WO1995014783A1 - Lipase gene and variant lipase - Google Patents

Lipase gene and variant lipase Download PDF

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Publication number
WO1995014783A1
WO1995014783A1 PCT/JP1994/001965 JP9401965W WO9514783A1 WO 1995014783 A1 WO1995014783 A1 WO 1995014783A1 JP 9401965 W JP9401965 W JP 9401965W WO 9514783 A1 WO9514783 A1 WO 9514783A1
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eu
lipase
er
amino acid
gene
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PCT/JP1994/001965
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French (fr)
Japanese (ja)
Inventor
Tadashi Yoneda
Yoshiaki Miyota
Kei Ohno
Junji Sasuga
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Showa Denko K.K.
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Priority to JP5293631A priority Critical patent/JPH07143883A/en
Priority to JP5/293631 priority
Application filed by Showa Denko K.K. filed Critical Showa Denko K.K.
Publication of WO1995014783A1 publication Critical patent/WO1995014783A1/en

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    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/16Hydrolases (3) acting on ester bonds (3.1)
    • C12N9/18Carboxylic ester hydrolases (3.1.1)
    • C12N9/20Triglyceride splitting, e.g. by means of lipase

Abstract

A lipase gene isolated from a chromosome DNA of Pseudomonas mendocian SD702; a variant lipase gene obtained by the variation of the above gene; and a variant lipase coded for by the above variant gene and having physical or chemical properties changed thereby. The invention gene serves to facilitate production and modification of lipase LP or a variant lipase thereof. The modification of lipase LP permits production of a variant lipase that has a new amino acid sequence and is more suitable to industrial and other application than the lipase LP, thus providing a lipase useful in the fields of detergent, food processing, papermaking and so forth.

Description

Item: lipase gene and mutant Lipa - Ze

Technical field

The present invention, detergents, food processing, gene and its nucleotide sequence encoding a useful novel lipase in the field of the papermaking industry, etc., by mutation and variants of a gene to further alter the physical properties or chemical properties of the lipase code for the mutant lipase. BACKGROUND

Lipase is a lipolytic enzyme, food processing enzymes for flavor formation of dairy products, medical enzymes as digestive aid, cross enzymes, fat hydrolysis Ya reforming diagnosis for the measurement of blood lipid , it has been extensively used particularly as industrial enzymes, etc. for decomposing and removing lipids of soiled as a component of a detergent composition o

The microorganisms produce lipases, the shoes Pseudomonas (eudomonas) genus ヽ Alcaligenes (Alcal igenes) genus ヽ Mucor (Mucor) genus, the can Deida (Candida) spp, including full Mikora (Humicola) genus are known. Although some of these are some things that the lipase gene has been acquired, it is among them Gerhard one Pseudomonas (Pseudomonas) obtaining a number of lipase genes of a microorganism belonging to the genus. The ones known so far, Gerhard one Pseudomonas fragi (Pseudomona fragi) (JP 62- 228279, JP-A-2 39890), the shoes Pseudomonas' Sepashia (Pseudomonas cepacia) (JP-A-3- 87187, Hei 3 - 47079), Zhu one Pseudomonas putida (Pseudomonas putida) ヽ shoe Pseudomonas, the shoes Doaruka Rigenesu (Pseudomonas pseudoalcal igenes) (JP-A-3 - 500 845), the shoes Domo eggplant * Aezoreginosa (Pseudomonas aeruginosa (J. Gen. Microbio l. (1992) 138, 1325-1335), Gerhard one Pseudomonas sp. (Pseudomonas sp.) 1 0 9 (J. Biol. Chem. (1991) 266, 18135-18140), the shoes Pseudomonas * click ,, Zoremae ( Pseudomonas gluiae) (Appl. Envir. Microbiol. (1992) 58, 12, 3787-3791) there is.

Lipase that the shoes Pseudomonas (Pseudomonas) bacteria secrete production, detergents, food processing, are used in industrial fields, such as for the paper industry. Lipases utilized in these fields of the temperature, PH, is required to be stable to conditions of use of the oxygen, the solvent, such as pressure. In particular, the lipases as the enhance the cleaning effect agent aids be incorporated into the detergent, p H at al force Li range, temperature, oxygen, have a high relative additives in detergents, including oxidizing agent stability is required. As a method for obtaining such chemically stable properties, it is known to alter the Amino acid sequence of the enzyme. Examples include and the like improvements to Protea Ichize and oxidant in JP-A 4-500608. The Applicant has excellent properties for use in industrial fields such as detergent, found a novel lipase (hereinafter abbreviated as lipase LP.) Having the Amino acid sequence depicted in SEQ ID NO: 1, patents previously is performed application (JP-a-6-38746). The purpose of the invention

An object of the present invention, the lipase LP co one gene encoding and quinuclidine Reochi de sequence, and physical properties of the lipase LP was also properly is varied more suitable for applications such as for E industry chemistries mutant lipase Ichize, and to provide a gene changing the nucleotide sequence so that said mutant lipase co Solo mode. Disclosure of the Invention

The present inventors have, in order to achieve the above purpose, first, the lipase LP is one of the production to Shiyu over Pseudomonas bacteria belonging to the genus, by the applicant of Japan International Trade and Industry Ministry of Agency of Industrial Science Technology Research Tokoro (National Inst itute of Bioscience and Human-Technology, Agency of Industrial Science and Techno l ogy) get the lipase gene derived from a shoe that has been deposited on one Pseudomonas and eye down Doshina (Pseudomonas mendocina) SD 7 0 2 shares did. It should be noted, Shiyu over Domu na scan and eye down de Shi Na (Ps eudomona s mendocina) SD 7 0 2 strain has been deposited with the depositary institution in 1 date May 1992 FERMP- 1 2 9 4 4 made accession number is been granted, "international approval Budape strike Convention on the certification of the deposit of microorganisms for the Purposes of Patent procedure" (BUDAPEST TREATY oN in the above-mentioned depositary institutions 1 2 dated May 1993 tHE INTERNATIONAL RECOGNITION oF tHE dEPOSIT oF mICROORGANISMS fOR tHE PURPOSE oF is converted to an international deposit under the PATENT PPROCEDURE), FERMBP- 4 2 9 1 comprising accession number is given.

Furthermore, the specific mutations of the SD 7 0 2 strains derived gene, nucleotide sequence as one or more variant lipase obtained by substituting Amino acids other Amino acid co Solo de of Amino acid sequence of a lipase LP is It was acquired the altered gene. The gene was introduced into a host bacterium, after culturing the resulting transformant to obtain the various lipase by conventional separation methods. Among these lipases, physical properties of the lipase LP also properly changes the chemistry, sure. More useful variant lipase one peptidase is obtained in the industrial field such as detergent Applications, this has led to the completion of the present invention.

That is, the present invention is,

1) gene containing part properly even all of the nucleotide sequences described lipase described in SEQ ID NO: 2 that co one de in SEQ ID NO: 1, 2) part of the nucleotide sequence of SEQ ID NO: 2 the 1 Symbol placement of genes including,

3) gene, the entire nucleotide sequence set forth in SEQ ID NO: 2 of the 1, wherein the including lipase gene gene,

4) mutants lipase Amino acid residues with one place less of amino acid sequences described are substituted by other Amino acid residues in SEQ ID NO: 1,

5) The next position in the amino acid sequence having at least 50% or more homology Amino acid sequence also properly from its Amino acid sequence set forth in SEQ ID NO: 1: 1 8, 2 1, 2 5, 3 1 , 43, 60, 75, 79, 93, 104, 1 0 7, 1 25, 1 42, 1 45, 1 48, 1 55, 1 5 6 1 5 9, 1 64, 1 8 3 1 9 8 , 2 0 3, 2 1 0, 2 1 6, 22 2, 2 2 3, 224, 242, 246, 24 7, 2 5 7, 2 6 6, 2 6 7 2 7 6, and of 2 92 mutant lipase Amino acid residues with one place less of a has been substituted with another Amino acid residues,

6) the following substitutions: G 1 y 1 8 A 1 a; M et 2 1 L eu; A sp 2 5 L eu; A sp 25 A rg; A sn 3 1 A sp; A sp 4 3 A sn; A 1 a 6 0 V a 1; I le 75 L eu; G ly 7 9 P ro; T hr 9 3 V a 1; V a 1 1 04 I le; V all 0 7 A la; G lyl 2 5 G ln ; I lel 42 L eu; G lyl 45 S er; T hrl 4 8 A la; G lyl 5 5 S er; S erl 5 6 G ly; T hrl 5 9 G ly; A lal 64 S er; P hel 8 3 T yr; S erl 9 8 L ys; A rg 2 0 3 S er; T hr 2 1 0 S er; V al 2 1 6 P he; L eu 222 A 1 a; L eu 22 3 P he; M et 2 2 4 L eu; A rg 2 42 T hr; A rg 246 H is; M et 24 7 L eu; M et 2 5 7 L eu; T hr 2 6 6 V a 1; L eu 2 6 7 P he; a sp 2 7 6 S er; and G iy 2 9 2 S variants Li eighth least the 5 further comprising one of the er 0 - Zeヽ

7) genes comprising all or part of the nucleotide sequence encoding the variant lipase one zero according to any one of 4 to 6,

8) The next position in the Amino acid sequence set forth in SEQ ID NO: 1: 1 8, 2 1, 2 5, 3 1, 4 3, 6 0, 7 5, 7 9, 9 3, 1 04, 1 0 7 ,

1 2 5, 1 42, 1 4 5 1 48, 1 5 5 1 5 6 1 5 9, 1 64, 1 8 3 1 9 8 2 0 3, 2 1 0, 2 1 6, 2 2 2, 2 2 3, 22 4, 242, 24 6, 24 7, 2 5 7, 2 6 6, 2 6 7 2 7 6, and 2 Amino acid residues at least in one portion in 92 other § Mi Roh acid residues replacement lipase to co one de, genes corresponding sites of Nukure Ochido sequence set forth in SEQ ID NO: 2 has been changed, and

9) the substitution of the following amino acid residues in the Amino acid sequence set forth in SEQ ID NO 1: G lyl 8 A la; M et 2 1 L eu; A sp 2 5 L eu; A sp 2 5 A rg; A sn 3 1 A sp; A sp 4 3 A sn; A 1 a 6 0 V a 1; I le 7 5 L eu; G ly 79 P ro; T hr 9 3 V al; V a 1 1 04 I le; V all 0 7 A la; G lyl 2 5 G ln; I lel 42 L eu; G lyl 4 5 S er; T hrl 4 8 A la; G 1 y 1 5 5 S er; S erl 5 6 G ly; T hrl 5 9 G ly; A lal 64 S er; P hel 8 3 T yr; S erl 9 8 L ys; A rg 2 0 3 S er; T hr 2 1 0 S er; V al 2 1 6 P he; L eu 22 2 A la; L eu 22 3 P he; M et 224 L eu; A rg 2 42 T hr; A rg 2 46 H is; M et 2 4 7 L eu; M et 2 5 7 L eu; T hr 2 6 6 V a 1; L eu 2 6 7 P he; a sp 2 7 6 S er; and G ly 2 9 2 S to at least 1 Tsuganasa lipase of the er co to one de , Hisage the gene according to the corresponding sites of nucleotide sequences set forth is changed to SEQ ID NO: 2 It is intended to. BRIEF DESCRIPTION OF THE DRAWINGS

Figure 1 shows a restriction map of plasmid p SDL 2 3. Arrows in the figure indicate the position of the structural gene of the lipase. Detailed Description of the Invention

In the claims and the specification, mutant lipase substituted and Amino acids Amino acids have been substituted it is expressed as follows. That is, the name (3 letter code) of the original Amino acid residues by connexion substitution mutation, the position to be substituted in Amino acids within the sequence, in the order of names of the amino acid residues after being replaced (3 letter code) It indicated by notation. For example, glycine position 1 8 mutants substituted with Aranin is denoted as G lyl 8 A la. In the present invention, a lipase gene encoding may be isolated from the chromosomal DNA by a known way of forming method of click Riazon on colony High Priestess Daize one Deployment Method Ya plate medium.

That is, in the colony High Priestess die peptidase one to down method, first to prepare a chromosomal DNA library scratch. Then, if all or part of the amino acid sequence of Riva Ichize is known, to prepare homologous Origonukureochi Dopurobu, it allows the lipase co one de performing colony hybridization using it gene it can be isolated.

Alternatively, the method of forming the click Riazon, lipase to produce a chromosomal DNA library in bacteria that do not produce, to flat plates onto agar containing a substrate for lipase. Bacteria with chromosomal DNA fragment containing the lipase gene, around colonies of that, because it forms a clear zone produced for lipase one zero to degrade substrate is co one de lipase by using it gene it can be isolated.

In the present invention, the Amino acid sequence having the amino acid sequence or at least 50% homologous with the Amino acid sequence of a lipase LP described in SEQ ID NO: 1, one or more Amino acids other Amino acid the substituted variant lipase as a method nucleotide sequence derives its altered gene so as to co one de is a lipase LP in gene heritage including co one sul nucleotide sequence of the lipase LP amino acid sequence of as long as it can cause a mutation in nucleotide sequence to cause the replacement of a target site amino acids may be used any method.

Such mutations in one way to cause a high frequency, there is a site-directed mutagenesis. The site-directed mutagenesis in the 铸型 wild type enzyme gene, a method for the synthesis Origonuku Reochi de having a base substitution mutation target site and mutagens (. J. Zoller, M. Smith, "Method in Enzymology" vol.100, R. Wu, L. Grossmann, K. Moldave ed., P468, an Academic Press (1983)), Kunkel (Kunkel) method (Kunkel, TA (1985) Proc. Natl. Acad. USA., 82, 488) and gears Ppudo duplex (Gapped duplex) method (Karmer, W. et al (1984) Nucl. AcidsRes., there is a 12, 9441) modification of such. Matapo Rimera Ichize method using a 'chain' Riakusho emissions (PCR) (Mullis, K., Faloona, F., Scharf, S., Saiki, R /. Horn, G. and Erlich, H., (1986) Cold Spring Harber Symp:. 263) there is also such.

Another method of causing the mutation, there is a random mutagenesis causing amino acid substitutions in particular constant morin mutation target site. Are several methods are known for this. For example, there is a method of introducing a plus Mi de incorporating the lipase gene in the mutator strain of E. coli. Further, for example, magnesium ions, a method (Zhou performing presence in poly ra one Ze chain 'reaction (PCR) reactions, such as manganese ions, Y., Zhang, X., Ebright, RH (1991) Nucleic Acid Research 19, 6052, Tindall, KR, Kunkel, TA (1988) Biochemistry 27, 6008-6013) and a method of performing DNA amplification reaction using no repair function DNA polymerase Ichize (Liao, X., Wise, JA ( 1990) Gene 107 - 111) is.

Furthermore, for example nitrous acid, formic acid, a method using a mutagenic agent such as hydrazine (Myers, RM, Lerman, LS, Maniatis, T. (1985) Science 229, 242- 247), and the like. How to cause mutations may use other whether Naru method is not limited thereto. For example, by mutation, such as natural or artificially ultraviolet, it is also considered gene Ru resulting process according to the present invention from a strain of the desired mutation has occurred.

The 銪型 for mutation, lipase gene, can be used, for example those incorporating a vector one good Una E. coli p UC system. The mutant lipase genes obtained as described above into a host bacterium. For example, when using Shiyudomonasu (Pseudomonas) bacteria as hosts, a method of stably maintained extrachromosomally with RSF 1 0 1 0 broad host range plasmid such as, in the form which can not be replicated in the host bacteria genes there is a method in which Komu assembled into the chromosome using.

The shoes Pseudomonas (Pseudomonas) if the bacterium used as the host, strange variant lipase is secreted into the culture medium. Separation and purification of the mutant lipase Ichize from the culture solution can be carried out according to a conventional method. For example, pressurizing example ammonium sulfate to the culture solution, a variant lipase crudely fractionating, after removal of the ammonium sulfate by dialysis, until a single-band in SDS polyacrylamide Riruami Dogeru electrophoresis by fractionated CM cellulose column the variant lipase is purified. Production of mutant lipase, and purification method is not limited to the above method, it is of course possible also in other ways.

Variant lipase of the present invention by a change in its physical properties or chemical properties, structure is stabilized, and Z or has been enhanced, it is possible to improve the properties such as thermal weaker qualitative and specific activity. Stabilization of structure, the direction to enhance the hydrophobic interaction of the internal structure, the direction to reduce the surface of the positive charge, the direction to stabilize the secondary structure, altering amino acid residues in the direction of stabilizing the loop structure It is achieved by.

Position of the preferred amino acid sequences to stabilize the structure, 1 8, 3 1, 6 0, 7 9, 9 3, 1 04, 1 2 5, 1 45, 1 5 5 1 64, 1 8 3, 2 0 3, 2 1 6, 2 2 3, 242, 246, 2 6 7, 2 is 92.

Specific examples of preferred substituted, G lyl 8 A la; A sn 3 1 A sp; A 1 a 6 0 V a 1; G ly 7 9 P ro; T hr 9 3 V al; V a 1 1 04 I le; G lyl 2 5 G ln; G lyl 4 5 S er; G lyl 5 5 S- er; A lal 64 S er; P hel 8 3 T yr; A rg 2 0 3 S er; V al 2 1 6 P he; L eu 223 P he; a rg 242 Th r; a rg 2 4 6 H is; L eu 2 6 7 P he, those with which 1 Tsuganasa least one substitution of G ly 2 9 2 S er and the like.

Also, the strengthening function, the direction of increasing positive charge near the active center, a direction to reduce the sublime of Amino acid residue, a direction to prevent the modification of the loop structure, the direction Heamino to reduce the structural shape of the interaction of the loop structure more is achieved by varying the residue.

Position of the preferred amino acid sequences to enhance functionality, 2 1, 2 5, 4 3, 7 5, 1 0 7, 1 4 2, 1 48, 1 5 6 1 5 9, 1 9 8 2 1 0, 22 2, 2 24, 2 4 7, 2 5 7, 2 6 6, 2 7 6.

Specific examples of preferred substituted, M et 2 1 L eu; A sp 2 5 L eu; A sp 2 5 A rg; A sp 4 3 A sn; I le 7 5 L eu; V al 1 0 7 A la ; I lel 42 L eu; T hrl 4 8 A la; S erl 5 6 G ly; T hrl 5 9 G ly; S erl 9 8 L ys; T hr 2 1 0 S er; L eu 2 2 2 A la ; M et 224 L eu; Me t 247 L eu; M et 2 5 7 L eu; T hr 2 6 6 V al; at least one of the substituents of a sp 2 7 6 S er include those being 1 Tsuganasa It is.

Incidentally, the substitution of the above-mentioned Amino acid residues, when applied to a lipase having the Amino acid sequences showing at least 50% homologous with Amino acid sequence according to SEQ ID NO: 1, positions thereof substituted If the homology of two amino acid sequences were juxtaposed amino acid sequence of the lipase having while providing a defect position as needed to maximize the amino acid sequence homology of placing serial in SEQ ID NO: 1 the position corresponding to, a representation at amino acid position of SEQ ID NO: 1. While the best mode invention for carrying out the invention will be described by way of example, the present invention is not limited to the following examples.

Example 1: Preparation of chromosomal DN A

Gerhard one Pseudomonas, main emission Doshina (Pseudomonas mendocina) SD 7 0 2 strain L medium (Poripepu tons 1%, 0.5% yeast extract, Na Application Benefits um 0.5% chloride) 3 was inoculated into Om l, at 37 after 1 晚 culture, removing the supernatant by centrifugation, to obtain the cells. This 0.4M chloride isocyanatomethyl Li um, 5 Omm preparative squirrel-HCl buffer containing 1 0mM E DTA (p H 8) was suspended in 5 m 1. This lysozyme 2.5mg and RN ase A 0.25 mg was added, 30 minutes gentle shaking at 37 ° C, were lysed. Then, for 10 minutes it was heated at 60 ° C, completely solubilized. The solution in TE buffer (10 mM preparative squirrel-HCl buffer containing 1 mM EDTA (p H 8)) Fuwenoru saturated with an equal volume added, gently mixed by inversion recovery upper aqueous layer by centrifugation it was repeated three times that. The aqueous layer was collected in third ethanol cooled to a 20 ° C 2 times was added and the precipitate was taken up in plastic rods. After re Nsu the precipitated sediment with ethanol, vacuum dried and redissolved in TE buffer 0.5 m 1.

Example 2: Preparation of chromosomal DNA library one

After partially digesting the chromosomal D NA restriction enzyme E c 0 RI, full Nord-black port Holm extracted and the DNA fragment was recovered by ethanol precipitation. On the other hand, it decomposes with old ink stick de p WE 1 5 similarly E co RI, was alkanoate Rihosufa synthetase process. Both were ligated with T 4 DNA ligase. The Re This was packaged into phage particles. The phage, maltose, pressurized example the E. coli culture 6 0 0 μ I cultured in L medium containing sulfuric Maguneshiumu, after 1 5 minutes incubation preparative 3 7 ° C, in addition to cormorants'll become the L medium lml, for 1 hour incubated preparative 3 7 ° C. The paste was applied on L plate medium containing ampicillin 5 0 ppm (L medium which solidified with Agarosu 1.5%), and 1 晚 incubated at 3 7 ° C. As a result, to obtain a transformants of about 1000 colonies.

Example 3: Preparation of oligonucleotide probe

The N-terminal Amino acid sequence of the purified lipase was separated off at Amino Acid Sequencer to obtain the results shown in SEQ ID NO: 3. The oligonucleotide probe shown in SEQ ID NO: 4 based on this synthesized in a DNA synthesizer.Thereto, Ί - 32 Ρ- A Τ Ρ and T 4 Porinuku Reochi Dokinaze was added, reacted at at 37, was radiolabeled.

Example 4: Isolation of the lipase gene encoding

Transformants about 1000 colonies was 1 晚 incubated at 3 7 ° C over two Toroseruro pass filter one placed on L plate medium. Peeled off filter, lysed for 10 minutes on paper braze immersed in 0.5M aqueous oxidation isocyanatomethyl Li um Z 1.5M chloride isocyanatomethyl Riumu solution, 1.5M diisocyanato chloride Li um, with 1 M preparative squirrel-HCl buffer (p H 7) soaked braze paper for 7 minutes, and neutralized twice. Form 2 hours sintered filters at 8 0 ° C, 0.5% dodecyl sodium sulfate (SDS) / 6 XSSC (1 XSSC is, 0.99 mM sodium chloride Zl 5 mM Kuen acid Natoriumu solution. N XSSC n times of 1 XSSC refers to the concentration of chloride isocyanatomethyl Riumu / Kuen acid sodium solution.) was washed residue of bacteria in. 0.1% sodium dodecyl sulfate (SD S) / 5 X Denhardt's solution (Denhardts solution) (0.1% ί ico 1 1, 0.1% poly Binirupiro Li pyrrolidone, 0.1% BSA) filter pre High Priestess die Ze in / 5 x SSC an attempt emission was carried out for 1 hour at 37 ° C. Similar solutions of the above radiolabeled Origonukureochi Dopurobu added in was performed 1 晚 the Haipuridaize one to emissions of filters 37 ° C. Then, for 10 minutes the filter with 4 XSSC, twice in 2 XSSC 20 minutes and then washed twice for 20 minutes in 1 XSSC.

As a result of such colony hybrida See sucrose down to give a number of positive colonies. The resulting old ink stick de recovered from one of the colonies, the fragments digested with E c 0 RI and separated by Agarosu electrophoresis and adsorbed into two Toroseru loin filter. Colony High Priestess die internalized the same way the procedure was subjected to Southern High Priestess die See Chillon in. As a result, it was hybridized to a fragment of 18 kbp.

This fragment was recovered and ligated into E co RI sites of plasmid P UC 1 1 9, and the E. coli J Ml 01 was transformed. The plasmid was recovered, digested with restriction enzymes S ac I, and subjected to Southern High Priestess die Ze one Deployment in the same procedure. As a result, we obtain a fragment of 2.3kbp.

Example 5: Nucleotide sequencing of lipase gene

A fragment of 2.3kbp obtained in Example 4 were consolidated into S ac I site of p UC 1 1 9, and the E. coli JM 1 01 was transformed. This plasmid was named p S DL 2 3. The restriction enzyme map of plasmid P SDL 23 illustrated in Figure 1. Using this positive Mi de, Jidokishi method Sanger (Sanger, F., Nicklen, S., Coulson, AR (1977) Pro Natl. Acad. Sci. USA., 74, 5463) at nucleotide lipase gene DN A and sequenced. That is, using the ABI's die de O carboxymethyl coater Mine Isseki one-Shigenshingu-kit, and analyzed the nucleotide sequence by DNA sequencer. As a result, to obtain a nucleotide sequence encoding a lipase one zero as SEQ ID NO: 2. Shows the Amino acid sequence deduced from this sequence SEQ ID NO: 1.

Construction of mutant lipase gene by site-directed mutagenesis: Example 6

Site Amino acid residues specifically substituted variants of lipase (A 1 a 60

V al Moshiku constructed a gene for L eu 223 P he), as follows. To convert the partially specifically Amino acids, oligonucleotides shown in SEQ ID NO: 5 and SEQ ID NO: 6 was chemically synthesized and used to re-phosphorylated 5 'ends using of T 4 polynucleotide kinase. On the other hand, 铸型 mutations was used bra scan Mi de p SDL 23 (FIG. 1). Using p SDL 23 E. coli B W31 3 strains (H fr KL 1 6 POZ45 [lys A (61 - 62)], dut 1, nu 1, thy- 1, re 1 A 1) was transformed, this form from quality transformants, main ashing et al. method (Viera.J. and Messing, J. (1987) method in Enzymology, 153, 3-11) according to prepare a single-stranded DNA, some of Dokishichimi down in the DNA There obtain single-stranded DNA replacing a Dokishiurashiru was used as 铸型.

Mutagens were prepared as described above O oligo nucleotides and 铸型 DNA the Aniri Ngubaffu § chromatography (2 Omm Tris-HCl buffer (p H 8), 1 0 mM magnesium chloride, 5 Omm sodium chloride, I mM D TT) It was mixed at medium, 1 5 minutes allowed to stand at 65 ° C, for 1 5 minutes to stand at 37 ° C, and the mutagens oligonucleotide is Aniri ring to the target site of mutation.

Next, the DN A mixture of 2.5 volumes of Extension buffer (50 mM T ris HC l, pH8.0, 6 OmM CHgCOONH ,. 5 mM M g C l 2, 5 m MD TT, I mM NAD, 0.5 m M dATP, 0.5 mM d CTP, 0.5 mM dGT P, 0.5 m M d TTP) was added, further E. coli DNA ligase and T 4 by the addition of DNA polymerase complementary to stand 2 hours = 25 ° C in the synthesis of the chain went. Then, E. coli BMH 71 with the DN A - a 1 8 mut S transformed colonies were selected for ampicillin resistance. Several Karapu Rasumi de DN A of the transformants are prepared, to determine the Nukure O Ji de sequence similarly by Jidokishi method as in Example 5, is converted into codons corresponding to amino acid residues of interest It was confirmed.

After complete degradation of plasmid prepared as described above by S ac I, the DN A fragment containing the mutant lipase gene portion was fractionated Agarosugeru electrophoresis, and extracted and purified from in Agarosugeru. After completely decompose pM FY 42 is a broad-host-range base Kuta one S ac I, mixed with DN A fragment containing the purified mutant lipase gene portion as described above, by the T 4 DN A ligase connexion perform ligation reaction, Escherichia coli J Ml 01 strain was transformed, and colonies were selected for kanamycin resistance. These extracted plasmid DNA from the transformant, purified, analyzed, to obtain a plasmid which S ac I DNA fragment was inserted containing the mutant lipase genes in S ac I cleavage site PMFY 42. Example 7: Preparation of the lipase

Using a plasmid containing a plasmid or wild type lipase gene including the variant lipase gene obtained in Example 6, a lipase-deficient strain LD 9 strain (Gerhard one Pseudomonas, main emission Doshina (Pseudomonas mendocina) in SD 702 strain N- methyl-N, one nitro one N- nitroso guaiacolsulfonate reacted with two gin, cultured plated on plate medium containing lipase substrate, electronics mutant strains) obtained by selecting a strain that does not form formed a click Riazon Toropore to transformed with emission method to select kanamycin-resistant colonies. That is, after the first LD 9 strains were grown in L medium 5 m 1 to OD == 0.7, the cells were collected by centrifugation. The bacterial cells were suspended in sterilized water, was recovered again, and resuspended in 5 0 0 1 sterile water. Plus Mi de DNA was added to the cell suspension, was transferred to the electrode with 4 mm cell, Ola head (BI0RAD) manufactured by Gene. Pulser one-Ereku Toroporeshiyo emissions. High voltage by the system (Gene Pulser electropolation system) electrical 0 Noresu (¾ pressure 2.5k V, capacitance 2 5 F, resistor 1000 [Omega]) were given. Thereafter, the L medium lm 1 was added to the bacterial suspension Nigoeki, 3 7 ° After 1 hour shaking culture at C, L plate medium containing Emaru John O Li one Buoiru a substrate for kanamycin 2 0 ppm and lipase It was applied to. 3 7 1 晚 cultured ° C, of ​​the grown co Roni one, were selected that formed clear zones around colonies to obtain transformant strains.

The transformant strain, Tween (Tw een) 8 0 containing 1%, carbonate Na Application Benefits um 3 5 ° in lipase production medium 3 0 O m 1 adjusted to PH 9 with C. 1 4 hours with shaking cultured, it was produced and secreted a variant lipase in the culture medium. Culture of this was centrifuged, The supernatant was the crude enzyme solution was prepared. This fractionated ammonium sulfate precipitation, after removal of the ammonium sulfate by dialysis, were treated with CM cellulose column and purified to single bands in SDS polyacrylamide Riruami Dogeru electrophoresis.

Example 8: The specific activity of the variant lipase

The number of molecules of the variant lipase by site-directed mutagenesis purified in Example 7

In the constant absorption of 2 8 0 nm to measure the activity, compared to wild-type lipase. Activity measurements were carried out by the following methods.

Dissolved p- nitro off We sulfonyl palmitate over preparative (hereinafter abbreviated as p NPP) in isopropyl alcohol so as to 2 m gZ m 1. The p NPP solution and 1 0 0 mM bicine buffer (Bicine buffer) (p H 8.0) 1: 1 mixed at a ratio of 0, and a substrate solution. Substrate solution 5 0 0 mu I enzyme solution 2 0 1 was added to and reacted 1-1 0 min at room temperature, quenched with 200 1 added 1 N hydrochloric acid, the measuring absorbance 405 nm in a spectrophotometer to.

Table 1 shows the values ​​of specific activity when the activity of the wild-type enzyme 1 00. Example 9: Thermal stability of the variant lipase

Wild-type lipase was measured as follows thermostability of the variant (A la 60V al and L eu 223 P he) lipase by site-specific mutations prepared above. Of the activity value amount, in variant lipase solution and wild-type lipase solution 5 Omm borate buffer (p HIO), After incubation for 1 0 minutes at 60 ° C, the lipase activity. Table 1 shows the results when the activity before the heat treatment of the wild-type enzyme 1 00.

Enzyme specific activity thermostability

Wild-type 1 00 51

Ala 60 Val 98 59

Leu 223 Phe 64 84 Effect of the Invention

The genes of the present invention, the lipase according to the present invention, i.e. the wild-type lipase LP Moshiku is facilitated production and modifications thereof variant lipase.

Moreover, by modification of lipase LP according to the invention has a novel Amino acid sequence, as compared to the lipase LP, for example, heat rise, etc. stability properly the specific activity, the physical properties or chemical properties due to the application field compatible so altered variant lipase can be obtained, detergents, food processing, industrial fields such as papermaking industry can provide useful lipases. SEQ ID NO: 1

The length of the sequence: 2 9 3

The type of the sequence: amino acid

Topology: linear

Array of categories: protein

origin

Biological name: Gerhard one Tomonasu mendocina (Pseudomonas mendocina; stock name: SD 7 0 2

Array

Ala Trp Phe Gly Ser Ser Gly Tyr Thr Gin Thr Lys Tyr Pro lie Val 1 5 10 15

Leu Gly His Gly Met Leu Gly Phe Asp Ser He Leu Gly Val Asn Tyr

20 25 30

Trp Tyr Gly lie Pro Ala Ala Leu Arg Arg Asp Gly Ala Ser Val Tyr

35 40 45

Val Thr Glu Val Ser Gin Leu Asp Thr Ser Glu Ala Arg Gly Glu Gin 50 55 60

Leu Leu Gin Gin Val Glu Asp lie Val Ala lie Ser Gly Lys Gly Lys

65 70 75 80

Val Asn Leu He Gly His Ser His Gly Gly Pro Thr Thr Arg Tyr Val

85 90 95

Ala Ala Val Arg Pro Asp Leu Val Ala Ser Val Thr Ser Val Gly Ala

100 105 110

Pro His Lys Gly Ser Ala Ala Ala Asp Phe Leu Lys Gly lie Ser Asp

115 120 125

Gly Pro Ala Gly Pro Val Ala Thr Pro Leu Leu Ala Gly lie Val Asn 130 135 140 Gly Leu Gly Thr Leu lie Asn Phe Leu Ser Gly Ser Ser Ser Thr Thr 145 150 155 160

Pro Gin Asn Ala Leu Gly Ser Leu Glu Ser Leu Asn Ser Glu Gly Ala

165 170 175 Ala Arg Phe Asn Ala Lys Phe Pro Gin Gly lie Pro Thr Ser Ala Cys

180 185 190

Gly Glu Gly Ala Tyr Ser Val Asn Gly Val Arg Tyr Tyr Ser Trp Ser

195 200 205

Gly Thr Ser Pro Leu Thr Asn Val Leu Asp Pro Ser Asp Leu Leu Met 210 215 220

Gly Ala Ser Ser Leu Thr Phe Gly Ser Glu Ala Asn Asp Gly Leu Val 225 230 235 240

Gly Arg Cys Ser Ser Arg Met Gly Gin Val lie Arg Asp Asn Tyr Arg

245 250 255 Met Asn His Leu Asp Glu Val Asn Gin Thr Leu Gly Leu Thr Ser Leu

260 265 270

Phe Glu Thr Asp Pro Val Thr Val Tyr Arg Gin His Ala Asn Arg Leu

275 280 285

Lys Asn Ala Gly Leu

290 SEQ ID NO: 2

The length of the array: 8 7 9

The type of the array: Nucleic Acids

The number of chains: double-stranded

Topology: linear

Array of type: Genomic DNA

origin

Biological name: Shiyudomonasu mendocina (Pseudomonas mendocina) Co., Ltd. Name: SD 7 0 2

Features of the array

Symbol representing the characteristics: mat peptide

Existing position:. 1.879

Method to determine the feature: S

Array

GCC TGG TTC GGC TCC TCC GGC TAC ACC CAG ACC AAG TAC CCC ATC GTC 48 Ala Trp Phe Gly Ser Ser Gly Tyr Thr Gin Thr Lys Tyr Pro lie Val 1 5 10 15

CTC GGC CAC GGC ATG CTC GGC TTC GAC AGC ATC CTC GGC GTC AAT TAC 96

Leu Gly His Gly Met Leu Gly Phe Asp Ser lie Leu Gly Val Asn Tyr

20 25 30

TGG TAT GGC ATC CCG GCC GCC CTG CGC CGC GAC GGT GCC AGC GTC TAC 144 Trp Tyr Gly lie Pro Ala Ala Leu Arg Arg Asp Gly Ala Ser Val Tyr

35 40 45

GTC ACC GAG GTC AGT CAG CTC GAT ACC TCC GAA GCG CGC GGC GAG CAG 192 Val Thr Glu Val Ser Gin Leu Asp Thr Ser Glu Ala Arg Gly Glu Gin

50 55 60

TTG CTG CAG CAA GTC GAG GAT ATC GTC GCC ATC AGC GGC AAA GGC AAG 240 Leu Leu Gin Gin Val Glu Asp lie Val Ala lie Ser Gly Lys Gly Lys

65 70 75 80

GTC AAT CTG ATC GGC CAC AGC CAC GGC GGC CCC ACC ACG CGC TAC GTT 288 Val Asn Leu lie Gly His Ser His Gly Gly Pro Thr Thr Arg Tyr Val

85 90 95

GCC GCC GTG CGG CCG GAC CTG GTC GCC TCG GTC ACC AGC GTC GGT GCA 336

Ala Ala Val Arg Pro Asp Leu Val Ala Ser Val Thr Ser Val Gly Ala

100 105 110

CCG CAC AAG GGC TCG GCC GCT GCC GAC TTC CTC AAG GGC ATC AGC GAT 384 Pro His Lys Gly Ser Ala Ala Ala Asp Phe Leu Lys Gly He Ser Asp -

m 313 393 QVV 339 V0 9V3 100 3VX 3X3 33V 0X9 933 XV9 33V 9V0 OIL

m 092

J "31 Π31 iqi ui3 usy ΐ¾ nig dsy ng ^ si {{usy H

918 3X3 30V 33V 9X3 330 9X3 33V 9V3 3VV 3X3 3V3 3V0 3X3 0Ώ 3VV 9XV 丄 usy dsy Sjy UI9; 3M S-iV s-iy

89L 093 3VI 3VV 3VD 0D3 9V3 309 9XV 333 03X 10V 30X 393 330

Λ dsy usy Interview io sqd -iqi nai • I3S s BTV

310 3X3 300 3V0 OVV 339 3V0 031 3D9 3X1 30V 013 931 33X 339 300 02 n9q dsy JGS OJJ dsy usv I nsq 0Jd S

2Z9 DIV 013 9X3 OVO 33V 333 OVO 313 919 3VV 03V 013 933 39V 33V 300

SOS 002 96T

J Interview ΑΐΟ usy m Interview ^ TV niO 5ΐ ^ 9 3DV 901 0.丄 3VI IVl 393 310 390 3VV 013 39V 3VI V3G 990 WO 399

06T 081

JRI OJJ 3TI 9¾i sAq BIV usy sqd

X3X 330 33V 33V 333 OXV 300 9V3 333 3XX 3VV ODD XVV 3XX 303 333

S9I Οΐ eiV ηΐθ usv J3S Aio Π9 ^ IV usy u [9 OJJ

330 333 VVG 33V 3VV 313 D3I 9V0 913 03X 100 0X0 339 3VV 9V3 933

09T SSI OS!

■ I9S J3S usy an nsq • iqi naq Λ ο

08 ^ 33V 33V 30V 331 XOV 309 331 j OkLtL 3VV OXV 0X3 03V 390 013 390

O

usy A 3Π Βΐν BIV m BTV ojj Ai

Z 3VV 310 DIV 309 D 010 0X3 333 VOV 339 310 933 900 330 333 390

021

S96lO / t? 6df / XDd £ 8 I / S6 OAV Phe Glu Thr Asp Pro Val Thr Val Tyr Arg Gin His Ala Asn Arg Leu

275 280 285

AAG AAC GCC GGG CTA 879 Lys Asn Ala Gly Leu

290 SEQ ID NO: 3

The length of the sequence: 3 0

Biological name: shoot Monas mendocina (Pseudomonas mendocina Li

Ltd. Name: SD 7 0 2

Array

Ala Trp Phe Gly Ser Ser Gly Tyr Thr Gin Thr Lys Tyr Pro lie Val 1 5 10 15

Leu Gly His Gly Met Leu Gly Phe Asp Ser lie Leu Gly Val

20 25 30 SEQ ID NO: 4

The length of the sequence: 2 0

The type of the array: Nucleic Acids

The number of chain: single-stranded

Topology: linear

Sequence type: other nucleic acid synthetic DNA

Array

CACGGCATGC TCGGCTTCGA 20 SEQ ID NO: 5

The length of the sequence: 2 2

The type of the array: Nucleic Acids

Number of strands: single strand Topology: linear sequence type: other nucleic acid synthetic DNA sequence

ACCTCCGAAG TCCGCGGCGA GC 22 SEQ ID NO: 6

The length of the sequence: 29

The type of the array: Nucleic Acids

The number of chain: single-stranded

Topology: linear

Sequence type: other nucleic acid synthetic DNA sequence

TCGACCCCAG CGATCTGTTC ATGGGCGCC 29

Claims

The scope of the claims
1) gene containing part properly even all of the nucleotide sequences described lipase described in SEQ ID NO: 2 that co one de in SEQ ID NO: 1.
Genes range 囲第 one of claims claim comprising a portion of the nucleotide sequence set forth in 2) SEQ ID NO: 2.
3) gene, all containing Muripa nucleotide sequence set forth in SEQ ID NO: 2 - Gene ranging first claim of claim is zero gene.
4) SEQ ID NO: 1 has been at least one position variant lipase Amino acid residues are substituted with another Amino acid residues of the Amino acid sequence according to.
5) The next position in the amino acid sequence having at least 50% or more homology Amino acid sequence also properly from its Amino acid sequence set forth in SEQ ID NO: 1: 1 8, 2 1, 2 5, 3 1 , 43, 60, 75, 79, 93, 1 04, 1 0 7, 1 2 5, 1 42, 1 4 5 1 4 8, 1 5 5 1 5 6 1 5 9,
1 64, 1 8 3 1 9 8 2 0 3 2 1 0, 2 1 6, 22 2, 22 3, 2 2 4, 242, 2 46, 2 4 7 2 5 7, 2 6 6, 2 6 7, 2 7 6, and 2 9 2 of at least portions variant lipase Amino acid residues are substituted with other § Mi Bruno acid residues.
6) the following substitutions: G 1 y 1 8 A 1 a M et 2 1 L eu; A sp 2 5 L eu; A sp 2 5 A rg; A sn 3 1 A sp; A sp 4 3 A sn; A 1 a 6 0 V a 1; I le 7 5 L eu; G ly 7 9 P ro; T hr 9 3 V a 1; V a 1 1 0 4 I le; V all 0 7 A la; G lyl 2 5 G ln; I lel 42 L eu; G lyl 4 5 S er; T hrl 4 8 A la; G ly 1 5 5 S er; S er 1 5 6 G 1 y; T hr 1 5 9 G 1 y; A 1 a 1
64 S er; P hel 8 3 T yr; S er 1 9 8 L ys; A rg 2 0 3
S er; T hr 2 1 0 S er; V al 2 1 6 P he; L eu 222 A 1 a; L eu 223 P he; Me t 224 L eu; A rg 242 Th r; A rg 246 H is; Me t 247 L eu; Me t 257 L eu; T hr 266 V a 1; L eu 267 P he; a sp 276 S er; and at least claims comprising one of the G 1 y 292 S er variant lipase of paragraph 5, wherein.
7) genes comprising all or part of the mutant lipase the code sul nucleotide sequence according to any one of the paragraphs claims paragraph 4 to paragraph 6.
8) The next position in the Amino acid sequence set forth in SEQ ID NO: 1 18 21, 25, 31, 43, 60, 75, 79, 93, 104, 1 07, 125, 142, 145, 148, 155, 156, 159, 164, 183, 198, 203, 210, 216, 222, 223, 224, 242, 246, 247, 257, 266, 267, 276 or of at least one portion of the two 92 Amino acid residue, the lipase groups are substitution to other Amino acid residue to co one de, of Nukure Ochido sequence set forth in SEQ ID NO: 2 corresponding site is changed gene.
9) the substitution of the following Amino acid residues in the Amino acid sequence set forth in SEQ ID NO 1: G lyl 8 A la; Me t 21 L eu; A sp 25 L eu; A sp 25A rg; A sn 31 A sp ; A sp 43 A sn; A la 60 V a 1; I le 75 L eu; G ly 79 P ro; Th r 93 V al; V a 1 104 1 le; V all 07A la; G lyl 25 G ln; I lei 42 L eu; G lyl 45 S er; Th rl 48 A la; G lyl 55 S er; S erl 56 G ly; Th rl 59 G ly; A lal 64 S er; P hel 83 Ty r; S erl 98 L ys; A rg 203 S er; Th r 21 0 S er; V al 216 P he; L eu 222 A la; L eu 223 P he; Me t 224 L eu; A rg 242 Th r; A rg 2 of and G ly 2 9 2 S er; 46 H is; Me t 247 L eu; Me t 257 L eu; T hr 266 V a 1; L eu 2 6 7 P he; a sp 2 7 6 S er the least 1 Tsuganasa lipase to co one de, gene described in the scope paragraph 8 claims corresponding site is changed in nucleotide sequence set forth in SEQ ID NO: 2.
PCT/JP1994/001965 1993-11-24 1994-11-21 Lipase gene and variant lipase WO1995014783A1 (en)

Priority Applications (2)

Application Number Priority Date Filing Date Title
JP5293631A JPH07143883A (en) 1993-11-24 1993-11-24 Lipase gene and mutant lipase
JP5/293631 1993-11-24

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Country Status (2)

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WO (1) WO1995014783A1 (en)

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