM in the organic phase within 6 h, resulting in an average specific and volumetric productivity of 6.4 mmol/g dry cells/h (106 U/g dry cells) and 67 mM/h (1110 U/L-aq), respectively. under mild reaction conditions. These results indicated that the high productivity and the high product yield on energy source were driven by the high enzyme activity. Therefore, it was concluded that oxygenase activity of whole-cell biocatalysts is one of the critical factors to determine their catalytic performance. (C) 2009 Elsevier Ltd. All rights reserved.
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