Bench scale production of nicotinic acid using a newly isolated Stenotrophomonas maltophilia AC21 producing highly-inducible and versatile nitrilase

Badoei-dalfard, Arastoo; Karami, Zahra; Ramezani-pour, Narjes

doi:10.1016/j.molcatb.2016.11.019

Cited by 13 publications

(6 citation statements)

References 34 publications

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“…Wolbachia has been shown to have highly conserved pathways for synthesis of vitamins [54] and can also provide vitamins, biotin, and riboflavin to their hosts [55][56][57]. Nicotinic acid (B3) is generally present in the form of nicotinic acid amide co-enzyme (NAD, nicotinamide-adenine dinucleotide and NADP, nicotinamide-adenine dinucleotide PLOS PATHOGENS phosphate) [58], pantothenic acid is an obligate precursor of coenzyme A (CoA) [59,60], and Vitamin H is the coenzyme of acetylcoa carboxylase, pyruvate fusinase and many other enzymes [61], all of them play vital roles in the oxidation-reduction reaction. Therefore, Wolbachia infection may induce paternal defects in hosts through changing the vitamin levels and thus the oxidation-reduction pathway.…”

Section: Plos Pathogensmentioning

confidence: 99%

Metabolomics provide new insights into mechanisms of Wolbachia-induced paternal defects in Drosophila melanogaster

et al. 2021

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Wolbachia is a group of intracellular symbiotic bacteria that widely infect arthropods and nematodes. Wolbachia infection can regulate host reproduction with the most common phenotype in insects being cytoplasmic incompatibility (CI), which results in embryonic lethality when uninfected eggs fertilized with sperms from infected males. This suggests that CI-induced defects are mainly in paternal side. However, whether Wolbachia-induced metabolic changes play a role in the mechanism of paternal-linked defects in embryonic development is not known. In the current study, we first use untargeted metabolomics method with LC-MS to explore how Wolbachia infection influences the metabolite profiling of the insect hosts. The untargeted metabolomics revealed 414 potential differential metabolites between Wolbachia-infected and uninfected 1-day-old (1d) male flies. Most of the differential metabolites were significantly up-regulated due to Wolbachia infection. Thirty-four metabolic pathways such as carbohydrate, lipid and amino acid, and vitamin and cofactor metabolism were affected by Wolbachia infection. Then, we applied targeted metabolomics analysis with GC-MS and showed that Wolbachia infection resulted in an increased energy expenditure of the host by regulating glycometabolism and fatty acid catabolism, which was compensated by increased food uptake. Furthermore, overexpressing two acyl-CoA catabolism related genes, Dbi (coding for diazepam-binding inhibitor) or Mcad (coding for medium-chain acyl-CoA dehydrogenase), ubiquitously or specially in testes caused significantly decreased paternal-effect egg hatch rate. Oxidative stress and abnormal mitochondria induced by Wolbachia infection disrupted the formation of sperm nebenkern. These findings provide new insights into mechanisms of Wolbachia-induced paternal defects from metabolic phenotypes.

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Section: Plos Pathogensmentioning

confidence: 99%

Metabolomics provide new insights into mechanisms of Wolbachia-induced paternal defects in Drosophila melanogaster

et al. 2021

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“…A broad spectrum of microorganisms described in the literature has the potential to produce nitrilase and/or nitrile hydratase/amidase enzyme systems when induced by nitriles 7,20,22–24 . Many of these microorganisms can express one or both enzyme systems due to a range of factors, such as gene determination, induction by different types of nitrile, and nature of substances in the microenvironment, in addition to different types of carbohydrates, temperature, and pH of microorganism growth 19 . Based on the results obtained in microbial screening for phenylacetonitrile in the present study, colorimetric studies were performed to evaluate the production and distinction of nitrilase and nitrile hydratase/amidase enzymes in situations a (with glucose) and b (without glucose).…”

Section: Resultsmentioning

confidence: 99%

“…7,20,[22][23][24] Many of these microorganisms can express one or both enzyme systems due to a range of factors, such as gene determination, induction by different types of nitrile, and nature of substances in the microenvironment, in addition to different types of carbohydrates, temperature, and pH of microorganism growth. 19 Based on the results obtained in microbial screening for phenylacetonitrile in the present study, colorimetric studies were performed to evaluate the production and distinction of nitrilase and nitrile hydratase/amidase enzymes in situations a (with glucose) and b (without glucose). Therefore, the enzyme screening was performed in an Elisa microplate with triplicate assays and with the following appropriate control solutions: microbial, acetonitrile, acetic acid, acetamide, and DEPA, as well as the control solution without the presence of DEPA (Figure 1A).…”

Section: Enzyme Screeningmentioning

confidence: 99%

“…The profile and enzymatic behavior of nitrilases and nitrile hydratases/amidases in different microorganisms can be determined using colorimetric methods. 3,18,19 Angelini et al, 18 for example, evaluated the distinction between nitrilase and nitrile hydratase enzymes in different microorganisms through colorimetry. Sahu et al 3 screened 108 bacterial strains isolated from soil samples and used colorimetry analysis to determine differences among the strains based on pH changes.…”

Section: Introductionmentioning

confidence: 99%

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High‐throughput screening for distinguishing nitrilases from nitrile hydratases in Aspergillus and application of a Box–Behnken design for the optimization of nitrilase

Santos

Menezes

Santos

et al. 2021

Biotech and App Biochem

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Nitrilases and nitrile hydratases/amidases hydrolyze nitriles into carboxylic acids and/or amides, which are used in industrial chemical processes. In the present study, 26 microorganisms, including yeasts and filamentous fungi, in a minimum solid mineral medium supplemented with glucose and phenylacetonitrile were screened to evaluate their biocatalytic potential. Of these microorganisms, five fungi of the genus Aspergillus were selected and subjected to colorimetry studies to evaluate the production and distinction of nitrilase and nitrile hydratase/amidase enzymes. Aspergillus parasiticus Speare 7967 and A. niger Tiegh. 8285 produced nitrilases and nitrile hydratase, respectively. Nitrilase optimization was performed using a Box–Behnken design (BBD) and fungus A. parasiticus Speare 7967 with phenylacetonitrile volume (μl), pH, and carbohydrate source (starch:glucose; g/g) as independent variables and nitrilase activity (U ml–1) as dependent variable. Maximum activity (2.97 × 10–3 U ml–1) was obtained at pH 5.5, 80 μl of phenylacetonitrile, and 15 g of glucose. A. parasiticus Speare 7967 showed promise in the biotransformation of nitriles to carboxylic acids.

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“…[ 32,33 ] Different technologies have been applied from resting cells harboring nitrilase to recombinant enzymes in various forms, purified, lysates or whole cells, in batches or immobilized forms. [ 34,35,36,37 ] Here, the reusability of immobilized nitrilase using various supports was investigated to select the most efficient immobilization method. At the same time, this study focused on the identification of a more robust enzyme that can remain stable for days.…”

Section: Introductionmentioning

confidence: 99%

Nitrilase immobilization and transposition from a micro‐scale batch to a continuous process increase the nicotinic acid productivity

Teepakorn

Zajkoska

Cwicklinski

et al. 2021

Biotechnology Journal

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In recent years, many biocatalytic processes have been developed for the production of chemicals and pharmaceuticals. In this context, enzyme immobilization methods have attracted attention for their advantages, such as continuous production and increased stability. Here, enzyme immobilization methods and a collection of nitrilases from biodiversity for the conversion of 3‐cyanopyridine to nicotinic acid were screened. Substrate conversion over 10 conversion cycles was monitored to optimize the process. The best immobilization conditions were found with cross‐linking using glutaraldehyde to modify the PMMA beads. This method showed good activity over 10 cycles in a batch reactor at 30 and 40°C. Finally, production with a new thermostable nitrilase was examined in a continuous packed bed reactor, showing very high stability of the biocatalytic process at a flow rate of 0.12 ml min–1 and a temperature of 50°C. The complete conversion of 3‐cyanopyridine was obtained over 30 days of operation. Future steps will concern reactor scale‐up to increase the production rate with reasonable pressure drops.

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Bench scale production of nicotinic acid using a newly isolated Stenotrophomonas maltophilia AC21 producing highly-inducible and versatile nitrilase

Cited by 13 publications

References 34 publications

Metabolomics provide new insights into mechanisms of Wolbachia-induced paternal defects in Drosophila melanogaster

Metabolomics provide new insights into mechanisms of Wolbachia-induced paternal defects in Drosophila melanogaster

High‐throughput screening for distinguishing nitrilases from nitrile hydratases in Aspergillus and application of a Box–Behnken design for the optimization of nitrilase

Nitrilase immobilization and transposition from a micro‐scale batch to a continuous process increase the nicotinic acid productivity

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