Production of 1,3-propanediol using a novel 1,3-propanediol dehydrogenase from isolated Clostridium butyricum and co-biotransformation of whole cells

Yun, Jimmy; Yang, Miaomiao; Magocha, Tinashe Archbold; Zhang, Huan‐Huan; Xue, Yanbo; Zhang, Guoyan; Qi, Xianghui; Sun, Wenjing

doi:10.1016/j.biortech.2017.09.180

Cited by 33 publications

(11 citation statements)

References 33 publications

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“…The plasmid was then transformed into E. coli Rosetta (DE3) cells by heat shock method and the transformants were cultured in 0.5 L LB-containing kanamycin (50 µg/mL) at 37 • C, 200 rpm. After cells reaching OD 600 at 0.6-0.8, enzyme expression was induced by adding 1 mM of IPTG (Yun et al, 2018). The culture was then incubated overnight at 25 • C and 150 rpm.…”

Section: Gene Mining Cloning and Expressionmentioning

confidence: 99%

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

et al. 2020

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D-allulose, which is one of the important rare sugars, has gained significant attention in the food and pharmaceutical industries as a potential alternative to sucrose and fructose. Enzymes belonging to the D-tagatose 3-epimerase (DTEase) family can reversibly catalyze the epimerization of D-fructose at the C3 position and convert it into D-allulose by a good number of naturally occurring microorganisms. However, microbial synthesis of D-allulose is still at its immature stage in the industrial arena, mostly due to the preference of slightly acidic conditions for Izumoring reactions. Discovery of novel DTEase that works at acidic conditions is highly preferred for industrial applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was applications. In this study, a novel DTEase, DTE-CM, capable of catalyzing D-fructose into D-allulose was DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The DTE-CM on D-fructose was found to be remarkably influenced and modulated by the type of metal ions (co-factors). The 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on D-fructose at pH 6.0 and 50°C from 0.5 to 3.5 h at a concentration of 0.1 mM. The enzyme exhibited its maximum catalytic activity on -fructose at pH 6.0 and 50°C with a Kcat/Km value of 45 mM−1min−1. The 500 g/L D-fructose, which corresponded to 30% conversion rate. With these interesting catalytic properties, this enzyme could be a promising candidate for industrial biocatalytic applications.

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Section: Gene Mining Cloning and Expressionmentioning

confidence: 99%

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

et al. 2020

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“…coli B21(DE3)-araA was grown in LB broth at 37 • C and 200 rpm until OD 600 value reached to 0.4-0.6. Then, 1.0 mM of IPTG was added to it for inducing the expression of gene, and incubated for further 10 h at 25 • C and 120 rpm (Yun et al, 2018). Due to strong expression and misfolding of BAAI during induction process, recombinant BAAI formed inclusion bodies as also reported for L-AI of C. hylemonae (Nguyen et al, 2018).…”

Section: Expression and Purification Of Recombinant Baaimentioning

confidence: 75%

Exploring a Highly D-Galactose Specific L-Arabinose Isomerase From Bifidobacterium adolescentis for D-Tagatose Production

Zhang

Parvez

et al. 2020

Front. Bioeng. Biotechnol.

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D-Galactose-specific L-arabinose isomerase (L-AI) would have much potential for the enzymatic conversion of D-Galactose into D-tagatose, while most of the reported L-AIs are L-arabinose specific. This study explored a highly D-Galactose-specific L-AI from Bifidobacterium adolescentis (BAAI) for the production of D-tagatose. In the comparative protein-substrate docking for D-Galactose and L-arabinose, BAAI showed higher numbers of hydrogen bonds in D-Galactose-BAAI bonding site than those found in L-arabinose-BAAI bonding site. The activity of BAAI was 24.47 U/mg, and it showed good stability at temperatures up to 65 • C and a pH range 6.0-7.5. The K m , V max , and K cat /K m of BAAI were found to be 22.4 mM, 489 U/mg and 9.3 mM −1 min −1 , respectively for D-Galactose, while the respective values for L-arabinose were 40.2 mM, 275.1 U/mg, and 8.6 mM −1 min −1 . Enzymatic conversion of D-Galactose into D-tagatose by BAAI showed 56.7% conversion efficiency at 55 • C and pH 6.5 after 10 h.

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“…Moreover, the reaction process with BA/TDND cells could accumulate 282 ± 8.9 mM glutaric acid with 70.8 ± 2.2% conversion at 48 hr. Since multiple expression of heterologous proteins can be a burden for a cell (Kurland & Dong, ), similar to the whole cell co‐biotransformation involved in E. coli or Clostridium butyricum whole cells, high yield glutaric acid production was achieved by the co‐biotransformation approach using two heterologous whole cells (Qi et al, ; Yun et al, ).…”

Section: Resultsmentioning

confidence: 99%

Enhanced production of glutaric acid by NADH oxidase and GabD‐reinforced bioconversion from l‐lysine

Hong

Moon

Choi

et al. 2018

Biotech & Bioengineering

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Glutaric acid is a promising alternative chemical to phthalate plasticizer since it can be produced by the bioconversion of lysine. Though, recent studies have enabled the high-yield production of its precursor, 5-aminovaleric acid (AMV), glutaric acid production via the AMV pathway has been limited by the need for cofactors. Introduction of NAD(P)H oxidase (Nox) withGabTD enzyme remarkably diminished the demand for oxidized nicotinamide adenine dinucleotide (NAD + ). Supply of oxygen through vigorous shaking had a significant effect on the conversion of AMV with a reduced requirement of NAD + . A high conversion rate was achieved in Nox coupled GabTD reaction under optimized expression vector, terrific broth (TB), and pH 8.5 at high cell density. Supplementary expression of GabD resulted in the production of 353 ± 35 mM glutaric acid with 88.3 ± 8.7% conversion from 400 mM AMV. Moreover, the reaction with a higher concentration of AMV could produce 528 ± 21 mM glutaric acid with 66.0 ± 2.7% conversion. In addition, the co-biotransformation strategy of GabTD and DavBA whole cells could produce 282 mM glutaric acid with 70.8% conversion from lysine, compared to the 111 mM glutaric acid yield from the combined GabTD-DavBA system.

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Production of 1,3-propanediol using a novel 1,3-propanediol dehydrogenase from isolated Clostridium butyricum and co-biotransformation of whole cells

Cited by 33 publications

References 33 publications

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

Biocatalytic Synthesis of D-Allulose Using Novel D-Tagatose 3-Epimerase From Christensenella minuta

Exploring a Highly D-Galactose Specific L-Arabinose Isomerase From Bifidobacterium adolescentis for D-Tagatose Production

Enhanced production of glutaric acid by NADH oxidase and GabD‐reinforced bioconversion from l‐lysine

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