Nitrilase-Catalyzed Production of Nicotinic Acid from 3-Cyanopyridine in
            <i>Rhodococcus rhodochrous</i>
            J1

Mathew, C. Deepal; Nagasawa, Tôru; Kobayashi, Michihiko; Yamada, Hideaki

doi:10.1128/aem.54.4.1030-1032.1988

Cited by 133 publications

(33 citation statements)

References 2 publications

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“…In both cases, H‐NHase is the effective enzyme. Due to the ease of cultivation and stability of R. rhodochrous J1 cells, the strain is also promising for the synthesis of various other amides [12, 13], and, furthermore, acids by a nitrilase [14].…”

Section: Discussionmentioning

confidence: 99%

Low-molecular-mass nitrile hydratase fromRhodococcus rhodochrousJ1: purification, substrate specificity and comparison with the analogous high-molecular-mass enzyme

Wieser

Takeuchi

Wada

et al. 1998

FEMS Microbiology Letters

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In addition to a previously described nitrilase and a high‐molecular‐mass nitrile hydratase, Rhodococcus rhodochrous J1 contains a second, low‐molecular‐mass nitrile hydratase, which was purified, characterized and compared with the high‐molecular‐mass enzyme. Due to its wide substrate spectrum, the low‐molecular‐mass enzyme broadens the nitrile‐converting capacity of this strain. The versatility of nitrile metabolism in this organism and the significance of the low‐molecular‐mass enzyme for the synthesis of valuable amides is discussed.

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Section: Discussionmentioning

confidence: 99%

Low-molecular-mass nitrile hydratase fromRhodococcus rhodochrousJ1: purification, substrate specificity and comparison with the analogous high-molecular-mass enzyme

Wieser

Takeuchi

Wada

et al. 1998

FEMS Microbiology Letters

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“…The above characteristics suggest the potential use of these enzymes as industrial biocatalysts. In fact, production of acrylamide [12] and nicotinic acid [13] on an industrial scale have proved the commercial ability of these enzymes.…”

Section: Introductionmentioning

confidence: 99%

Biotransformation of p‐methoxyphenylacetonitrile into p‐methoxyphenylacetic acid by resting cells of Bacillus subtilis

Chen

Zheng

Shen

2008

Biotech and App Biochem

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Resting cells of Bacillus subtilis ZJB-063 were used for the direct transformation of MOPAN (p-methoxyphenylacetonitrile) to MOPAA (p-methoxyphenylacetic acid), which is an important pharmaceutical intermediate. The B. subtilis ZJB-063 culture conditions for the production of nitrilase and the reaction conditions for this nitrilase-mediated conversion were optimized. The maximum production of nitrilase was achieved when glucose and a combination of ammonium sulfate and yeast powder were added as carbon and nitrogen sources respectively. Previously reported inducers were found to be unnecessary for the production of nitrilase from B. subtilis ZJB-063, which indicated that this nitrilase appeared to be constitutive. However, when epsilon-caprolactam (6-hexanolactam) was added as the inducer, B. subtilis ZJB-063 exhibited nitrile hydratase and amidase activity. The maximum conversion of MOPAN into MOPAA (specific activity 17.03 units.g(-1)(DCW); DCW is dry cell weight) was observed in a solution containing 50 mM phosphate buffer (pH 7.0), 10 mM MOPAN, 2.7 mg DCW.ml(-1) wet resting cells and 5% (v/v) DMSO for 4 h at 32 degrees C. MOPAN (10 mM) was completely converted into MOPAA (9.65 mM) in 5 h in shake flasks without the formation of p-methoxyphenylacetamide. The small deviation of MOPAA (9.65 mM) from the theoretical amount (10 mM) may be due to partial consumption of the products by B. subtilis ZJB-063. Both MOPAN and MOPAA inhibited the hydrolysis at concentrations above 15 mM. Scale up of the reaction to 200 ml in a bubble bioreactor shortened the reaction time compared with the reactions performed in shake flasks.

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“…In both cases, H-NHase is the e¡ective enzyme. Due to the ease of cultivation and stability of R. rhodochrous J1 cells, the strain is also promising for the synthesis of various other amides [12,13], and, furthermore, acids by a nitrilase [14].…”

Section: Discussionmentioning

confidence: 99%

Low-molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1: purification, substrate specificity and comparison with the analogous high-molecular-mass enzyme

Wieser¹

1998

FEMS Microbiology Letters

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Nitrilase-Catalyzed Production of Nicotinic Acid from 3-Cyanopyridine in Rhodococcus rhodochrous J1

Cited by 133 publications

References 2 publications

Low-molecular-mass nitrile hydratase fromRhodococcus rhodochrousJ1: purification, substrate specificity and comparison with the analogous high-molecular-mass enzyme

Low-molecular-mass nitrile hydratase fromRhodococcus rhodochrousJ1: purification, substrate specificity and comparison with the analogous high-molecular-mass enzyme

Biotransformation of p‐methoxyphenylacetonitrile into p‐methoxyphenylacetic acid by resting cells of Bacillus subtilis

Low-molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1: purification, substrate specificity and comparison with the analogous high-molecular-mass enzyme

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