Lipases from hyphozyma

Details Lipases from hyphozyma Lipases from hyphozyma

1994-12-22

1999-01-05

Patterson, Jr., Charles L.

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Hydrolase

435278, C12N 920, D21C 300

Patent

active

058561633

DESCRIPTION:

BRIEF SUMMARY
CROSS-REFERENCE TO RELATED APPLICATIONS

This application is a 371 of PCT/DK93/00194 filed Jun. 3, 1993, which is incorporated herein by reference.


TECHNICAL FIELD

The present invention relates to novel microorganisms and to novel enzymes obtainable therefrom. More specifically, the invention relates to a new species of the genus Hyphozyma, and to novel lipases obtainable therefrom,
The invention also relates to a process for obtaining the enzymes, immobilized lipase preparations, and industrial applications of these enzymes in the paper pulp industry, for use in ester hydrolysis, ester synthesis or interesteri- fication, and for manufacmre of leather.


BACKGROUND ART

When resinous wood species are used in pulping processes, particularly mechanical pulping processes, pitch problems arise. This widespread phenomenon causes production intermptions and a decreased paper product quality.
Pitch contains considerable amounts of triglycerides, more commonly known as fats, and other esters. Faty acid glyceride hydrolysing enzymes, in the following called lipases, may advantageously be used for efficient hydrolysis of water-insoluble esters, particularly triglycerides.
In order to comply with the prerequisite for paper pulp processing, lipases applied in methods for enzymatic pitch control should be acidophilic and thermophilic.
Enzymes suggested in the prior art for pitch control include lipases derived from strains of Pseudomonas, Humicola, Candida, Chromobacter and Aspergillus.
Some of these lipases are markedly thermophilic, others are markedly acidophilic, but none of these lipases possess both characteristics.
Hyphozyma is a nlew genus of yeast-like Hyphomycetes (vide de Hoog, G. S. & Smith, M.Th.; Antonie van Leeuwenhoek 47 (1981) 339-352), and the following species are reported: H. vanabilis, M. variabilis var. odora, H. sanguinea, and H. roseoniger. However, no lipase production has previously been ascribed to these organsms.


SUMMARY OF THE INVENTION

We have now found that a new species of Hyphooma is able to produce lipase. Moreover, we have found that these novel lipases possess excellent paper pulp processing possibilities due to their markedly thermophilic and acidophilic characteristics. Moreover, we have also found that these novel lipases are well suited for use in ester hydrolysis, ester synthesis or iteresterification, and vafious other industrial applications.
Accordingly, in its first aspect, the present invention provides a biologically pure culture of a species belonging to the genus Hyphozyma, which has the ability to produce lipase. In a more specific embodiment of this aspect, the invention provides a biologically pure culture of a new species represented by the strain Hyphozyma sp. LF132, CBS 648.91.
In its most specific embodiment of this aspect, the invention provides a biologically pure culture of the strain Hyphogyma sp. LP132, CBS 648.91, or mutants or variants thereof.
In its second aspect, the present invention provides a lipolytic enzyme being immunologically reactive with an antibody raised against a purified lipase derived from the strain Hyphozyma sp. LF132, CBS 648.91.
In its third aspect, the present invention provides a lipolytic enzyme comprising one or more of the following partial no acid sequences: Phe TbrPro Phe Pro (SEQ ID NO:4); Thr Gly Ala Asp Pro (SEQ ID NO:5); Ala Phe Thr Gln Ser (SEQ ID NO:6); Gln Ala Thr Leu Asp Ala Gly Leu Thr (SEQ ID NO:7); Gly Ser Gly Ser Lys (SEQ ID NO:8); Val Pro Val Leu Thr Trp Ser (SEQ ID NO:9); Thr Trp Ser Gln Gly Gly Leu Ala Ala GOn (SEQ ID NO:10); Ala Gin Gin Lys Leu Asp Ser Ala Ala Ile Ile Leu (SEQ ID NO:11); Val Ala Gly Lys Asa lie Val Thr Gly Pro Lys Gln (SEQ ID NO: 12); Asn Cys Glu Pro Asp Leu Met Pro Tyr Ala Arg Lys Tyr (SEQ ID NO: 13); and Arg Ile Gly Lys Lys Thr Cys Ser Gly Val Ile Thr Gly (SEQ ID NO:14).
In a more specific embodiment of this aspect, the present invention provides a lipolytic enzyme comprising one or more of the following partial ano acid sequences: Phe Thr Pro Phe Pro Thr Gly Ala Asp Pro (SEQ ID NO:15); A

REFERENCES:
patent: 4818695 (1989-04-01), Elgtved
patent: 5173417 (1992-12-01), Takeda et al.
patent: 5191071 (1993-03-01), Kirk et al.
patent: 5273898 (1993-12-01), Ishii
Fischer and Messner, "Adsorption of lipase on pulp fibers during biological pitch control in paper industry", Enzyme MicrobTechnol (1992) 14:470-473.
Uppenberg et al, The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candid antarctical Structure (1994) 2:293-308.

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