Processes for the production of amidase

Details Processes for the production of amidase Processes for the production of amidase

1998-07-24

2000-11-14

Lilling, Herbert J.

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Preparing nitrogen-containing organic compound

435 711, 435134, 435135, 435136, 435146, 435227, 4352521, C12P 1300, C12P 762, C12N 978

Patent

active

061468614

DESCRIPTION:

BRIEF SUMMARY
This invention relates to the production of enzymes by fermentation processes and the use of the enzymes as catalysts. It also relates to novel microorganisms particularly suitable for the production of certain improved enzymes.
It is known to convert amide molecules to their corresponding acid or acid salt. This is desired in particular in the case of acrylamide.
Conversion of (meth) acrylamide to its acid or salt is required on an industrial scale for production of (meth) acrylic acid monomer or a salt thereof.
Conversion of (meth) acrylamide to (meth) acrylic acid monomer is also desired for the purification of (meth) acrylamide homopolymer or copolymer of (meth) acrylamide with other monomers. Hydrolysis of residual (meth) acrylamide monomer is desirable as a way of meeting environmental concerns about the monomer.
It is known to use enzyme catalysts to hydrolyse residual monomeric (meth) acrylamide for the purification of (meth) acrylamide-containing polymers. Processes of this type are described in EP-A-0329324, EP-A-0329325 and WO92/05205.
It has also been suggested by Hawaz et al, in Applied and Environmental Microbiology, September 1994, p.3343-3348, that it would be desirable to use enzyme catalysts for the large scale production of acrylic acid if appropriate enzymes were available. In this paper Nawaz et al describe a Rhodococcus species which can use acrylamide as a growth substrate and produce an amidase enzyme. The bacterial cells were grown in batch culture.
It is generally found that when enzyme catalysts are used in the hydrolysis of monomeric (meth) acrylamide that the presence of the (meth) acrylamide monomer has a detrimental effect on the long term stability of the enzyme. There is a tendency for the enzyme catalyst to lose activity over time. This necessitates addition of further enzyme catalyst to return the catalytic activity to its original level. The lower the stability of the enzyme catalyst the less economical the process.
It is also known to convert nitrile molecules to their corresponding acid or acid salt. This can be carried out by the direct conversion of nitrile to acid using a nitrilase enzyme as catalyst. As used herein, a "nitrilase" is an enzyme which carries out the direct conversion of a nitrile to its corresponding acid without release of an amide intermediate. Nitrilases have been described in, inter alia, EP-A-444,640, JP-B-632596, Biotechnol. Appl. Biochem. 15, 283-302 (1992), Appl. Microbiol. Biotechnol. (1990) 34:322-324, Biotechnol. Appl. Biochem. 11, 581-601 (1989) and J. Bacteriol., September 1990, pages 4807 to 4815.
As with amidases, these enzymes often show a tendency to destabilise in the presence of large amounts of substrate (nitrile). As with amidases, instability results in a less economic process.
The normal way of cultivating microorganisms which produce an amidase or nitrilase is batch culturing. In this method an initial amount of the microorganism is placed in a growth medium containing a large excess of all nutrients necessary for growth of the microorganism. Growth proceeds either until it is terminated by harvesting the batch of cultured microorganism or until termination of growth due to exhaustion of nutrients or toxification of the growth medium due to build-up of by-products from the microorganism.
An alternative culture method is known as continuous culture. Continuous culture methods are generally known. In the most commonly used methods the culture, containing microorganism and growth medium and usually in liquid form, is continuously removed from the culture vessel and is replaced at the same rate with fresh growth medium so that the volume of liquid culture remains constant. Under steady state conditions the replication rate of the microorganism is governed by addition of new growth medium such that the biomass concentration of the culture is constant.
In continuous culture methods it is usual to provide one element which is metabolised to depletion in the culture medium and governs the steady state biomass concentration. This is kn

REFERENCES:
Bioscience, Biotechnology, and Biochemistry, vol. 57, No. 11, Nov. 1993, pp. 1949-1950, M. Kobayashi et al: "Occurrence of Amidases in the Industrial Microbe Rhodococcus rhodochrous J1".
Applied and Environmental Microbiology, Sep. 1994, pp. 3343-3348, M. Nawaz et al: "Purification and Characterization of an Amidase from an Acrylamide-Degrading Rhodococcus sp.".
Journal of Bacteriology, Sep. 1990, pp. 4807-4815, M. Kobayashi et al: "Purification and Characterization of a Novel Nitrilase of Rhodococcus rhodochrous K22 That acts on aliphatic Nitriles".
Biotechnology and Applied Biochemistry 11, 581-601 (1989), A. Goldlust et al: "Induction, Purification, and Characterization of the Nitrilase of Fusarium oxysporum f. sp. melonis".
Biotechnology and Applied Biochemistry 15, 283-302 (1992), D. Stevenson et al: "Mechanistic and Structural Studies on Rhodococcus ATCC 39484 Nitrilase".
Applied Microbiology Biotechnology (1990) vol. 34, pp. 322-324, T. Nagasawa et al: "Production of acrylic acid and methacrylic acid using Rhodococcus rhodochrous J1 nitrilase".

Affiliated with

Also associated with

Rating

Processes for the production of amidase does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Processes for the production of amidase, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Processes for the production of amidase will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-2063865