Production of Low Molecular Weight P(3HB-co-3HV) by Butyrateacetoacetate CoA-transferase (cftAB) in Escherichia coli
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-hyd...
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Published in | Biotechnology and bioprocess engineering Vol. 25; no. 2; pp. 279 - 286 |
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Main Authors | , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Seoul
The Korean Society for Biotechnology and Bioengineering
01.04.2020
Springer Nature B.V 한국생물공학회 |
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Abstract | 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. |
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AbstractList | 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. 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. 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. KCI Citation Count: 1 |
Author | Yang, Yung-Hun Gurav, Ranjit Choi, Tae-Rim Song, Hun-Suk Park, Jun-Young Jeon, Jong-Min Yoon, Jeong-Jun Han, Yeong Hoon Seo, Seung-Oh Park, Ye Lim Bhatia, Shashi Kant Park, Hyung Yeon |
Author_xml | – sequence: 1 givenname: Tae-Rim surname: Choi fullname: Choi, Tae-Rim organization: Department of Biological Engineering, College of Engineering, Konkuk University – sequence: 2 givenname: Jong-Min surname: Jeon fullname: Jeon, Jong-Min organization: Green and Sustainable Materials R&D Department, Korea Institute of Industrial Technology (KITECH) – sequence: 3 givenname: Shashi Kant surname: Bhatia fullname: Bhatia, Shashi Kant organization: Department of Biological Engineering, College of Engineering, Konkuk University – sequence: 4 givenname: Ranjit surname: Gurav fullname: Gurav, Ranjit organization: Department of Biological Engineering, College of Engineering, Konkuk University – sequence: 5 givenname: Yeong Hoon surname: Han fullname: Han, Yeong Hoon organization: Department of Biological Engineering, College of Engineering, Konkuk University – sequence: 6 givenname: Ye Lim surname: Park fullname: Park, Ye Lim organization: Department of Biological Engineering, College of Engineering, Konkuk University – sequence: 7 givenname: Jun-Young surname: Park fullname: Park, Jun-Young organization: Department of Biological Engineering, College of Engineering, Konkuk University – sequence: 8 givenname: Hun-Suk surname: Song fullname: Song, Hun-Suk organization: Department of Biological Engineering, College of Engineering, Konkuk University – sequence: 9 givenname: Hyung Yeon surname: Park fullname: Park, Hyung Yeon organization: Department of Biological Engineering, College of Engineering, Konkuk University – sequence: 10 givenname: Jeong-Jun surname: Yoon fullname: Yoon, Jeong-Jun organization: Green and Sustainable Materials R&D Department, Korea Institute of Industrial Technology (KITECH) – sequence: 11 givenname: Seung-Oh surname: Seo fullname: Seo, Seung-Oh email: drsos@catholic.ac.kr organization: Department of Food Science and Nutrition, The Catholic University of Korea – sequence: 12 givenname: Yung-Hun surname: Yang fullname: Yang, Yung-Hun email: seokor@konkuk.ac.kr organization: Department of Biological Engineering, College of Engineering, Konkuk University |
BackLink | https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART002585282$$DAccess content in National Research Foundation of Korea (NRF) |
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Keywords | acetoacetyl-CoA acetyltransferase 3HV bioplastic polyhydroxyalkanoate acetate-CoA transferase P(3HB |
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Title | Production of Low Molecular Weight P(3HB-co-3HV) by Butyrateacetoacetate CoA-transferase (cftAB) in Escherichia coli |
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ispartofPNX | Biotechnology and Bioprocess Engineering, 2020, 25(2), , pp.279-286 |
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