Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Patent
1994-11-02
1996-10-29
Naff, David M.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
435 681, 4352521, 435267, 435822, C12N 952, C12N 112, C12P 2106, C07G 1700
Patent
active
055695990
DESCRIPTION:
BRIEF SUMMARY
The invention is relative to a novel microorganism with proteolytic properties, an enzyme composition obtainable from the microorganism, the use of the microorganism as well as methods of hydrolysis especially of keratin.
DESCRIPTION OF THE STATE OF THE ART
It is known that special enzymes, the proteases, hydrolyse proteins, giving rise to oligopeptides and, finally, amino acids. These enzymes are also formed from microorganisms such as e.g. from bacteria of the genus Pseudomonas, Bacillus or Proteus. A few enzymes, the so-called thermophilic enzymes, exhibit the above-named activity even at temperatures .gtoreq. 70.degree. C., thus making possible hydrolyses which are of interest, especially to industry. E.g. thermophilic microorganisms are a source for such thermophilic enzymes. A survey of this is offered by BFE 9, No. 7/8, pp. 466-470 (1992) in the article "Thermophilic Enzymes as Industrial Catalysts?" by K. Peek et al. A further enzyme which still exhibits a certain activity above 70.degree. C. is known from Biosci. Biotech. Biochem., 56 (10), pp. 1667-9 (1992). This enzyme also exhibits, in addition to usual proteolytic properties, a certain keratinase activity. Thus, hairs were attacked with this enzyme at a temperature up to 90.degree. C.; however, this was at a pH of 11.0 and over a period of 1 h, although the enzyme had already lost one half of its activity after 10 min already under the conditions indicated (see Appl. Microbiol. Biotechnol. (1989) 30, pp. 120-124). Since the decomposition of human hair presented in Biosci. in FIG. 2b exhibits even at temperatures above 80.degree. C. an even higher decomposition, this decomposition must be of a chemical nature and not of an enzymatic nature on account of the enzyme deactivation. Due to the stability of this described enzyme which drops sharply at 70.degree. C. it is not suitable for degrading keratin as it occurs e.g. in feathers, horn or hairs on an industrial scale, that is, within a few hours to a few days since only those amounts of keratin can be added for a completely enzymatic degradation which are degraded in less than 3 h, especially clearly more rapidly than in 1 h.
DESCRIPTION OF THE INVENTION
The present invention involves the isolation of a microorganism which has proteolytic properties and can also degrade keratin in natural products in a relatively short time. Other embodiments of the present invention are are therefore a keratin-degrading enzyme composition obtainable from this microorganism and a method of degrading especially keratin.
The microorganism, strain W, was deposited with the German Collection for Microorganisms and Cell Cultures Ltd., Mascheroder Weg 1b, D-3300 Braunschweig on Mar. 12, 1992 and received the receipt number DSM 7003. Due to its properties, the microorganism received the designation Fervidobacterium pennavorans.
The microorganism is viable and deposited and available in accordance with the Budapest Convention on the International Recognition of the Deposition of Microorganisms for the Purpose of Patent Granting Procedures.
The microorganism as well as the proteases formed from this microorganism exhibit a sufficiently high activity, so that even an enzyme composition obtainable from the microorganism exhibits a good in-vitro activity vis-a-vis proteins, especially vis-a-vis keratin and keratin-containing substances. Thus, this enzyme composition can also be used isolated from the microorganism.
F. pennavorans is the first known thermophilic microorganism which utilizes feathers (e.g. chicken feathers) as substrate very well.
Not only insoluble structural proteins but also soluble proteins can be treated with the novel microorganism and also with the enzyme composition. The degradation can be complete; however, as a rule short peptide sequences which can also be further utilized industrially, if desired, are also produced in addition to individual amino acids. The biological degradation has the particular advantage over traditional methods that a chemical and/or mechanical treatment of the proteins
REFERENCES:
Takami et al., Appl. Microbiol. Biotechnol., 30: 120-124, 1989.
Takami et al., Biosci. Biotech. Biochem., 56(10), 1667-1669, 1992.
Degussa - Aktiengesellschaft
Naff David M.
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