Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing oxygen-containing organic compound
Patent
1998-02-24
1999-12-07
Weber, Jon P.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Preparing oxygen-containing organic compound
435227, 4352522, C12P 760, C12N 978, C12N 120
Patent
active
059981806
DESCRIPTION:
BRIEF SUMMARY
This invention relates to enzymatic processes for the production of ammonium acrylate and to novel micro-organisms and enzymes useful in these processes.
Acrylic acid (or its salts) is generally made by a single stage chemical conversion from propylene oxide or a two-stage conversion from acrylonitrile, through acrylamide sulphate intermediate. This chemical conversion can give a product containing undesirable impurities from side reactions including the formation of some dimeric acrylic acid, which tends to form when the product acrylic acid is present in high concentration under the conditions of manufacture.
The use of an amidase for converting acrylamide to acrylic acid (as the ammonium salt) has frequently been described in the literature. It has been described primarily for converting residual monomer impurity in an acrylamide polymer to ammonium acrylate but it has also been proposed that it would be desirable to use an amidase for the commercial production of ammonium acrylate from acrylamide.
Processes of making acrylamide from acrylonitrile by a nitrile hydratase are known and are described in, for instance, EP-A-307,926 and Appl. Microbiol. Biotechnol. 1993, 40, pages 189 to 195. This latter article shows that a nitrile hydratase can be obtained from, inter alia, R rhodochrous J1. EP-A-188316 describes the conversion of acrylonitrile to acrylamide using a nitrile hydratase. One nitrile hydratase is obtained from Rhodococcus sp.S-6. WO95/04828 describes nitrile hydratases, one of which, from Comamonas NI1, is illustrated as converting acrylonitrile to acrylamide. Such processes, if applied to the production of ammonium acrylate, would involve two stages, namely the production of acrylamide as a first stage and the hydrolysis of this to acrylic acid as a second stage. Use of a two step process generally gives rise to the presence of two types of impurity. These are unreacted starting material from the first stage and unreacted product of the first stage, which is the starting material for the second stage.
A further conversion of nitrile to its corresponding acid is described in GB 1,475,540. This conversion is carried out on various nitriles which include acrylonitrile by particular strains of bacteria. These are of genera Bacillus, Bacteridium, Micrococcus or Brevibacterium. The exemplified conversions are on lactonitrile, glycinonitrile, amino propionitrile hydrochloride, amino-3-propionitrile and .alpha.-amino-.gamma.-methyl thiobutyronitrile. We believe that the microorganisms carried out the hydrolysis by producing a nitrile hydratase enzyme which converts the nitrile to an amide and an amidase enzyme which subsequently converts the amide to an acid.
It would be desirable to be able to produce ammonium acrylate by an enzymatic, commercially convenient, process in a single stage from acrylonitrile, using an acrylonitrilase.
Processes of converting acrylonitrile to ammonium acrylate using a nitrilase have been described in the literature, for instance EP-A-187,680, JP-B-63-2596 and Appl Microbiol. Biotechnol. 1990, 34, pages 322 to 324, which uses a nitrilase derived from R rhodochrous J1 (the same micro-organisms discussed in EP-A-307,926 above), and in EP-A-444,640 which also describes a nitrilase from R rhodochrous J1 as being preferred.
The use of R rhodochrous K22 is described in J. Bacteriol. 172, 9, pages 4807 to 4815 for the process of converting acrylonitrile to ammonium acrylate.
Nitrilase from Fusarium oxysporum f.sp. melonis is demonstrated acting on up to 60 mM acrylonitrile to produce acrylic acid in Biotech. Appl. Biochem., 1989, 11, pages 581 to 601.
Stevenson et al in Biotech. and Appl. Biochem. 15, 283-302 (1992) describe studies on a nitrilase produced by Rhodococcus ATCC 39484. The enzyme is most effective for hydrolysis of aromatic nitrites and shows little or no activity for many aliphatic nitriles such as acrylonitrile. The enzyme is said to have a pH optimum of 7.5, to be totally inactivated outside the pH range 5.0 to 9.0 and irreversibly inactivated by preincubation a
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Armitage Yvonne Christine
Hughes Jonathan
Webster Neil Andrew
Ciba Specialty Chemicals Water Treatments Limited
Crichton David R.
Weber Jon P.
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