Structured Review

GenScript adp1 genome
(A) Growth (represented as OD 600 ) of the strains W1 and <t>ADP1</t> WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​
Adp1 Genome, supplied by GenScript, used in various techniques. Bioz Stars score: 80/100, based on 0 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/adp1 genome/product/GenScript
Average 80 stars, based on 1 article reviews
Price from $9.99 to $1999.99
adp1 genome - by Bioz Stars, 2020-09
80/100 stars

Related Products / Commonly Used Together

reference genome
acn1667 whole genome sequencing

Images

1) Product Images from "Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1"

Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

Journal: Metabolic Engineering Communications

doi: 10.1016/j.mec.2020.e00128

(A) Growth (represented as OD 600 ) of the strains W1 and ADP1 WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​
Figure Legend Snippet: (A) Growth (represented as OD 600 ) of the strains W1 and ADP1 WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​

Techniques Used:

Comparison of (A) WE titer, (B) content and (C) CDW between ADP1 WT and W1 when grown in 50% baker’s yeast hydrolysate. The results represent the mean of two replicates and the error bars represent the standard deviations. (D) WE visualization by TLC. For each strain, the same amount of biomass was taken for lipid extraction. The extracted lipid was analyzed with TLC. Jojoba oil was used as the standard of WEs. ∗ P ​
Figure Legend Snippet: Comparison of (A) WE titer, (B) content and (C) CDW between ADP1 WT and W1 when grown in 50% baker’s yeast hydrolysate. The results represent the mean of two replicates and the error bars represent the standard deviations. (D) WE visualization by TLC. For each strain, the same amount of biomass was taken for lipid extraction. The extracted lipid was analyzed with TLC. Jojoba oil was used as the standard of WEs. ∗ P ​

Techniques Used: Thin Layer Chromatography

(A) Removal of the glyoxylate shunt hypothetically increases the availability of the central metabolite, acetyl-CoA, for fatty acid synthesis and energy generation. (B) The simplified metabolic pathway for the synthesis of wax esters from glucose and amino acids by A. baylyi ADP1. In the engineered strain, the gene aceA encoding for the isocitrate lyase, was deleted, blocking the glyoxylate shunt. The gene acr1 , encoding for the fatty acyl-CoA reductase, was overexpressed to facilitate wax ester production. In the final step of wax ester synthesis, fatty alcohol is esterified with fatty acyl-CoA by wax ester synthase (wax-dgaT).
Figure Legend Snippet: (A) Removal of the glyoxylate shunt hypothetically increases the availability of the central metabolite, acetyl-CoA, for fatty acid synthesis and energy generation. (B) The simplified metabolic pathway for the synthesis of wax esters from glucose and amino acids by A. baylyi ADP1. In the engineered strain, the gene aceA encoding for the isocitrate lyase, was deleted, blocking the glyoxylate shunt. The gene acr1 , encoding for the fatty acyl-CoA reductase, was overexpressed to facilitate wax ester production. In the final step of wax ester synthesis, fatty alcohol is esterified with fatty acyl-CoA by wax ester synthase (wax-dgaT).

Techniques Used: Blocking Assay

(A) Cumulative luminescence signal generated by W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, ADP1+iluxAB and ADP1 FAR-neg.+iluxAB when grown in 200 ​mM glucose. All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations. (B) Visualization of the produced WEs by TLC (Thin-layer chromatography) analysis. The strains W1, ADP1 Acr1, ADP1 Δ aceA, and ADP1 WT were cultivated in 200 ​mM glucose for 48 ​h. For each strain, the same amount of biomass was taken for lipid extraction. Jojoba oil was used as the standard for WEs. Two replicates were analyzed and one representative image is shown.
Figure Legend Snippet: (A) Cumulative luminescence signal generated by W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, ADP1+iluxAB and ADP1 FAR-neg.+iluxAB when grown in 200 ​mM glucose. All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations. (B) Visualization of the produced WEs by TLC (Thin-layer chromatography) analysis. The strains W1, ADP1 Acr1, ADP1 Δ aceA, and ADP1 WT were cultivated in 200 ​mM glucose for 48 ​h. For each strain, the same amount of biomass was taken for lipid extraction. Jojoba oil was used as the standard for WEs. Two replicates were analyzed and one representative image is shown.

Techniques Used: Generated, Luciferase, Activity Assay, Produced, Thin Layer Chromatography

(A) Growth (determined as OD 600 ) and (B) cumulative luminescence of W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, and ADP1+iluxAB grown on alanine, asparagine, aspartate, glutamate, glutamine, and proline (the 6 amino acids can be used by A. baylyi ADP1 as sole carbon source). All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations.
Figure Legend Snippet: (A) Growth (determined as OD 600 ) and (B) cumulative luminescence of W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, and ADP1+iluxAB grown on alanine, asparagine, aspartate, glutamate, glutamine, and proline (the 6 amino acids can be used by A. baylyi ADP1 as sole carbon source). All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations.

Techniques Used: Luciferase, Activity Assay

Comparison of (A) WE titer, (B) yield, (C) content and (D) CDW between ADP1 WT and W1 after 24 ​h and 48 ​h of cultivation with 200 ​mM glucose as carbon source. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗ P ​
Figure Legend Snippet: Comparison of (A) WE titer, (B) yield, (C) content and (D) CDW between ADP1 WT and W1 after 24 ​h and 48 ​h of cultivation with 200 ​mM glucose as carbon source. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗ P ​

Techniques Used:

2) Product Images from "Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1"

Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

Journal: Metabolic Engineering Communications

doi: 10.1016/j.mec.2020.e00128

(A) Growth (represented as OD 600 ) of the strains W1 and ADP1 WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​
Figure Legend Snippet: (A) Growth (represented as OD 600 ) of the strains W1 and ADP1 WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​

Techniques Used:

Comparison of (A) WE titer, (B) content and (C) CDW between ADP1 WT and W1 when grown in 50% baker’s yeast hydrolysate. The results represent the mean of two replicates and the error bars represent the standard deviations. (D) WE visualization by TLC. For each strain, the same amount of biomass was taken for lipid extraction. The extracted lipid was analyzed with TLC. Jojoba oil was used as the standard of WEs. ∗ P ​
Figure Legend Snippet: Comparison of (A) WE titer, (B) content and (C) CDW between ADP1 WT and W1 when grown in 50% baker’s yeast hydrolysate. The results represent the mean of two replicates and the error bars represent the standard deviations. (D) WE visualization by TLC. For each strain, the same amount of biomass was taken for lipid extraction. The extracted lipid was analyzed with TLC. Jojoba oil was used as the standard of WEs. ∗ P ​

Techniques Used: Thin Layer Chromatography

(A) Removal of the glyoxylate shunt hypothetically increases the availability of the central metabolite, acetyl-CoA, for fatty acid synthesis and energy generation. (B) The simplified metabolic pathway for the synthesis of wax esters from glucose and amino acids by A. baylyi ADP1. In the engineered strain, the gene aceA encoding for the isocitrate lyase, was deleted, blocking the glyoxylate shunt. The gene acr1 , encoding for the fatty acyl-CoA reductase, was overexpressed to facilitate wax ester production. In the final step of wax ester synthesis, fatty alcohol is esterified with fatty acyl-CoA by wax ester synthase (wax-dgaT).
Figure Legend Snippet: (A) Removal of the glyoxylate shunt hypothetically increases the availability of the central metabolite, acetyl-CoA, for fatty acid synthesis and energy generation. (B) The simplified metabolic pathway for the synthesis of wax esters from glucose and amino acids by A. baylyi ADP1. In the engineered strain, the gene aceA encoding for the isocitrate lyase, was deleted, blocking the glyoxylate shunt. The gene acr1 , encoding for the fatty acyl-CoA reductase, was overexpressed to facilitate wax ester production. In the final step of wax ester synthesis, fatty alcohol is esterified with fatty acyl-CoA by wax ester synthase (wax-dgaT).

Techniques Used: Blocking Assay

(A) Cumulative luminescence signal generated by W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, ADP1+iluxAB and ADP1 FAR-neg.+iluxAB when grown in 200 ​mM glucose. All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations. (B) Visualization of the produced WEs by TLC (Thin-layer chromatography) analysis. The strains W1, ADP1 Acr1, ADP1 Δ aceA, and ADP1 WT were cultivated in 200 ​mM glucose for 48 ​h. For each strain, the same amount of biomass was taken for lipid extraction. Jojoba oil was used as the standard for WEs. Two replicates were analyzed and one representative image is shown.
Figure Legend Snippet: (A) Cumulative luminescence signal generated by W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, ADP1+iluxAB and ADP1 FAR-neg.+iluxAB when grown in 200 ​mM glucose. All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations. (B) Visualization of the produced WEs by TLC (Thin-layer chromatography) analysis. The strains W1, ADP1 Acr1, ADP1 Δ aceA, and ADP1 WT were cultivated in 200 ​mM glucose for 48 ​h. For each strain, the same amount of biomass was taken for lipid extraction. Jojoba oil was used as the standard for WEs. Two replicates were analyzed and one representative image is shown.

Techniques Used: Generated, Luciferase, Activity Assay, Produced, Thin Layer Chromatography

(A) Growth (determined as OD 600 ) and (B) cumulative luminescence of W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, and ADP1+iluxAB grown on alanine, asparagine, aspartate, glutamate, glutamine, and proline (the 6 amino acids can be used by A. baylyi ADP1 as sole carbon source). All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations.
Figure Legend Snippet: (A) Growth (determined as OD 600 ) and (B) cumulative luminescence of W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, and ADP1+iluxAB grown on alanine, asparagine, aspartate, glutamate, glutamine, and proline (the 6 amino acids can be used by A. baylyi ADP1 as sole carbon source). All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations.

Techniques Used: Luciferase, Activity Assay

Comparison of (A) WE titer, (B) yield, (C) content and (D) CDW between ADP1 WT and W1 after 24 ​h and 48 ​h of cultivation with 200 ​mM glucose as carbon source. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗ P ​
Figure Legend Snippet: Comparison of (A) WE titer, (B) yield, (C) content and (D) CDW between ADP1 WT and W1 after 24 ​h and 48 ​h of cultivation with 200 ​mM glucose as carbon source. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗ P ​

Techniques Used:

Related Articles

Clone Assay:

Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1
Article Snippet: .. To construct the strain ADP1 ΔaceA , the cassette PT5 -kan r was cloned from previously contructed plasmid PT5 -kan r /pAK400c ( ) to the plasmid pUC57(ΔaceA ) containing the sequences flanking the gene aceA in the ADP1 genome (purchased from GenScript, USA) by digestion and ligation with the restriction enzymes AvrII and MfeI. .. The resulting plasmid pUC57(ΔaceA )- PT5 -kan r was used to transform ADP1 WT to obtain the strain ADP1 ΔaceA .

Construct:

Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1
Article Snippet: .. To construct the strain ADP1 ΔaceA , the cassette PT5 -kan r was cloned from previously contructed plasmid PT5 -kan r /pAK400c ( ) to the plasmid pUC57(ΔaceA ) containing the sequences flanking the gene aceA in the ADP1 genome (purchased from GenScript, USA) by digestion and ligation with the restriction enzymes AvrII and MfeI. .. The resulting plasmid pUC57(ΔaceA )- PT5 -kan r was used to transform ADP1 WT to obtain the strain ADP1 ΔaceA .

Plasmid Preparation:

Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1
Article Snippet: .. To construct the strain ADP1 ΔaceA , the cassette PT5 -kan r was cloned from previously contructed plasmid PT5 -kan r /pAK400c ( ) to the plasmid pUC57(ΔaceA ) containing the sequences flanking the gene aceA in the ADP1 genome (purchased from GenScript, USA) by digestion and ligation with the restriction enzymes AvrII and MfeI. .. The resulting plasmid pUC57(ΔaceA )- PT5 -kan r was used to transform ADP1 WT to obtain the strain ADP1 ΔaceA .

Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1
Article Snippet: .. The plasmid pIM1463 contains the sequences flanking the prophage region in the ADP1 genome ( ). ..

Ligation:

Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1
Article Snippet: .. To construct the strain ADP1 ΔaceA , the cassette PT5 -kan r was cloned from previously contructed plasmid PT5 -kan r /pAK400c ( ) to the plasmid pUC57(ΔaceA ) containing the sequences flanking the gene aceA in the ADP1 genome (purchased from GenScript, USA) by digestion and ligation with the restriction enzymes AvrII and MfeI. .. The resulting plasmid pUC57(ΔaceA )- PT5 -kan r was used to transform ADP1 WT to obtain the strain ADP1 ΔaceA .

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 80
    dsmz adp1 genome
    (A) Growth (represented as OD 600 ) of the strains W1 and <t>ADP1</t> WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​
    Adp1 Genome, supplied by dsmz, used in various techniques. Bioz Stars score: 80/100, based on 0 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adp1 genome/product/dsmz
    Average 80 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adp1 genome - by Bioz Stars, 2020-09
    80/100 stars
      Buy from Supplier

    80
    GenScript adp1 genome
    (A) Growth (represented as OD 600 ) of the strains W1 and <t>ADP1</t> WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​
    Adp1 Genome, supplied by GenScript, used in various techniques. Bioz Stars score: 80/100, based on 0 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adp1 genome/product/GenScript
    Average 80 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adp1 genome - by Bioz Stars, 2020-09
    80/100 stars
      Buy from Supplier

    Image Search Results


    (A) Growth (represented as OD 600 ) of the strains W1 and ADP1 WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: (A) Growth (represented as OD 600 ) of the strains W1 and ADP1 WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​

    Article Snippet: To construct the strain ADP1 Acr1, an Acr1-negative strain was first constructed by transforming the wild type ADP1 with the plasmid pUC57(Δacr1 ) containing the sequences flanking the gene acr1 in the ADP1 genome (purchased from Genscript, USA).

    Techniques:

    Comparison of (A) WE titer, (B) content and (C) CDW between ADP1 WT and W1 when grown in 50% baker’s yeast hydrolysate. The results represent the mean of two replicates and the error bars represent the standard deviations. (D) WE visualization by TLC. For each strain, the same amount of biomass was taken for lipid extraction. The extracted lipid was analyzed with TLC. Jojoba oil was used as the standard of WEs. ∗ P ​

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: Comparison of (A) WE titer, (B) content and (C) CDW between ADP1 WT and W1 when grown in 50% baker’s yeast hydrolysate. The results represent the mean of two replicates and the error bars represent the standard deviations. (D) WE visualization by TLC. For each strain, the same amount of biomass was taken for lipid extraction. The extracted lipid was analyzed with TLC. Jojoba oil was used as the standard of WEs. ∗ P ​

    Article Snippet: To construct the strain ADP1 Acr1, an Acr1-negative strain was first constructed by transforming the wild type ADP1 with the plasmid pUC57(Δacr1 ) containing the sequences flanking the gene acr1 in the ADP1 genome (purchased from Genscript, USA).

    Techniques: Thin Layer Chromatography

    (A) Removal of the glyoxylate shunt hypothetically increases the availability of the central metabolite, acetyl-CoA, for fatty acid synthesis and energy generation. (B) The simplified metabolic pathway for the synthesis of wax esters from glucose and amino acids by A. baylyi ADP1. In the engineered strain, the gene aceA encoding for the isocitrate lyase, was deleted, blocking the glyoxylate shunt. The gene acr1 , encoding for the fatty acyl-CoA reductase, was overexpressed to facilitate wax ester production. In the final step of wax ester synthesis, fatty alcohol is esterified with fatty acyl-CoA by wax ester synthase (wax-dgaT).

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: (A) Removal of the glyoxylate shunt hypothetically increases the availability of the central metabolite, acetyl-CoA, for fatty acid synthesis and energy generation. (B) The simplified metabolic pathway for the synthesis of wax esters from glucose and amino acids by A. baylyi ADP1. In the engineered strain, the gene aceA encoding for the isocitrate lyase, was deleted, blocking the glyoxylate shunt. The gene acr1 , encoding for the fatty acyl-CoA reductase, was overexpressed to facilitate wax ester production. In the final step of wax ester synthesis, fatty alcohol is esterified with fatty acyl-CoA by wax ester synthase (wax-dgaT).

    Article Snippet: To construct the strain ADP1 Acr1, an Acr1-negative strain was first constructed by transforming the wild type ADP1 with the plasmid pUC57(Δacr1 ) containing the sequences flanking the gene acr1 in the ADP1 genome (purchased from Genscript, USA).

    Techniques: Blocking Assay

    (A) Cumulative luminescence signal generated by W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, ADP1+iluxAB and ADP1 FAR-neg.+iluxAB when grown in 200 ​mM glucose. All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations. (B) Visualization of the produced WEs by TLC (Thin-layer chromatography) analysis. The strains W1, ADP1 Acr1, ADP1 Δ aceA, and ADP1 WT were cultivated in 200 ​mM glucose for 48 ​h. For each strain, the same amount of biomass was taken for lipid extraction. Jojoba oil was used as the standard for WEs. Two replicates were analyzed and one representative image is shown.

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: (A) Cumulative luminescence signal generated by W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, ADP1+iluxAB and ADP1 FAR-neg.+iluxAB when grown in 200 ​mM glucose. All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations. (B) Visualization of the produced WEs by TLC (Thin-layer chromatography) analysis. The strains W1, ADP1 Acr1, ADP1 Δ aceA, and ADP1 WT were cultivated in 200 ​mM glucose for 48 ​h. For each strain, the same amount of biomass was taken for lipid extraction. Jojoba oil was used as the standard for WEs. Two replicates were analyzed and one representative image is shown.

    Article Snippet: To construct the strain ADP1 Acr1, an Acr1-negative strain was first constructed by transforming the wild type ADP1 with the plasmid pUC57(Δacr1 ) containing the sequences flanking the gene acr1 in the ADP1 genome (purchased from Genscript, USA).

    Techniques: Generated, Luciferase, Activity Assay, Produced, Thin Layer Chromatography

    (A) Growth (determined as OD 600 ) and (B) cumulative luminescence of W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, and ADP1+iluxAB grown on alanine, asparagine, aspartate, glutamate, glutamine, and proline (the 6 amino acids can be used by A. baylyi ADP1 as sole carbon source). All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations.

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: (A) Growth (determined as OD 600 ) and (B) cumulative luminescence of W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, and ADP1+iluxAB grown on alanine, asparagine, aspartate, glutamate, glutamine, and proline (the 6 amino acids can be used by A. baylyi ADP1 as sole carbon source). All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations.

    Article Snippet: To construct the strain ADP1 Acr1, an Acr1-negative strain was first constructed by transforming the wild type ADP1 with the plasmid pUC57(Δacr1 ) containing the sequences flanking the gene acr1 in the ADP1 genome (purchased from Genscript, USA).

    Techniques: Luciferase, Activity Assay

    Comparison of (A) WE titer, (B) yield, (C) content and (D) CDW between ADP1 WT and W1 after 24 ​h and 48 ​h of cultivation with 200 ​mM glucose as carbon source. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗ P ​

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: Comparison of (A) WE titer, (B) yield, (C) content and (D) CDW between ADP1 WT and W1 after 24 ​h and 48 ​h of cultivation with 200 ​mM glucose as carbon source. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗ P ​

    Article Snippet: To construct the strain ADP1 Acr1, an Acr1-negative strain was first constructed by transforming the wild type ADP1 with the plasmid pUC57(Δacr1 ) containing the sequences flanking the gene acr1 in the ADP1 genome (purchased from Genscript, USA).

    Techniques:

    (A) Growth (represented as OD 600 ) of the strains W1 and ADP1 WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: (A) Growth (represented as OD 600 ) of the strains W1 and ADP1 WT in 10 and 20 ​g/L casein amino acids. (B) Comparison of WE content between W1 and ADP1 WT in the exponential phase when grown in 10 and 20 ​g/L casein amino acids. Cells of both strains were harvested during exponential phase; ADP1 WT was harvested after 4 ​h, and WI was harvested after 11 ​h. Comparison of (C) CDW and (D) WE content between W1 and ADP1 when cultivated with 20 ​g/L yeast extract. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗∗ P ​

    Article Snippet: The plasmid pIM1463 contains the sequences flanking the prophage region in the ADP1 genome ( ).

    Techniques:

    Comparison of (A) WE titer, (B) content and (C) CDW between ADP1 WT and W1 when grown in 50% baker’s yeast hydrolysate. The results represent the mean of two replicates and the error bars represent the standard deviations. (D) WE visualization by TLC. For each strain, the same amount of biomass was taken for lipid extraction. The extracted lipid was analyzed with TLC. Jojoba oil was used as the standard of WEs. ∗ P ​

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: Comparison of (A) WE titer, (B) content and (C) CDW between ADP1 WT and W1 when grown in 50% baker’s yeast hydrolysate. The results represent the mean of two replicates and the error bars represent the standard deviations. (D) WE visualization by TLC. For each strain, the same amount of biomass was taken for lipid extraction. The extracted lipid was analyzed with TLC. Jojoba oil was used as the standard of WEs. ∗ P ​

    Article Snippet: The plasmid pIM1463 contains the sequences flanking the prophage region in the ADP1 genome ( ).

    Techniques: Thin Layer Chromatography

    (A) Removal of the glyoxylate shunt hypothetically increases the availability of the central metabolite, acetyl-CoA, for fatty acid synthesis and energy generation. (B) The simplified metabolic pathway for the synthesis of wax esters from glucose and amino acids by A. baylyi ADP1. In the engineered strain, the gene aceA encoding for the isocitrate lyase, was deleted, blocking the glyoxylate shunt. The gene acr1 , encoding for the fatty acyl-CoA reductase, was overexpressed to facilitate wax ester production. In the final step of wax ester synthesis, fatty alcohol is esterified with fatty acyl-CoA by wax ester synthase (wax-dgaT).

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: (A) Removal of the glyoxylate shunt hypothetically increases the availability of the central metabolite, acetyl-CoA, for fatty acid synthesis and energy generation. (B) The simplified metabolic pathway for the synthesis of wax esters from glucose and amino acids by A. baylyi ADP1. In the engineered strain, the gene aceA encoding for the isocitrate lyase, was deleted, blocking the glyoxylate shunt. The gene acr1 , encoding for the fatty acyl-CoA reductase, was overexpressed to facilitate wax ester production. In the final step of wax ester synthesis, fatty alcohol is esterified with fatty acyl-CoA by wax ester synthase (wax-dgaT).

    Article Snippet: The plasmid pIM1463 contains the sequences flanking the prophage region in the ADP1 genome ( ).

    Techniques: Blocking Assay

    (A) Cumulative luminescence signal generated by W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, ADP1+iluxAB and ADP1 FAR-neg.+iluxAB when grown in 200 ​mM glucose. All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations. (B) Visualization of the produced WEs by TLC (Thin-layer chromatography) analysis. The strains W1, ADP1 Acr1, ADP1 Δ aceA, and ADP1 WT were cultivated in 200 ​mM glucose for 48 ​h. For each strain, the same amount of biomass was taken for lipid extraction. Jojoba oil was used as the standard for WEs. Two replicates were analyzed and one representative image is shown.

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: (A) Cumulative luminescence signal generated by W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, ADP1+iluxAB and ADP1 FAR-neg.+iluxAB when grown in 200 ​mM glucose. All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations. (B) Visualization of the produced WEs by TLC (Thin-layer chromatography) analysis. The strains W1, ADP1 Acr1, ADP1 Δ aceA, and ADP1 WT were cultivated in 200 ​mM glucose for 48 ​h. For each strain, the same amount of biomass was taken for lipid extraction. Jojoba oil was used as the standard for WEs. Two replicates were analyzed and one representative image is shown.

    Article Snippet: The plasmid pIM1463 contains the sequences flanking the prophage region in the ADP1 genome ( ).

    Techniques: Generated, Luciferase, Activity Assay, Produced, Thin Layer Chromatography

    (A) Growth (determined as OD 600 ) and (B) cumulative luminescence of W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, and ADP1+iluxAB grown on alanine, asparagine, aspartate, glutamate, glutamine, and proline (the 6 amino acids can be used by A. baylyi ADP1 as sole carbon source). All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations.

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: (A) Growth (determined as OD 600 ) and (B) cumulative luminescence of W1+iluxAB, ADP1 Acr1+iluxAB, ADP1 Δ aceA ​+ ​iluxAB, and ADP1+iluxAB grown on alanine, asparagine, aspartate, glutamate, glutamine, and proline (the 6 amino acids can be used by A. baylyi ADP1 as sole carbon source). All the strains express bacterial luciferase LuxAB that produces luminescence when reacting with the WE synthesis pathway intermediates, fatty aldehydes, indicating the relative activity of the synthesis pathway. The results represent the mean of two replicates and the error bars represent the standard deviations.

    Article Snippet: The plasmid pIM1463 contains the sequences flanking the prophage region in the ADP1 genome ( ).

    Techniques: Luciferase, Activity Assay

    Comparison of (A) WE titer, (B) yield, (C) content and (D) CDW between ADP1 WT and W1 after 24 ​h and 48 ​h of cultivation with 200 ​mM glucose as carbon source. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗ P ​

    Journal: Metabolic Engineering Communications

    Article Title: Wax ester production in nitrogen-rich conditions by metabolically engineered Acinetobacter baylyi ADP1

    doi: 10.1016/j.mec.2020.e00128

    Figure Lengend Snippet: Comparison of (A) WE titer, (B) yield, (C) content and (D) CDW between ADP1 WT and W1 after 24 ​h and 48 ​h of cultivation with 200 ​mM glucose as carbon source. The results represent the mean of two replicates and the error bars represent the standard deviations. ∗ P ​

    Article Snippet: The plasmid pIM1463 contains the sequences flanking the prophage region in the ADP1 genome ( ).

    Techniques: