Ornithine Decarboxylation System of Shewanella baltica Regulates Putrescine Production and Acid Resistance

Bao, Xingyue; Wang, Feifei; Yang, Rendi; Zhang, Yan; Fu, Linglin; Li, Han

doi:10.4315/jfp-20-227

Cited by 7 publications

(6 citation statements)

References 42 publications

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“…The fermentation results showed that blocking these two genes promoted the accumulation of L -ornithine; the L -ornithine titers of the NBO1 and NBO2 strains reached 1.97 g/L and 1.95 g/L, respectively. In addition, the speF gene, encoding L -ornithine decarboxylase ( Bao et al, 2021 ), was knocked out to block the catabolism of L -ornithine to putrescine in B. amyloliquefaciens NBO3 [with argF and argI genes deleted in B. amyloliquefaciens NB (Δ pgsBCA )], thereby obtaining the B. amyloliquefaciens strain NBO4. The L -ornithine titer of NBO4 was further increased to 3.51 g/L ( Figure 2B ).…”

Section: Resultsmentioning

confidence: 99%

Metabolic Engineering of Bacillus amyloliquefaciens to Efficiently Synthesize L-Ornithine From Inulin

Zhu

Hu²,

Yan³

et al. 2022

Front. Bioeng. Biotechnol.

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Bacillus amyloliquefaciens is the dominant strain used to produce γ-polyglutamic acid from inulin, a non-grain raw material. B. amyloliquefaciens has a highly efficient tricarboxylic acid cycle metabolic flux and glutamate synthesis ability. These features confer great potential for the synthesis of glutamate derivatives. However, it is challenging to efficiently convert high levels of glutamate to a particular glutamate derivative. Here, we conducted a systematic study on the biosynthesis of L-ornithine by B. amyloliquefaciens using inulin. First, the polyglutamate synthase gene pgsBCA of B. amyloliquefaciens NB was knocked out to hinder polyglutamate synthesis, resulting in the accumulation of intracellular glutamate and ATP. Second, a modular engineering strategy was applied to coordinate the degradation pathway, precursor competition pathway, and L-ornithine synthesis pathway to prompt high levels of intracellular precursor glutamate for l-ornithine synthesis. In addition, the high-efficiency L-ornithine transporter was further screened and overexpressed to reduce the feedback inhibition of L-ornithine on the synthesis pathway. Combining these strategies with further fermentation optimizations, we achieved a final L-ornithine titer of 31.3 g/L from inulin. Overall, these strategies hold great potential for strengthening microbial synthesis of high value-added products derived from glutamate.

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Section: Resultsmentioning

confidence: 99%

Metabolic Engineering of Bacillus amyloliquefaciens to Efficiently Synthesize L-Ornithine From Inulin

Zhu

Hu²,

Yan³

et al. 2022

Front. Bioeng. Biotechnol.

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“…3,19 Pereira et al demonstrated that certain microorganisms, such as Citrobacter freundii and Lactobacillus collinoides, can modulate their intracellular pH by converting ornithine to putrescine. 20 This conversion is mediated by the ornithine-dependent acid-fast system, which involves the enzymes ODC (SpeF/ODC) and the antiporter PotE, 21 which decarboxylates under the action F I G U R E 7 Phylogenetic analysis: ornithine decarboxylase (ODC) and other pyridoxal-5′-phosphate (PLP)-dependent amino decarboxylases. Each protein sequence in the phylogenetic tree is accompanied by its corresponding NCBI database number and protein source.…”

Section: Discussionmentioning

confidence: 99%

“…Pereira et al. demonstrated that certain microorganisms, such as Citrobacter freundii and Lactobacillus collinoides , can modulate their intracellular pH by converting ornithine to putrescine 20 . This conversion is mediated by the ornithine‐dependent acid‐fast system, which involves the enzymes ODC (SpeF/ODC) and the antiporter PotE, 21 which decarboxylates under the action of ODC, consuming protons and generating putrescine and gaseous ammonia.…”

Section: Discussionmentioning

confidence: 99%

Enzymatic properties of ornithine decarboxylase from Clostridium aceticum DSM1496

Tan,

Gou,

Fan

et al. 2024

Biotech and App Biochem

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Clostridium aceticum DSM1496 is an acid‐resistant strain in which ornithine decarboxylase (ODC) plays a crucial role in acid resistance. In this study, we expressed ODC derived from C. aceticum DSM1496 in Escherichia coli BL21 (DE3) and thoroughly examined its enzymatic properties. The enzyme has a molecular weight of 55.27 kDa and uses pyridoxal‐5′‐phosphate (PLP) as a coenzyme with a Km = 0.31 mM. ODC exhibits optimal activity at pH 7.5, and it maintains high stability even at pH 4.5. The peak reaction temperature for ODC is 30°C. Besides, it can be influenced by certain metal ions such as Mn2+. Although l‐ornithine serves as the preferred substrate for ODC, the enzyme also decarboxylates l‐arginine and l‐lysine simultaneously. The results indicate that ODC derived from C. aceticum DSM1496 exhibits the ability to produce putrescine, cadaverine, and agmatine through decarboxylation. These polyamines have the potential to neutralize acid in an acidic environment, facilitating the growth of microorganisms. These significant findings provide a strong basis for further investigation into the acid‐resistant mechanisms contributed by ODC.

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“…BAs are primarily created by bacteria using substrate-specific decarboxylase enzymes to decarboxylate the relevant amino acids. Because they are frequently active at acidic pH levels, these enzymes may assist in retaining pH homeostasis or shorten the development time by detoxifying the extracellular medium [ 6 ]. Free amino acids, the existence of decarboxylase-positive microbes and favorable conditions for bacterial development are all factors that the procedure of fermentation of fish may give [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

Characterization and Mechanism of Tea Polyphenols Inhibiting Biogenic Amine Accumulation in Marinated Spanish Mackerel

Chang

Zhou

et al. 2023

Foods

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Putrescine is a low-molecular-weight organic compound that is widely found in pickled foods. Although the intake of biogenic amines is beneficial to humans, an excessive intake can cause discomfort. In this study, the ornithine decarboxylase gene (ODC) was involved in putrescine biosynthesis. After cloning, expression and functional verification, it was induced and expressed in E. coli BL21 (DE3). The relative molecular mass of the recombinant soluble ODC protein was 14.87 kDa. The function of ornithine decarboxylase was analyzed by determining the amino acid and putrescine content. The results show that the ODC protein could catalyze the decarboxylation of ornithine to putrescine. Then, the three-dimensional structure of the enzyme was used as a receptor for the virtual screening of inhibitors. The binding energy of tea polyphenol ligands to the receptor was the highest at −7.2 kcal mol−1. Therefore, tea polyphenols were added to marinated fish to monitor the changes in putrescine content and were found to significantly inhibit putrescine production (p < 0.05). This study lays the foundation for further research on the enzymatic properties of ODC and provides insight into an effective inhibitor for controlling the putrescine content in pickled fish.

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Ornithine Decarboxylation System of Shewanella baltica Regulates Putrescine Production and Acid Resistance

Cited by 7 publications

References 42 publications

Metabolic Engineering of Bacillus amyloliquefaciens to Efficiently Synthesize L-Ornithine From Inulin

Metabolic Engineering of Bacillus amyloliquefaciens to Efficiently Synthesize L-Ornithine From Inulin

Enzymatic properties of ornithine decarboxylase from Clostridium aceticum DSM1496

Characterization and Mechanism of Tea Polyphenols Inhibiting Biogenic Amine Accumulation in Marinated Spanish Mackerel

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