A strain of Rhodococcus rhodochrous in which a gene coding at least part of a nitrile hydratase enzyme or any gene coding a protein involved in the transcription, translation or formation of at least part of the nitrile hydratase enzyme has been deactivated or rendered ineffective or a strain of Rhodococcus rhodochrous cultured under condition wherein the nitrile hydratase enzyme is been inhibited.

The present invention relates to regioselective chemical and electrochemical processes for the preparation of an oxidized heterocyclic alpha-amino amide compounds. By applying specific catalysts or catalyst systems during chemical oxidation or by applying particular electrochemical oxidation conditions the present invention provides access to valuable alpha amino amide compounds, which are oxidized at the heterocyclic amino group by regioselective introduction of either a hydroxyl or a keto group. In a more particular embodiment, the present invention describes a chemical oxidation reaction, which advantageously is applicable in the enantioselective synthesis of valuable oxidized heterocyclic alpha-amino amide compounds, like levetiracetam, brivaracetam or the synthesis of piracetam. Another aspect of the present invention relates to a process for the electrochemical recycling of alkali perhalogenate oxidants as spent during said regioselective oxidation reactions of the invention. Still another aspect of the invention relates to the electrochemical preparation of perhalogenates.

Process for producing aqueous polyacrylamide concentrates by polymerizing an aqueous solution comprising at least acrylamide thereby obtaining an aqueous polyacrylamide gel, comminuting said aqueous polyacrylamide gel and mixing it with an aqueous liquid, wherein the manufacturing steps are allocated to two different locations A and B and the process comprises the step of transporting an aqueous polyacrylamide concentrate hold in a suitable transport unit from a location A to a location B. Modular, relocatable plant for manufacturing aqueous polyacrylamide, wherein the units of the plant are located at two different locations A and B.

The present invention relates to a novel biocatalytic process for the stereoselective preparation of alpha amino amide compounds catalyzed by NHase enzymes. A further aspect of the invention relates to novel NHase enzymes as well as further improved NHase enzyme mutants, nucleic acid molecules encoding these enzymes, recombinant microorganisms suitable for preparing such enzymes and mutants. Another aspect of the invention relates to a chemo-biocatalytic process for the preparation of lactam compounds comprising the new catalytic process for the preparation of alpha amino amide compounds catalyzed by NHase enzymes, as well as the chemical oxidation of the alpha amino amide by applying certain chemical oxidation catalysts suitable for converting the alpha amino amide under retention of its stereochemical configuration to the respective lactam. The novel chemo-biocatalytic process is particularly suited for the synthesis of valuable pharmaceutical compounds, like in particular (S)-Levetiracetam.

A microbiological process for the preparation of amides from the corresponding nitriles by enzymatic hydrolysis with nitrile hydratase enzyme from a bacterial strain of Rhodococcus biphenylivorans species is described.

The present invention relates to methods for preparing an aqueous acrylamide solution having a low acrylic acid concentration. In addition, the present invention relates to methods for reducing the acrylic acid concentration of an aqueous acrylamide solution. The methods involve a bioconversion of acrylonitrile to acrylamide in the presence of a biocatalyst, wherein during the bioconversion the content of acrylonitrile is maintained at 0.3 w/w % or more referred to the total weight of the composition in the reactor. Also provided is an aqueous acrylamide solution which is obtained by the methods of the present invention. Furthermore, the present invention is related to an acrylamide homopolymer or copolymer obtained by polymerizing the acrylamide of the aqueous solution.

Provided is a novel improved nitrile hydratase with improved resistance to amide compounds under high temperatures. Specifically provided is a nitrile hydratase having at least one amino acid mutation selected from (a) to (d) below, in the amino acid sequence expressed in SEQ ID NO:50 (X.sub.1 to X.sub.27 represent independent arbitrarily-defined amino acid residuals). (a) X.sub.1 is valine or glycine (b) X.sub.9 is valine or threonine (c) X.sub.23 is an amino acid selected from a group consisting of isoleucine, leucine, methionine and threonine, (d) X.sub.24 is leucine.

Provided is an improved nitrile hydratase with improved catalytic activity. Also provided are DNA for coding the improved nitrile hydratase, a recombinant vector that contains the DNA, a transformant that contains the recombinant vector, nitrile hydratase acquired from a culture of the transformant, and a method for producing the nitrile hydratase. Also provided is a method for producing an amide compound that uses the culture or a processed product of the culture. The improved nitrile hydratase contains an amino acid sequence represented by SEQ ID NO: 50 (GX.sub.1X.sub.2X.sub.3X.sub.4DX.sub.5X.sub.6R) in a beta subunit, and is characterized in that X.sub.4 is an amino acid selected from a group comprising cysteine, aspartic acid, glutamic acid, histidine, isoleucine, lysine, methionine, asparagine, proline, glutamine, serine and threonine.

The present invention relates to methods for cultivating a nitrile hydratase producing microorganism, compositions for cultivating a nitrile hydratase producing microorganism, and use of compositions comprising a saccharide and an organic acid for cultivating a nitrile hydratase producing microorganism. The composition provided in and to be employed in context with the present invention is particularly suitable for inducing both, growth and nitrile hydratase production of corresponding microorganisms.

The disclosure discloses a mutant of nitrile hydratase derived from Caldalkalibacillus thermarum, and belongs to the technical field of enzyme engineering. The nitrile hydratase mutant Cal. t Nhase-A20V provided by the disclosure has a half-life of about 10 min at 70° C., which does not change much compared with the thermal stability of the wild enzyme. The specific enzyme activity of the mutant Cal. t Nhase-A20V is 128% of that of the wild enzyme. At the same time, the mutant also has better tolerance to a substrate and a product, and the final yield of nicotinamide produced by whole-cell catalysis reaches 598 g/L. Therefore, the nitrile hydratase mutant Cal. t Nhase-A20V provided by the disclosure has good enzymatic properties and is beneficial to future industrial production.