Journal ArticleDOI
Development and evaluation of efficient recombinant Escherichia coli strains for the production of 3‐hydroxypropionic acid from glycerol
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The efficiency of the recombinant strain(s) was improved by expressing DhaB and AldH in two compatible isopropyl‐thio‐β‐galactoside inducible plasmids along with glycerol dehydratase reactivase (GDR) and it was found that the changes in protein expression were associated with their enzymatic activity and balance.Abstract:
3-Hydroxypropionic acid (3-HP) is a commercially valuable chemical with the potential to be a key building block for deriving many industrially important chemicals. However, its biological production has not been well documented. Our previous study demonstrated the feasibility of producing 3-HP from glycerol using the recombinant Escherichia coli SH254 expressing glycerol dehydratase (DhaB) and aldehyde dehydrogenase (AldH), and reported that an "imbalance between the two enzymes" and the "instability of the first enzyme DhaB" were the major factors limiting 3-HP production. In this study, the efficiency of the recombinant strain(s) was improved by expressing DhaB and AldH in two compatible isopropyl-thio-beta-galactoside (IPTG) inducible plasmids along with glycerol dehydratase reactivase (GDR). The expression levels of the two proteins were measured. It was found that the changes in protein expression were associated with their enzymatic activity and balance. While cloning an alternate aldehyde dehydrogenase (ALDH), alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH), instead of AldH, the recombinant E. coli SH-BGK1 showed the highest level of 3-HP production (2.8 g/L) under shake-flask conditions. When an aerobic fed-batch process was carried out under bioreactor conditions at pH 7.0, the recombinant SH-BGK1 produced 38.7 g 3-HP/L with an average yield of 35%. This article reports the highest level of 3-HP production from glycerol thus far.read more
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Metabolic engineering of Escherichia coli for direct production of 1,4-butanediol
Harry Yim,Robert Haselbeck,Wei Niu,Catherine J. Pujol-Baxley,Anthony P. Burgard,Jeff Boldt,Julia Khandurina,John D. Trawick,Robin E. Osterhout,Rosary Stephen,Jazell Estadilla,Sy Teisan,H. Brett Schreyer,Stefan Andrae,Tae Hoon Yang,Sang Yup Lee,Mark J. Burk,Stephen J. Van Dien +17 more
TL;DR: This work engineered the E. coli host to enhance anaerobic operation of the oxidative tricarboxylic acid cycle, thereby generating reducing power to drive the BDO pathway, leading to a strain of Escherichia coli capable of producing 18 g l(-1) of this highly reduced, non-natural chemical.
Journal ArticleDOI
Catalytic Conversion of Carbohydrates to Initial Platform Chemicals: Chemistry and Sustainability
TL;DR: Recent advances and developments in catalytic transformations of the carbohydrate content of lignocellulosic biomass to IPCs (i.e., ethanol, 3-hydroxypropionic acid, isoprene, succinic and levulinic acids, furfural, and 5-hydroxymethylfurfural) are overviewed.
Journal ArticleDOI
Valorization of industrial waste and by-product streams via fermentation for the production of chemicals and biopolymers
Apostolis A. Koutinas,Anestis Vlysidis,Daniel Pleissner,Nikolaos Kopsahelis,Isabel Lopez Garcia,Ioannis K. Kookos,Seraphim Papanikolaou,Tsz Him Kwan,Carol Sze Ki Lin +8 more
TL;DR: It is evident that fermentative production of chemicals and biopolymers via refining of waste and by-product streams is a highly important research area with significant prospects for industrial applications.
Journal ArticleDOI
Transformation of biomass into commodity chemicals using enzymes or cells
Journal ArticleDOI
Bio-based production of C2–C6 platform chemicals
Yu-Sin Jang,Byoungjin Kim,Jae Ho Shin,Yong-Jun Choi,Sol Choi,Chan Woo Song,Joungmin Lee,Hye Gwon Park,Sang Yup Lee +8 more
TL;DR: This study reviews the current status of the bio‐based production of major C2–C6 platform chemicals, focusing on the microbial production of platform chemicals that have been used for the production of chemical intermediates, building block compounds, and polymers.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal ArticleDOI
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
Book
Molecular Cloning: A Laboratory Manual
TL;DR: Molecular Cloning has served as the foundation of technical expertise in labs worldwide for 30 years as mentioned in this paper and has been so popular, or so influential, that no other manual has been more widely used and influential.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Book
Molecular cloning : a laboratory manual
Joseph Sambrook,David W. Russell +1 more
TL;DR: The content has been entirely recast to include nucleic-acid based methods selected as the most widely used and valuable in molecular and cellular biology laboratories.