Isolation of advantageous mutants of Pseudomonas chlororaphis B23 for the enzymatic production of acrylamide.

Ryuno, Koichiro; Nagasawa, Tôru; Yamada, Hideaki

doi:10.1271/bbb1961.52.1813

Cited by 31 publications

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“…Recently, the P. chlororaphis B23 nitrile hydratase has been used as a catalyst for industrial production of acrylamide from acrylonitrile, an important chemical commodity Ryuno et al 1988;; Nagasawa and Y a m a d a 1989). We have purified and crystallized the nitdle hydratases from P. ehlororaphis B23 and Brevibacterium R312 ).…”

Section: R C N + H 2 0 ~ R C O N Hmentioning

confidence: 99%

Optimum culture conditions for the production of cobalt-containing nitrile hydratase by Rhodococcus rhodochrous J1

Nagasawa

Takeuchi

Nardi‐Dei

et al. 1991

Appl Microbiol Biotechnol

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We sought the optimum conditions for production of nitrile hydratase by Rhodococcus rhodochrous J1. The addition of both cobalt ions and an aliphatic nitrile or amide as an inducer was indispensable for the appearance of nitrile hydratase activity in R. rhodochrous J1 cells. Crotonamide was an efficient inducer and, moreover, urea was found to be the most powerful inducer for the production of nitrile hydratase. When R. rhodochrous J1 was cultivated under optimal conditions, the enzyme activity in the culture broth and the specific activity was approximately 32,000 and 512 times higher than the initially obtained levels, respectively. The nitrile hydratase formed corresponded to more than 45% of the total soluble protein in urea-induced cells, as judged by quantitative evaluation of the gel track.

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Section: R C N + H 2 0 ~ R C O N Hmentioning

confidence: 99%

Optimum culture conditions for the production of cobalt-containing nitrile hydratase by Rhodococcus rhodochrous J1

Nagasawa

Takeuchi

Nardi‐Dei

et al. 1991

Appl Microbiol Biotechnol

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“…Both nitrile-converting enzymes have attracted increasing attention as catalysts for processing organic chemicals, since they can convert nitriles to the corresponding higher-value acids or amides. Recently, the use of Pseudomonas chlororaphis B23 nitrile hydratase, which was found in our laboratory, for the industrial production (6,000 ton per year) of the important chemical commmodity acrylamide was pioneered in Japan (3,36). We have purified and characterized the nitrile hydratases of P. chlororaphis B23 (30), Brevibacterium sp.…”

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confidence: 97%

Purification and characterization of a novel nitrilase of Rhodococcus rhodochrous K22 that acts on aliphatic nitriles

et al. 1990

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A novel nitrilase that preferentially catalyzes the hydrolysis of aliphatic nitriles to the corresponding carboxylic acids and ammonia was found in the cells of a facultative crotononitrile-utilizing actinomycete isolated from soil. The strain was taxonomically studied and identified as Rhodococcus rhodochrous. The nitrilase was purified, with 9.08% overall recovery, through five steps from a cell extract of the stain. After the last step, the purified enzyme appeared to be homogeneous, as judged by polyacrylamide gel electrophoresis, analytical centrifugation, and double immunodiffusion in agarose. The relative molecular weight values for the native enzyme, estimated from the ultracentrifugal equilibrium and by high-performance liquid chromatography, were approximately 604,000 + 30,000 and 650,000, respectively, and the enzyme consisted of 15 to 16 subunits identical in molecular weight (41,000). The enzyme acted on aliphatic olefinic nitriles such as crotononitrile and acrylonitrile as the most suitable substrates. The apparent Km values for crotononitrile and acrylonitrile were 18.9 and 1.14 mM, respectively. The nitrilase also catalyzed the direct hydrolysis of saturated aliphatic nitriles, such as valeronitrile, 4-chlorobutyronitrile, and glutaronitrile, to the corresponding acids without the formation of amide intermediates. Hence, the R. rhodochrous K22 nitrilase is a new type distinct from all other nitrilases that act on aromatic and related nitriles.

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“…Numerous microorganisms that utilize aliphatic nitriles have been reported (2,3,5,6,21,23). These organisms, which contain a nitrile hydratase and an amidase to metabolize nitriles, rarely degrade aromatic nitriles or their amides.…”

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Metabolism of benzonitrile and butyronitrile by Klebsiella pneumoniae

Nawaz

Heinze

Cerniglia

1992

Appl Environ Microbiol

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A strain of Klebsiella pneumoniae that used aliphatic nitriles as the sole source of nitrogen was adapted to benzonitrile as the sole source of carbon and nitrogen. Gas chromatographic and mass spectral analyses of culture filtrates indicated that K. pneumoniae metabolized 8.4 mM benzonitrile to 4.0 mM benzoic acid and 2.7 mM ammonia. In addition, butyronitrile was metabolized to butyramide and ammonia. The isolate also degraded mixtures of benzonitrile and aliphatic nitriles. Cell extracts contained nitrile hydratase and amidase activities. The enzyme activities were higher with butyronitrile and butyramide than with benzonitrile and benzamide, and amidase activities were twofold higher than nitrile hydratase activities. K. pneumoniae appears promising for the bioremediation of sites contaminated with aliphatic and aromatic nitriles.

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Isolation of advantageous mutants of Pseudomonas chlororaphis B23 for the enzymatic production of acrylamide.

Cited by 31 publications

References 0 publications

Optimum culture conditions for the production of cobalt-containing nitrile hydratase by Rhodococcus rhodochrous J1

Optimum culture conditions for the production of cobalt-containing nitrile hydratase by Rhodococcus rhodochrous J1

Purification and characterization of a novel nitrilase of Rhodococcus rhodochrous K22 that acts on aliphatic nitriles

Metabolism of benzonitrile and butyronitrile by Klebsiella pneumoniae

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