WO2005093073A1 - Exo-endo cellulase fusion protein - Google Patents
Exo-endo cellulase fusion protein Download PDFInfo
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- WO2005093073A1 WO2005093073A1 PCT/US2005/010158 US2005010158W WO2005093073A1 WO 2005093073 A1 WO2005093073 A1 WO 2005093073A1 US 2005010158 W US2005010158 W US 2005010158W WO 2005093073 A1 WO2005093073 A1 WO 2005093073A1
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- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
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- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
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- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
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- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
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- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
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- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01091—Cellulose 1,4-beta-cellobiosidase (3.2.1.91)
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- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
Definitions
- the present invention relates to a heterologous exo-endo cellulase fusion construct, which encodes a fusion protein having cellulolytic activity comprising a catalytic domain derived from a fungal exo-cellobiohydrolase and a catalytic domain derived from an endoglucanase.
- the invention also relates to vectors and fungal host cells comprising the heterologous exo-endo cellulase fusion construct as well as methods for producing a cellulase fusion protein and enzymatic cellulase compositions.
- Cellulose and hemicellulose are the most abundant plant materials produced by photosynthesis. They can be degraded and used as an energy source by numerous microorganisms, including bacteria, yeast and fungi, which produce extracellular enzymes capable of hydrolysis of the polymeric substrates to monomeric sugars (Aro et al., 2001). As the limits of non-renewable resources approach, the potential of cellulose to become a major renewable energy resource is enormous (Krishna et al., 2001). The effective utilization of cellulose through biological processes is one approach to overcoming the shortage of foods, feeds, and fuels (Ohmiya et al., 1997).
- Endoglucanases act mainly on the amorphous parts of the cellulose fiber, whereas cellobiohydrolases are also able to degrade crystalline cellulose.
- Cellulases are known to be produced by a large number of bacteria, yeast and fungi. Certain fungi produce a complete cellulase system capable of degrading crystalline forms of cellulose, such that the cellulases are readily produced in large quantities via fermentation.
- the complete cellulase system comprising components from each of the CBH, EG and BG classifications is required, with isolated components less effective in hydrolyzing crystalline cellulose (Filho et al., 1996).
- EG-type cellulases interact to more efficiently degrade cellulose than either enzyme used alone (Wood, 1985; Baker et al., 1994; and Nieves et al., 1995).
- cellulases are known in the art to be useful in the treatment of textiles for the purposes of enhancing the cleaning ability of detergent compositions, for use as a softening agent, for improving the feel and appearance of cotton fabrics, and the like (Kumar et al., 1997).
- Cellulase-containing detergent compositions with improved cleaning performance US Pat. No. 4,435,307; GB App. Nos.
- Trichoderma cellulase production has been improved by classical mutagenesis, screening, selection and development of highly refined, large scale inexpensive fermentation conditions. While the multi-component cellulase system of Trichoderma spp. is able to hydrolyze cellulose to glucose, there are cellulases from other microorganisms, particularly bacterial strains, with different properties for efficient cellulose hydrolysis, and it would be advantageous to express these proteins in a filamentous fungus for industrial scale cellulase production. However, the results of many studies demonstrate that the yield of bacterial enzymes from filamentous fungi is low (Jeeves et al., 1991).
- a heterologous exo-endo cellulase fusion construct which includes the coding region of a fungal exo-cellobiohydrolase (CBH) catalytic domain and a coding region of an endoglucanase (EG) catalytic domain, has been introduced and expressed in a filamentous fungi host cell to increase the yield and effectiveness of cellulase enzymes.
- CBH fungal exo-cellobiohydrolase
- EG endoglucanase
- the invention includes a heterologous exo-endo cellulase fusion construct comprising in operable linkage from the 5' end of said construct, (a) a DNA molecule encoding a signal sequence, (b) a DNA molecule encoding a catalytic domain of an exo-cellobiohydrolase, and (c) a DNA molecule encoding an endoglucanase catalytic domain.
- the heterologous exo-endo cellulase fusion construct further comprises a linker sequence located 3' of the catalytic domain of the exo- cellobiohydrolase and 5' of the catalytic domain of the endoglucanase.
- the heterologous exo-endo cellulase fusion construct lacks the cellulose binding domain (CBD) of the exo-cellobiohydrolase.
- the heterologous exo-endo cellulase fusion construct further comprises a kexin site located after the linker sequence and before the coding region of the endoglucanase catalytic domain.
- the endoglucanase catalytic domain is derived from a bacterial endoglucanase.
- the bacterial endoglucanase catalytic domain is selected from the group consisting of an Acidothermus cellulolyticus GH5A endoglucanase I (E1 ) catalytic domain; an Acidothermus cellulolyticus GH74 endoglucanase (GH74-EG) catalytic domain: and a Thermobifida fusca E5 endoglucanase (Tf-E5) catalytic domain.
- the heterologous exo- endo cellulase fusion construct lacks the cellulose binding domain of the endoglucanase.
- the endoglucanase is an Acidothermus cellulolyticus GH5A E1 and particularly the Acidothermus cellulolyticus GH5A E1 having an amino acid sequence of at least 90% sequence identity with the sequence set forth in SEQ ID NO. 8.
- the heterologous exo-endo cellulase fusion construct comprises a terminator sequence located 3' to the endoglucanase catalytic domain.
- the heterologous fusion construct comprises a selectable marker.
- the invention includes a vector comprising in operable linkage a promoter of a filamentous fungus secretable protein, a DNA molecule encoding a signal sequence, a DNA molecule encoding a catalytic domain of a fungal exo-cellobiohydrolase, a DNA molecule encoding a catalytic domain of an endoglucanase, and a terminator.
- the vector will further include a selectable marker.
- the vector will comprise a linker located 3' of the exo-cellobiohydrolase (CBH) catalytic domain and 5' of the EG catalytic domain.
- the vector will lack the CBH cellulose binding domain.
- the vector will comprise a kexin site.
- the catalytic domain of the endoglucanase is derived from a bacterial endoglucanase.
- the vector lacks the cellulose binding domain of the endoglucanase.
- the invention includes a fungal host cell transformed with a heterologous exo-endo cellulase fusion construct or a fungal host cell transformed with a vector comprising a heterologous exo-endo cellulase fusion construct.
- the invention includes a recombinant fungal cell comprising the heterologous exo-end cellulase fusion construct or a vector comprising the same.
- the fungal host cell is a Trichoderma host cell and more particularly a strain of T reesei.
- native cellulase genes such as cbhl, cbh2, egl1 and egl2 have been deleted from the fungal cells.
- the native cellulose binding domain has been deleted from the fungal cells.
- the invention includes an isolated cellulase fusion protein having • cellulolytic activity which comprises an exo-cellobiohydrolase catalytic domain and an endoglucanase catalytic domain, wherein the exo-cellobiohydrolase lacks a cellulose binding domain.
- the exo-cellobiohydrolase is a CBH1.
- the catalytic domain of the endoglucanase is derived from a bacterial cell.
- the bacterial cell is a strain of Acidothermus cellulolyticus.
- the invention concerns a cellulolytic composition comprising the isolated cellulase fusion protein.
- the invention includes a method of producing an enzyme having cellulolytic activity comprising, a) stably transforming a filamentous fungal host cell with a heterologous exo-endo cellulase fusion construct or vector as defined above in the first aspect and second aspect; b) cultivating the transformed fungal host cell under conditions suitable for said fungal host cell to produce an enzyme having cellulolytic activity; and c) recovering said enzyme.
- the filamentous fungal host cell is a Trichoderma cell, and particularly a T. reesei host cell.
- the exo- cellobiohydrolase is a CBH1 and the endoglucanase is an Acidothermus cellulolyticus endoglucanase or a Thermobifida fusca endoglucanase.
- the recovered enzyme is a cellulase fusion protein, components of the cellulase fusion protein, or a combination of the cellulase fusion protein and the components thereof.
- the recovered enzyme(s) is purified.
- the invention includes a Trichoderma host cell which expresses a cellulase fusion protein, wherein said fusion protein comprises a catalytic domain of an exo-cellobiohydrolase and a catalytic domain of an endoglucanase, wherein the exo-cellobiohydrolase lacks a cellulose binding domain.
- the Trichoderma host cell is a T. reesei cell.
- the exo- cellobiohydrolase is a CBH1 and the endoglucanase is an Acidothermus cellulolyticus endoglucanase and particularly an Acidothermus cellulolyticus E1 or GH74 endoglucanase.
- the endoglucanase lacks a cellulose binding domain.
- the T reesei host cell includes deleted native cellulase genes.
- the invention includes a fungal cellulase composition comprising a cellulase fusion protein or components thereof, wherein the fusion protein or components thereof is the product of a recombinant Trichoderma spp.
- Figure 1 is a representation of a heterologous exo-endo cellulase fusion construct encompassed by the invention, which includes a Trichoderma reesei cbhl promoter, a cbhl core (cbhl signal sequence and cbhl catalytic domain), a cbhl linker sequence, a kexin site, an E1 core (an Acidothermus cellulolyticus E1 endoglucanase catalytic domain), a cbh ⁇ terminator and an A. nidulans amdS selectable marker.
- Figure 2 is a DNA sequence (SEQ ID NO: 1) of the T.
- Figure 4 is an illustration of a nucleotide sequence (SEQ ID NO: 7) encoding an Acidothermus cellulolyticus GH5A endoglucanase I (E1 ) catalytic domain.
- Figure 5 is the predicted amino acid sequence (SEQ ID NO: 8) of the Acidothermus cellulolyticus GH5A E1 catalytic domain based on the nucleotide sequence provided ins Figure 4.
- Figures 6A and 6B are an illustration of a nucleotide sequence (SEQ ID NO: 9) encoding an Acidothermus cellulolyticus GH74- EG catalytic domain.
- Figure 11 is the predicted amino acid sequence (SEQ ID NO: 14) of the cellulase fusion protein based on the nucleic acid sequence in Figure 10.
- Figure 12 provides a schematic diagram of the pTrex4 plasmid, which was used for expression of a heterologous exo-endo cellulase fusion construct (CBH1-endoglucanase) as described in the examples and includes the Trichoderma reesei cbhl promoter, the T.
- CBH1-endoglucanase a heterologous exo-endo cellulase fusion construct
- FIG. 13A - E provide the nucleotide sequence (SEQ ID NO: 15) (10239 bp) of the pTrex4 plasmid of Figure 12 without the catalytic domain of the EG gene of interest.
- Figure 14 illustrates a SDS-PAGE gel of supernate samples of shake flask growth of clones of a T reesei strain deleted for the cellulases, cbhl, cbh2, egll and egl2 and transformed with the CBH1-E1 fusion construct.
- Lanes 1 and 10 represent MARK 12 Protein Standard (Invitrogen, Carlsbad, CA).
- Lanes 2 - 8 represent various transformants and lane 9 represents the untransformed 7 " . reesei strain.
- the upper arrow indicates the cellulase fusion protein and the lower arrow indicates the cleaved E1 catalytic domain.
- Figure 15 illustrates a SDS-PAGE gel of supernate samples of shake flask growth of clones of a T. reesei strain deleted for the cellulases, cbhl, cbh2, egll and egl2 and transformed with the CBH1-GH74 fusion construct.
- Lane 1 represents the untransformed control.
- Lane 3 represents MARK 12 Protein Standard (Invitrogen, Carlsbad, CA).
- Lanes 2 and 4 - 12 represent various transformants.
- the upper arrow indicates the CBH1-GH74 fusion protein and the lower arrow indicates the cleaved GH74 catalytic domain.
- Figure 16 illustrates a SDS-PAGE gel of supernate samples of shake flask growth of clones of a T.
- Lanel represents MARK 12 Protein Standard (Invitrogen, Carlsbad, CA). Lane 2 represents the untransformed strain and lanes 3 - 12 represent various transformants. Arrows indicate new bands observed in the CBH1- TfE5 expressing transformants.
- Figure 17 illustrates the % cellulose conversion to soluble sugars over time for a T. reesei parent strain comprising native cellulase genes with a corresponding T. reesei strain which expresses the CBH1-E1 fusion protein and reference is made to example 3.
- nucleic acids are written left to right in 5' to 3' orientation; amino acid sequences are written left to right in amino to carboxy orientation, respectively.
- components of a cellulase fusion protein refers to individual (cleaved) fragments of the cellulase fusion protein, wherein each fragment has cellulolytic activity and includes one of the catalytic domains of the fusion protein.
- cellulase refers to a category of enzymes capable of hydrolyzing cellulose (beta- 1 ,4-glucan or beta D-glucosidic linkages) polymers to shorter cello-oligosaccharide oligomers, cellobiose and/or glucose.
- exo-cellobiohydrolase (CBH) refers to a group of cellulase enzymes classified as EC 3.2.1.91.
- CBH enzymes hydrolyze cellobiose from the reducing or non-reducing end of cellulose.
- a CBH1 type enzyme preferentially hydrolyzes cellobiose from the reducing end of cellulose and a CBH2 type enzyme preferentially hydrolyzes the non- reducing end of cellulose.
- endoglucanase (EG) refers to a group of cellulase enzymes classified as EC 3.2.1.4.
- An EG enzyme hydrolyzes internal beta-1 ,4 glucosidic bonds of the cellulose.
- beta-glucosidases refers to a group of cellulase enzymes classified as
- cellulose binding domain refers to a portion of the amino acid sequence of a cellulase or a region of the enzyme that is involved in the cellulose binding activity of a cellulase.
- Cellulose binding domains generally function by non-covalently binding the cellulase to cellulose, a cellulose derivative or other polysaccharide equivalent thereof.
- CBDs typically function independent of the catalytic domain.
- a nucleic acid is "operably linked" when it is placed into a functional relationship with another nucleic acid sequence.
- DNA encoding a signal peptide is operably linked to DNA encoding a polypeptide if it is expressed as a preprotein that participates in the secretion of the polypeptide; a promoter is operably linked to a coding sequence if it affects the transcription of the sequence.
- operably linked means that the DNA sequences being linked are contiguous, and, in the case of the heterologous exo-endo cellulase fusion construct contiguous and in reading frame.
- the term "gene” means the segment of DNA involved in producing a polypeptide chain, that may or may not include regions preceding and following the coding region, e.g.
- polypeptide refers to a compound made up of a single chain of amino acid residues linked by peptide bonds.
- protein as used herein may be synonymous with the term “polypeptide” or may refer, in addition, to a complex of two or more polypeptides.
- nucleic acid molecule includes RNA, DNA and cDNA molecules.
- heterologous nucleic acid sequence has a portion of the sequence, which is not native to the cell in which it is expressed.
- heterologous with respect to a control sequence refers to a control sequence (i.e. promoter or enhancer) that does not function in nature to regulate the same gene the expression of which it is currently regulating.
- heterologous nucleic acid sequences are not endogenous to the cell or part of the genome in which they are present, and have been added to the cell, by infection, transfection, transformation, microinjection, electroporation, or the like.
- a "heterologous" nucleic acid sequence may contain a control sequence/DNA coding sequence combination that is the same as, or different from a control sequence/DNA coding sequence combination found in the native cell.
- the term heterologous nucleic acid sequence encompasses a heterologous exo-endo cellulase fusion construct according to the invention.
- the term "vector” refers to a nucleic acid sequence or construct designed for transfer between different host cells.
- host cell a cell that contains a heterologous exo-endo cellulase fusion construct encompassed by the invention or a vector including the same and supports the replication, and/or transcription or transcription and translation (expression) of the heterologous exo-endo cellulase construct.
- Host cells for use in the present invention can be prokaryotic cells, such as E. coli, or eukaryotic cells such as yeast, plant, insect, amphibian, or mammalian cells. In general, host cells are filamentous fungi. The term “filamentous fungi" includes all filamentous fungi recognized by those of skill in the art.
- an “equivalent” amino acid sequence is an amino acid sequence that is not identical to an original reference amino acid sequence but includes some amino acid changes, which may be substitutions, deletions, additions or the like, wherein the protein exhibits essentially the'same qualitative biological activity of the reference protein.
- An equivalent amino acid sequence will have between 80% - 99% amino acid identity to the original reference sequence. Preferably the equivalent amino acid sequence will have at least 85%, 90%, 93%, 95%, 96%, 98% and 99% identity to the reference sequence.
- substitution results from the replacement of one or more nucleotides or amino acid by different nucleotides or amino acids, respectively.
- a "wild type fungal cellulase composition” is one produced by a naturally occurring fungal source and which comprises one or more BG, CBH and EG components wherein each of these components is found at the ratio produced by the fungal source.
- a naturally occurring cellulase system may be purified into substantially pure components by recognized separation techniques well published in the literature, including ion exchange chromatography at a suitable pH, affinity chromatography, size exclusion and the like.
- a purified cellulase fusion protein or components thereof may then be added to the enzymatic solution resulting in an enriched cellulase solution.
- heterologous exo-endo cellulase fusion construct or vector comprising a heterologous exo-endo cellulase fusion construct includes in operable linkage from the 5' end, a promoter of a filamentous fungus secretable protein; a DNA molecule encoding a signal sequence; a DNA molecule encoding a catalytic domain of an exo-cellobiohydrolase, optionally a DNA molecule encoding the exo-cellobiohydrolase CBD; a DNA molecule encoding a catalytic domain of an endoglucanase; and a terminator.
- nidulans gpdA or trpC genes the Neurospora crassa cbhl or trpl genes; the A. niger or Rhizomucor miehei aspartic proteinase encoding genes; the 7 " . reesei cbhl, cbh2, eg , egl2, or other cellulase encoding genes; a CMV promoter, an SV40 early promoter, an RSV promoter, an EF-1 ⁇ promoter, a promoter containing the tet responsive element (TRE) in the tet-on or tet-off system as described (ClonTech and BASF), the beta actin promoter.
- TRE tet responsive element
- the promoter is one that is native to the fungal host cell to be transformed.
- the promoter is an exo-cellobiohydrolase cbhl or cbhl promoter and particularly a cbhl promoter, such as a T. reesei cbhl promoter.
- the T. reesei cbhl promoter is an inducible promoter, and reference is made to GenBank Accession No. D86235.
- the DNA sequence encoding an exo-cellobiohydrolase catalytic domain is operably linked to a DNA sequence encoding a signal sequence.
- the signal sequence is preferably that which is naturally associated with the exo-cellobiohydrolase to be expressed.
- a heterologous exo-endo cellulase fusion construct or expression vector of the invention may include a cleavage site, such as a protease cleavage site.
- the cleavage site is a kexin site which encodes the dipeptide Lys-Arg.
- the heterologous exo-endo cellulase fusion construct and an expression vector including the same will lack the CBD of the CBH. In other embodiments the CBD will be included in the construct or vector.
- BLAST programs which can be used to determine identity between two sequences include, but are not limited to, the suite of BLAST programs, e.g., BLASTN, BLASTX, and TBLASTX, BLASTP and TBLASTN, publicly available on the Internet at www.ncbi.nlm.nih.gov/BLAST/. See also, Altschul, et al., 1990 and Altschul, et al., 1997.
- a preferred vector is the vector disclosed in Figures 12 and 13, wherein the vector includes the nucleic acid sequence encoding the CBD, linker and catalytic domain of the Thermobifida fusca endoglucanase 5 (SEQ ID NO: 12).
- a preferred vector is the vector disclosed in Figures 12 and 13, wherein the vector includes the nucleotide sequence encoding an Acidothermus cellulolyticus GH5A endoglucanase catalytic domain (SEQ ID NO: 8).
- a filamentous host cell strain such as a Trichoderma host cell strain which has had one or more cellulase genes deleted prior to introduction of a heterologous exo-endo cellulase fusion construct encompassed by the invention.
- Such strains may be prepared by the method disclosed in U.S. Patent No. 5,246,853, U.S. Patent 5,861 ,271 and WO 92/06209, which disclosures are hereby incorporated by reference.
- a cellulase fusion protein or components thereof having cellulolytic activity in a host microorganism that is missing one or more cellulase genes the identification and subsequent purification procedures are simplified. Any gene from Trichoderma sp.
- the proteins thereby produced may be purified from the cells or cell culture by methods known in the art and reference is made to Deutscher, Methods in Enzymology, vol. 182, no. 57, pp. 779, 1990; and Scopes, Methods Enzymol. 90: 479-91 , 1982.
- the fungal cells expressing a heterologous exo-endo cellulase fusion construct are grown under batch or continuous fermentation conditions.
- a classical batch fermentation is a closed system, wherein the composition of the medium is set at the beginning of the fermentation and is not subject to artificial alterations during the fermentation. Thus, at the beginning of the fermentation the medium is inoculated with the desired organism(s). In this method, fermentation is permitted to occur without the addition of any components to the system.
- a batch fermentation qualifies as a "batch" with respect to the addition of the carbon source and attempts are often made at controlling factors such as pH and oxygen concentration.
- the metabolite and biomass compositions of the batch system change constantly up to the time the fermentation is stopped.
- a detergent composition refers to a mixture which is intended for use in a wash medium for the laundering of soiled cellulose containing fabrics.
- CBH1-E1 T. reesei CBH1 catalytic domain and linker fused to an Acidothermus cellulolyticus GH5A endoglucanase I catalytic domain;
- CBH1-74E T. reesei CBH1 catalytic domain and linker fused to an Acidothermus cellulolyticus GH74 endoglucanase catalytic domain
- phthalate buffer (sodium phthalate in water, 20mN, pH 5.0); PBS (phosphate buffered saline [150 mM NaCI, 10 mM sodium phosphate buffer, pH 7.2]);SDS (sodium dodecyl sulfate); Tris (tris(hydroxymethyl)aminomethane); w/v
- Amplification Buffer 5 ⁇ l 10 x PCRx Enhancer Solution; 1 ⁇ l Platinum Pfx DNA Polymerase (2.5U total); 33 ⁇ l water for 50 ⁇ l total reaction volume.
- Amplification parameters were: step 1 - 94°C for 2 min (1st cycle only to denature antibody bound polymerase); step 2 - 94°C for 45 sec; step 3 - 60°C for 30 sec; step 4 - 68°C for 2 min; step 5 - repeated step 2 for 24 cycles and step 6 - 68°C for 4 min.
- the appropriately sized PCR product was cloned into the Zero Blunt TOPO vector and transformed into chemically competent Top10 E.
- coli cells (Invitrogen Corp., Carlsbad, CA) - plated onto to appropriate selection media (LA with 50 ppm with kanamycin and grown overnight at 37°C. Several colonies were picked from the plate media and grown overnight in 5 ml cultures at 37°C in selection media (LB with 50 ppm kanamycin) from which plasmid mini-preps were made. Plasmid DNA from several clones was restriction digested to confirm the correct size insert. The correct sequence was confirmed by DNA sequencing. Following sequence verification, the E1 catalytic domain was excised from the TOPO vector by digesting with the restriction enzymes Spel and Ascl.
- the mycelial pellet was transferred into a 250 ml, CA Corning bottle containing 40ml of B glucanase solution and incubated at 30°C, 200 rpm for 2 hrs to generate protoplasts for transformation.
- Protoplasts were harvested by filtration through sterile miracloth into a 50ml conical tube. They were pelleted by spinning at 2000 rpm for 5 minutes, the supernate was aspirated off.
- the protoplast pellet was washed once with 50ml of 1.2 M sorbitol, spun down, aspirated, and washed with 25ml of sorbitol CaCI 2 .
- EXAMPLE 3 Assay of Cellulolytic Activity from Transformed Trichoderma reesei Clones The following assays and substrates were used to determine the cellulolytic activity of the CBH1-E1 fusion protein.
- Pretreated corn stover (PCS) - Corn stover was pretreated with 2% w/w H 2 SO 4 as described in Schell, D. et al., J. Appl. Biochem. Biotechnol. 105:69 - 86 (2003) and followed by multiple washes with deionized water to obtain a pH of 4.5.
- Sodium acetate was added to make a final concentration of 50mM and this was titrated to pH 5.0.
- Transformation of the fusion vector into T.reesei was performed using biolistic transformation according to the teaching of Hazell, B. W. et al., Lett. Appl. Microbiol. 30:282-286 (2000).
- Expression of the CBH1-74E fusion protein was determined as described above for expression of the CBH1-E1 fusion protein in Example 2 .
- the highest level of cleaved GH74 protein expression from a transformant in shake flasks was estimated to be greater then 3 g/L.
- Shake flask grown supernatant samples were run on BIS-TRIS SDS -PAGE gels (Invitrogen), under reducing conditions with MOPS (morpholinepropanesulfonic acid) SDS running buffer and LDS sample buffer. The results are provided in Figure 15.
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Abstract
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Priority Applications (8)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN2005800090651A CN1934258B (en) | 2004-03-25 | 2005-03-25 | Exo-endo cellulase fusion protein |
EP05744496A EP1740700B1 (en) | 2004-03-25 | 2005-03-25 | Exo-endo cellulase fusion protein |
DK05744496T DK1740700T3 (en) | 2004-03-25 | 2005-03-25 | Exo-endo cellulase |
DE602005010997T DE602005010997D1 (en) | 2004-03-25 | 2005-03-25 | EXO-ENDO CELLULASE Fusion Protein |
JP2007505236A JP2007530050A (en) | 2004-03-25 | 2005-03-25 | Exo-endocellulase fusion construct |
BRPI0509171-3A BRPI0509171B1 (en) | 2004-03-25 | 2005-03-25 | EXO-ENDO CELLULASE FUSION PROTEIN |
CA2560593A CA2560593C (en) | 2004-03-25 | 2005-03-25 | Exo-endo cellulase fusion protein |
HK07110262.3A HK1105011A1 (en) | 2004-03-25 | 2007-09-20 | Exo-endo cellulase fusion protein |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
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US55659804P | 2004-03-25 | 2004-03-25 | |
US60/556,598 | 2004-03-25 |
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WO2005093073A1 true WO2005093073A1 (en) | 2005-10-06 |
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PCT/US2005/010158 WO2005093073A1 (en) | 2004-03-25 | 2005-03-25 | Exo-endo cellulase fusion protein |
Country Status (11)
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US (2) | US8097445B2 (en) |
EP (2) | EP1740700B1 (en) |
JP (1) | JP2007530050A (en) |
CN (1) | CN1934258B (en) |
AT (1) | ATE414158T1 (en) |
BR (1) | BRPI0509171B1 (en) |
CA (1) | CA2560593C (en) |
DE (1) | DE602005010997D1 (en) |
DK (1) | DK1740700T3 (en) |
HK (1) | HK1105011A1 (en) |
WO (1) | WO2005093073A1 (en) |
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CN1934258B (en) | 2011-12-14 |
ATE414158T1 (en) | 2008-11-15 |
BRPI0509171A (en) | 2007-08-28 |
EP1740700A1 (en) | 2007-01-10 |
HK1105011A1 (en) | 2008-02-01 |
JP2007530050A (en) | 2007-11-01 |
US20120135499A1 (en) | 2012-05-31 |
EP1740700B1 (en) | 2008-11-12 |
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BRPI0509171B1 (en) | 2018-02-06 |
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CN1934258A (en) | 2007-03-21 |
CA2560593A1 (en) | 2005-10-06 |
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US20060057672A1 (en) | 2006-03-16 |
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