Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Patent
1997-07-15
1998-12-08
Weber, Jon P.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
4352533, C12N 920, C12N 120
Patent
active
058468013
DESCRIPTION:
BRIEF SUMMARY
CROSS-REFERENCE TO RELATED APPLICATIONS
This application is a 35 U.S.C. 371 national application of PCT/JP96/00454 filed Feb. 27, 1996 and claims priority under 35 U.S.C. 119 of Japanese application 7-45803 filed Mar. 6, 1995, the contents of which are fully incorporated herein by reference.
TECHNICAL FIELD
This invention relates to a novel lipase, a production method thereof and a microorganism producing the same, and more specifically, to a novel thermostable lipase showing high activity at high temperature which is produced by a bacterium belonging to Pseudomonas solanacearum, a microorganism producing the lipase and production method thereof.
BACKGROUND ART
A lipase is a general term of an enzyme which hydrolyze triglyceride, and has formerly been produced by extraction of internal organs of animals or by using microorganisms.
The lipase is extensively used as an enzyme for food processing to flavor dairy products, medicines as digestives, diagnosis of a blood lipid assay, industry in hydrolysis and improvement of fats and oils, and the like. The lipase is required to have various characteristics for each use, and a thermostable lipase is applied to a wide variety of fields and requested to be variously used.
In food processing, from a food-hygienic point of view, enzyme reaction at high temperature which is in low danger of bacterial contamination has been desired. In decomposition of fats and oils, application of the lipase has been considered. Hydrolysis of fats and oils is a process for producing fatty acid and glycerol which are materials of petrochemical products such as detergents, cosmetics and surface-active agents. At present the Colgate-emery method is mainly carried out which brings fats and oils into contact with steam at 250.degree. to 260.degree. C. and at 50 to 55 atmospheres, however, the method needs heavy facilities and is not appropriate for small-to-medium-scale production of soap, etc. Therefore, decomposition of fats and oils by a lipase has been investigated.
However, stearic acid (melting point: 67.degree. to 70.degree. C.) and palmitic acid (melting point: 63.degree. to 640.degree. C.) which constitute a variety of fats and oils are solid at ordinary temperature. For that reason, the reaction fats and oils must be reacted at the temperature above their melting points. Therefore, the lipase used for decomposition of fats and oils must have a high thermostability and a high reactivity at a high temperature.
Furthermore, in recent years, the lipase has been used for a solution of pitch troubles in paper-manufacturing industry (Japanese Examined Patent Publication No.
Hei. 4-29794). The optimum temperature of the enzyme reaction conventionally adopted for a solution of pitch troubles is from 35.degree. to 55.degree. C. Since the conventional enzyme is inactivated above 70.degree. C., the temperature of the enzyme reaction in the paper-manufacturing process is limited and the temperature must be controlled throughout the paper-manufacturing process in which the lipase is used. Also, the enzyme is not thermostable, which is one of the causes to inhibit the use of the enzyme for a solution of pitch troubles at the grinder treatment part.
At present, most of the well-known enzymes on the market used as a thermostable lipase are not adequate for the stability against heat and not practical. For that reason, a Japanese Unexamined Patent Publication No. Sho. 62-79782 proposed a thermostable lipase. However, the optimum temperature of the enzyme is from 60.degree. to 70.degree. C., and its thermostability is not sufficient, since the residual activity after treatment at 70.degree. C. for 15 minutes is below 10%. Moreover, because the enzyme hardly acts on triacetin and tributyrin, its use is restricted to food-processing. A thermostable lipase derived from Rhizopus has been disclosed (Japanese Unexamined Patent Publication Number Sho. 59-156282), but the optimum temperature of the enzyme is 60.degree. C. and the reactivity at a high temperature is not sufficient. Furthermore there
REFERENCES:
patent: 5454971 (1995-10-01), Sakai et al.
patent: 5480787 (1996-01-01), Negishi et al.
Sugihara et al., J. Biochem, vol. 112, pp. 598-603 (1992).
Kotsuka Takashi
Sakimoto Kazunori
Tanaka Keijitsu
Hanley Susan
Lambiris Elias J.
Novo Nordisk A S
Weber Jon P.
Zelson Steve T.
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