A new method to prepare amides by bioconversion of corresponding nitriles

Bui, K.; Arnaud, A.; Galzy, P.

doi:10.1016/0141-0229(82)90117-x

Cited by 57 publications

(9 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In order to harness the maximum catalytic potential of the cells to convert acrylonitrile to acrylamide, immobilization becomes highly desirable. Very few studies have been carried out using microbial cells immobilized in alginate, polyacrylamide and diethylaminoethyl (DEAE) cellulose for conversion of acrylonitrile to acrylamide [4,7,8,12,14]. Agar has also been used for the immobilization of cells and enzymes [2].…”

Section: Introductionmentioning

confidence: 99%

Acrylamide synthesis using agar entrapped cells of Rhodococcus rhodochrous PA-34 in a partitioned fed batch reactor

Raj

Sharma

Prasad

et al. 2007

J Ind Microbiol Biotechnol

View full text Add to dashboard Cite

The nitrile hydratase (Nhase) induced cells of Rhodococcus rhodochrous PA-34 catalyzed the conversion of acrylonitrile to acrylamide. The cells of R. rhodochrous PA-34 immobilized in 2% (w/v) agar (1.76 mg dcw/ml agar matrix) exhibited maximum Nhase activity (8.25 U/mg dcw) for conversion of acrylonitrile to acrylamide at 10 degrees C in the reaction mixture containing 0.1 M potassium phosphate buffer (pH 7.5), 8% (w/v) acrylonitrile and immobilized cells equivalent to 1.12 mg dcw (dry cell weight) per ml. In a partitioned fed batch reaction at 10 degrees C, using 1.12 g dcw immobilized cells in a final volume of 1 l, a total of 372 g of acrylonitrile was completely hydrated to acrylamide (498 g) in 24 h. From the above reaction mixture 87% acrylamide (432 g) was recovered through crystallization at 4 degrees C. By recycling the immobilized biocatalyst (six times), a total of 2,115 g acrylamide was produced.

show abstract

Section: Introductionmentioning

confidence: 99%

Acrylamide synthesis using agar entrapped cells of Rhodococcus rhodochrous PA-34 in a partitioned fed batch reactor

Raj

Sharma

Prasad

et al. 2007

J Ind Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…Pseudomonas ehlororaphis B23 (Asano et al 1982) and Brevibaeterium R312 (Bui et al 1982) exhibit high catalytic activity for hydration of aliphatic nitriles to the corresponding amides (Eq. 1).…”

Section: Introductionmentioning

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

View full text Add to dashboard Cite

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.

show abstract

“…Considering the industrial potential for the use of the nitrile hydratase enzyme (Bui et al, 1982), we also studied the effect of the structure of the substrate nitriles on the activity of hydratation of nitriles by the wild-type Breuibacrerium R312. The K , and V,,, of the nitrile hydratase were determined for 12 different substrates.…”

Section: Introductionmentioning

confidence: 99%

A Nitrile Hydratase with a Wide Substrate Spectrum Produced by a Brevibacterium sp.

et al. 1984

Self Cite

View full text Add to dashboard Cite

A mutant strain, Brevibacterium 19, defective for the enzyme nitrile hydratase but retaining all the amidase activity of the wild-type Brevibacterium R3 12, was isolated. This is genetic evidence in favour of the hypothesis that all the nitrile-hydratase activity of the wild-type was due to a single enzyme, the structural gene of which was lost in the mutant strain 19.The specific activities and K , of the nitrile hydratase were determined for 12 different substrates. The affinity of the enzyme increased as the number of hydrogen-bonding positions of the substrate increased, and decreased with more spatial crowding of the hydrocarbon chain. The specific activity of the enzyme for a substrate was enhanced by the nucleophilic and hydrophilic properties of the hydrocarbon side chain of that substrate. INTRODUCTIONThe wild-type strain Brevibacterium R312 (Arnaud et al., 1976a, b) was able to hydrolyse all water-soluble nitriles via the activities of its nitrile hydratase (Arnaud et al., 1977) and its amidase (Jallageas et al., 1978~). A mutant strain, Brevibacterium A4, unable to hydrolyse acetamide, was described by Jallageas et al. (1979) and Arnaud et al. (1980). Unlike the wildtype R3 12 (Amaud et al., 1976c), this mutant could no longer hydrolyse many amides such as the aliphatic amides, a-aminopropionamide, lactamide, benzamide and the D-a-aminopropionamides. This strain retained, however, the ability to hydrolyse L-a-aminoamides (Kieny-L'Homme et al., 1981). The enzyme no longer synthesized by the mutant A4 strain had previously been described and named acetamidase (Jallageas et al., 1978a).In the present work, we report the isolation of a mutant strain, Brevibacterium 19, which had lost its ability to hydrate nitriles, including cyanide, while retaining its amidase activity. Considering the industrial potential for the use of the nitrile hydratase enzyme (Bui et al., 1982), we also studied the effect of the structure of the substrate nitriles on the activity of hydratation of nitriles by the wild-type Breuibacrerium R312. The K , and V,,, of the nitrile hydratase were determined for 12 different substrates. METHODSBacterial strain. The wild-type strain used was Brecibactetium R3 12 (Arnaud et a/., 1976a, b). Media. The composition of the basal minimal medium was as previously described (Kieny-L'Homme et a/., 1981). Ammonium sulphate (5 g I-') and glucose (10 g 1-I) were added to the minimal medium. Slant cultures were maintained on YMPG-agar, the composition of which was given by Jallageas et a/. (1978~).Growth. Cultures were grown at 28 "C in conical flasks filled to 10% (v/v) RESULTS A N D DISCUSSIONIsolation and study of a nitrile hydratase defective mutant The isolation of a nitrile hydratase defective mutant was based on the following principle : in the presence of the wild-type, a halogenated nitrile would be hydrated into a halogenated amide, which would then be hydrolysed into a halogenated acid. Such compounds are toxic to some micro-organisms (Apirion, 1965;Hynes & Pateman, 1970;Clarke & Tata,...

show abstract

A new method to prepare amides by bioconversion of corresponding nitriles

Cited by 57 publications

References 7 publications

Acrylamide synthesis using agar entrapped cells of Rhodococcus rhodochrous PA-34 in a partitioned fed batch reactor

Acrylamide synthesis using agar entrapped cells of Rhodococcus rhodochrous PA-34 in a partitioned fed batch reactor

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

A Nitrile Hydratase with a Wide Substrate Spectrum Produced by a Brevibacterium sp.

Contact Info

Product

Resources

About