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Production of 3-hydroxypropionic acid from glycerol by a novel recombinant Escherichia coli BL21 strain
3-Hydroxypropionic acid (3-HP) is an important platform chemical from which several commodity and specialty chemicals can be generated. The present investigation focuses on the construction and evaluation of a recombinant strain Escherichia coli SH254 that produces 3-HP from glycerol. The strain was...
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Published in: | Process biochemistry (1991) 2008-12, Vol.43 (12), p.1440-1446 |
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container_issue | 12 |
container_start_page | 1440 |
container_title | Process biochemistry (1991) |
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creator | Raj, Subramanian Mohan Rathnasingh, Chelladurai Jo, Ji-Eun Park, Sunghoon |
description | 3-Hydroxypropionic acid (3-HP) is an important platform chemical from which several commodity and specialty chemicals can be generated. The present investigation focuses on the construction and evaluation of a recombinant strain
Escherichia coli SH254 that produces 3-HP from glycerol. The strain was developed by cloning two genes,
dhaB of
Klebsiella pneumoniae DSM 2026 encoding glycerol dehydratase and
aldH of
E. coli K-12 MG1655 encoding aldehyde dehydrogenase, respectively.
In vitro assays of crude enzyme extract of glycerol dehydratase (DhaB) showed 37.0
U
mg
−1 protein on glycerol with coenzyme B
12, and partially purified aldehyde dehydrogenase (AldH) exhibited 22.8
U
mg
−1 protein on 3-hydroxypropionaldehyde (3-HPA) with NAD
+ as a cofactor. When cultivated aerobically on a glycerol medium containing yeast extract, the recombinant
E. coli SH254 produced 3-HP at a maximum of 6.5
mmol
l
−1 (0.58
g
l
−1). The highest specific rate and yield of 3-HP production were estimated as 6.6
mmol
g
−1
cdw
h
−1 and 0.48
mol
mol
−1 glycerol, respectively. Although not optimized extensively, this study is encouraging for further development of a bioprocess to produce 3-HP from glycerol. |
doi_str_mv | 10.1016/j.procbio.2008.04.027 |
format | article |
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Escherichia coli SH254 that produces 3-HP from glycerol. The strain was developed by cloning two genes,
dhaB of
Klebsiella pneumoniae DSM 2026 encoding glycerol dehydratase and
aldH of
E. coli K-12 MG1655 encoding aldehyde dehydrogenase, respectively.
In vitro assays of crude enzyme extract of glycerol dehydratase (DhaB) showed 37.0
U
mg
−1 protein on glycerol with coenzyme B
12, and partially purified aldehyde dehydrogenase (AldH) exhibited 22.8
U
mg
−1 protein on 3-hydroxypropionaldehyde (3-HPA) with NAD
+ as a cofactor. When cultivated aerobically on a glycerol medium containing yeast extract, the recombinant
E. coli SH254 produced 3-HP at a maximum of 6.5
mmol
l
−1 (0.58
g
l
−1). The highest specific rate and yield of 3-HP production were estimated as 6.6
mmol
g
−1
cdw
h
−1 and 0.48
mol
mol
−1 glycerol, respectively. Although not optimized extensively, this study is encouraging for further development of a bioprocess to produce 3-HP from glycerol.</description><identifier>ISSN: 1359-5113</identifier><identifier>EISSN: 1873-3298</identifier><identifier>DOI: 10.1016/j.procbio.2008.04.027</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>3-Hydroxypropionaldehyde ; 3-Hydroxypropionic acid ; Aldehyde dehydrogenase ; Escherichia coli ; Glycerol ; Glycerol dehydratase ; Klebsiella pneumoniae ; Recombinant E. coli</subject><ispartof>Process biochemistry (1991), 2008-12, Vol.43 (12), p.1440-1446</ispartof><rights>2008 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-207dbadc428210e7d4431290248f76a74ba962a2139b5ba52d1eff328ab168f23</citedby><cites>FETCH-LOGICAL-c474t-207dbadc428210e7d4431290248f76a74ba962a2139b5ba52d1eff328ab168f23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Raj, Subramanian Mohan</creatorcontrib><creatorcontrib>Rathnasingh, Chelladurai</creatorcontrib><creatorcontrib>Jo, Ji-Eun</creatorcontrib><creatorcontrib>Park, Sunghoon</creatorcontrib><title>Production of 3-hydroxypropionic acid from glycerol by a novel recombinant Escherichia coli BL21 strain</title><title>Process biochemistry (1991)</title><description>3-Hydroxypropionic acid (3-HP) is an important platform chemical from which several commodity and specialty chemicals can be generated. The present investigation focuses on the construction and evaluation of a recombinant strain
Escherichia coli SH254 that produces 3-HP from glycerol. The strain was developed by cloning two genes,
dhaB of
Klebsiella pneumoniae DSM 2026 encoding glycerol dehydratase and
aldH of
E. coli K-12 MG1655 encoding aldehyde dehydrogenase, respectively.
In vitro assays of crude enzyme extract of glycerol dehydratase (DhaB) showed 37.0
U
mg
−1 protein on glycerol with coenzyme B
12, and partially purified aldehyde dehydrogenase (AldH) exhibited 22.8
U
mg
−1 protein on 3-hydroxypropionaldehyde (3-HPA) with NAD
+ as a cofactor. When cultivated aerobically on a glycerol medium containing yeast extract, the recombinant
E. coli SH254 produced 3-HP at a maximum of 6.5
mmol
l
−1 (0.58
g
l
−1). The highest specific rate and yield of 3-HP production were estimated as 6.6
mmol
g
−1
cdw
h
−1 and 0.48
mol
mol
−1 glycerol, respectively. Although not optimized extensively, this study is encouraging for further development of a bioprocess to produce 3-HP from glycerol.</description><subject>3-Hydroxypropionaldehyde</subject><subject>3-Hydroxypropionic acid</subject><subject>Aldehyde dehydrogenase</subject><subject>Escherichia coli</subject><subject>Glycerol</subject><subject>Glycerol dehydratase</subject><subject>Klebsiella pneumoniae</subject><subject>Recombinant E. coli</subject><issn>1359-5113</issn><issn>1873-3298</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNqFkMtOwzAURCMEEqXwCUhesUvw9SvJCkFVHlIlWMDacmyndZXGxU4r8ve4avdd3dHVzEhzsuwecAEYxOO62AavG-cLgnFVYFZgUl5kE6hKmlNSV5dJU17nHIBeZzcxrjGmAIAn2fIreLPTg_M98i2i-Wo0wf-NqXGbfk4jpZ1BbfAbtOxGbYPvUDMihXq_tx0KVvtN43rVD2ge9coGp1dOIe07h14WBFAcgnL9bXbVqi7au9OdZj-v8-_Ze774fPuYPS9yzUo25ASXplFGM1IRwLY0jFEgNSasakuhStaoWhBFgNYNbxQnBmzbUlKpBkTVEjrNHo69acDvzsZBblzUtutUb_0uSiowE6RkZ41QC8EJ58nIj0YdfIzBtnIb3EaFUQKWB_5yLU_85YG_xEwm_in3dMzZNHfvbJBRO9tra1yCNkjj3ZmGf2yvkZQ</recordid><startdate>20081201</startdate><enddate>20081201</enddate><creator>Raj, Subramanian Mohan</creator><creator>Rathnasingh, Chelladurai</creator><creator>Jo, Ji-Eun</creator><creator>Park, Sunghoon</creator><general>Elsevier Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7U5</scope><scope>F28</scope><scope>L7M</scope></search><sort><creationdate>20081201</creationdate><title>Production of 3-hydroxypropionic acid from glycerol by a novel recombinant Escherichia coli BL21 strain</title><author>Raj, Subramanian Mohan ; Rathnasingh, Chelladurai ; Jo, Ji-Eun ; Park, Sunghoon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-207dbadc428210e7d4431290248f76a74ba962a2139b5ba52d1eff328ab168f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>3-Hydroxypropionaldehyde</topic><topic>3-Hydroxypropionic acid</topic><topic>Aldehyde dehydrogenase</topic><topic>Escherichia coli</topic><topic>Glycerol</topic><topic>Glycerol dehydratase</topic><topic>Klebsiella pneumoniae</topic><topic>Recombinant E. coli</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Raj, Subramanian Mohan</creatorcontrib><creatorcontrib>Rathnasingh, Chelladurai</creatorcontrib><creatorcontrib>Jo, Ji-Eun</creatorcontrib><creatorcontrib>Park, Sunghoon</creatorcontrib><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Process biochemistry (1991)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Raj, Subramanian Mohan</au><au>Rathnasingh, Chelladurai</au><au>Jo, Ji-Eun</au><au>Park, Sunghoon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production of 3-hydroxypropionic acid from glycerol by a novel recombinant Escherichia coli BL21 strain</atitle><jtitle>Process biochemistry (1991)</jtitle><date>2008-12-01</date><risdate>2008</risdate><volume>43</volume><issue>12</issue><spage>1440</spage><epage>1446</epage><pages>1440-1446</pages><issn>1359-5113</issn><eissn>1873-3298</eissn><abstract>3-Hydroxypropionic acid (3-HP) is an important platform chemical from which several commodity and specialty chemicals can be generated. The present investigation focuses on the construction and evaluation of a recombinant strain
Escherichia coli SH254 that produces 3-HP from glycerol. The strain was developed by cloning two genes,
dhaB of
Klebsiella pneumoniae DSM 2026 encoding glycerol dehydratase and
aldH of
E. coli K-12 MG1655 encoding aldehyde dehydrogenase, respectively.
In vitro assays of crude enzyme extract of glycerol dehydratase (DhaB) showed 37.0
U
mg
−1 protein on glycerol with coenzyme B
12, and partially purified aldehyde dehydrogenase (AldH) exhibited 22.8
U
mg
−1 protein on 3-hydroxypropionaldehyde (3-HPA) with NAD
+ as a cofactor. When cultivated aerobically on a glycerol medium containing yeast extract, the recombinant
E. coli SH254 produced 3-HP at a maximum of 6.5
mmol
l
−1 (0.58
g
l
−1). The highest specific rate and yield of 3-HP production were estimated as 6.6
mmol
g
−1
cdw
h
−1 and 0.48
mol
mol
−1 glycerol, respectively. Although not optimized extensively, this study is encouraging for further development of a bioprocess to produce 3-HP from glycerol.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.procbio.2008.04.027</doi><tpages>7</tpages></addata></record> |
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subjects | 3-Hydroxypropionaldehyde 3-Hydroxypropionic acid Aldehyde dehydrogenase Escherichia coli Glycerol Glycerol dehydratase Klebsiella pneumoniae Recombinant E. coli |
title | Production of 3-hydroxypropionic acid from glycerol by a novel recombinant Escherichia coli BL21 strain |
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