Production of Low Molecular Weight P(3HB-co-3HV) by Butyrateacetoacetate CoA-transferase (cftAB) in Escherichia coli

• Published in: Biotechnology and bioprocess engineering Vol. 25; no. 2; pp. 279 - 286
• Main Authors: Choi, Tae-Rim, Jeon, Jong-Min, Bhatia, Shashi Kant, Gurav, Ranjit, Han, Yeong Hoon, Park, Ye Lim, Park, Jun-Young, Song, Hun-Suk, Park, Hyung Yeon, Yoon, Jeong-Jun, Seo, Seung-Oh, Yang, Yung-Hun
• Format: Journal Article
• Language: English
• Published: Seoul The Korean Society for Biotechnology and Bioengineering 01.04.2020; Springer Nature B.V; 한국생물공학회
• Subjects: 3-hydroxybutyric acid; Affinity; Bioplastics; Biopolymers; Biotechnology; Calorimetry; Chemical synthesis; Chemistry; Chemistry and Materials Science; composite polymers; E coli; Elution; Escherichia coli; Food industry; Industrial and Production Engineering; Ligands; Microorganisms; Molecular weight; NMR; Nuclear magnetic resonance; pH effects; Physical properties; Polyhydroxyalkanoates; Polymers; propionic acid; Research Paper; Sodium chloride; Thyroxine; Titration; Titration calorimetry; transferases; Zeta potential; 생물공학; acetoacetyl-CoA acetyltransferase; 3HV; bioplastic; polyhydroxyalkanoate; acetate-CoA transferase; P(3HB
• ISSN: 1226-8372; 1976-3816
• DOI: 10.1007/s12257-019-0366-1

Naturally degradable bioplastic polyhydroxyalkanoate (PHA) is a promising biopolymer and its physical properties could be changed by introducing of different monomers such as 3-hydroxybutyrate (3HB), 3-hydroxyvalerate (3HV), and 3-hydroxyhexanoate (3HHx). To produce poly(3-hydroxybutyrate- co -3-hydroxyvalerate) P(3HB- co -3HV)) including a high fraction of hydroxyvalerate, we introduced ctfAB into engineered Escherichia coli YJ200 possessing a pLW487 vector containing bktB , phaB , and phaC under control of the trc promoter. To enhance the HV fraction of P(3HB- co -3HV), the optimal concentrations of propionate, which acts as a precursor of 3HV and isopropyl β-D-1-thiogalactopyranoside, were determined and found to be 0.1 mM and 0.3%, respectively. Under the optimized conditions, E. coli , YJ201 produced P(3HB- co -3HV) containing a large amount of 3HV. Comparison with other CoA transferases showed that CtfAB produced relatively lower molecular weight copolymers. This demonstrates the necessity of identifying additional different CoA transferases, because CoA transferase can affect both the monomer fraction and molecular weight of polymers.