Abstract: The invention relates to a biocatalytic method or process for the synthesis of esters of acrylic acid and/or methacrylic acid free of positively chargeable/charged groups, comprising reacting one or more alcohols (alcohol starting materials) which are free of positively chargeable or charged groups with (meth)acrylyl-CoA, preferably in the presence of a catalyst (inorganic, organic or organometallic, or preferably a biocatalyst) capable of effecting the transfer of an alcohol radical from an alcohol starting material as defined above or below to (meth)acrylyl CoA under removal of the CoA moiety transferase activity, such as an enzyme of the transferase or hydrolase class of enzymes. The (meth)acrylyl-CoA is preferably formed by reaction of (meth)acrylic acid or its salts with coenzyme A in the presence of an energy providing substance and a biocatalyst e.g.

Abstract: The invention relates to a biocatalytic method or process for the synthesis of esters of acrylic acid and/or methacrylic acid free of positively chargeable/charged groups, comprising reacting one or more alcohols (alcohol starting materials) which are free of positively chargeable or charged groups with (meth)acrylyl-CoA, preferably in the presence of a catalyst (inorganic, organic or organometallic, or preferably a biocatalyst) capable of effecting the transfer of an alcohol radical from an alcohol starting material as defined above or below to (meth)acrylyl CoA under removal of the CoA moiety transferase activity, such as an enzyme of the transferase or hydrolase class of enzymes. The (meth)acrylyl-CoA is preferably formed by reaction of (meth)acrylic acid or its salts with coenzyme A in the presence of an energy providing substance and a biocatalyst e.g.

Abstract: An amidase or nitrilase is made by continuous culture under carbon limitation using a carbon source which includes, respectively, either (a) an amide or amide precursor or (b) a nitrile or nitrile precursor. Novel enzymes have particular stability. A novel microorganism is Rhodococcus rhodochrous NCIMB 40756 and is capable of producing a particularly stable amidase. The novel amidase, and the amidase made by the defined process, are effective for converting (meth)acrylamide to ammonium (meth)acrylate, for instance in or after the polymerisation of the acrylamide.

Abstract: Nitrilase enzymes are provided which have Km at pH 7.0 for acrylonitrile of 500 .mu.M or below. The enzymes also have Ki at pH 7.0 for ammonium acrylate of at least 100 mM. In particular, the nitrilases have a value of the ratio of the said Ki to the said Km of at least 200. Particularly preferred nitrilases are obtainable from the microorganisms Rhodococcus rhodochrous NCIMB 40757 or NCIMB 40833. These nitrilases can be used in processes of converting acrylonitrile to ammonium acrylate in aqueous or vapor form and for detecting low levels of nitrile in aqueous or vapor form.

Abstract: Acrylamidase enzymes are provided which have acrylamidase activity at pH 4.0 which is at least 50% of their acrylamidase activity at pH 7.0. Such enzymes can be produced by the novel microorganisms Rhodococcus strains NCIMB 40889 and NCIMB 40755. Such enzymes and microorganisms can be used for reducing free acrylamide in polyacrylamides which are produced at low pH and in particular cationic and substantially non-ionic polyacrylamides.