150results about How to "Efficient secretion" patented technology

This invention relates to a novel protein having a lecithin-cholesterol acyltransferase-like activity, etc. or its salt, a precursor protein of the protein or its salt, a partial peptide of the protein or its salt; a DNA coding for the protein; a recombinant vector; a transformant; a method for producing the protein, a pharmaceutical composition comprising the protein, the partial peptide or its salt; and an antibody to the protein or the partial peptide. The protein, the partial peptide or its salt, and the DNA are useful as an agent for treating or preventing arteriosclerosis, atherosclerosis, hyperlipidemia, hypercalorism, obesity or hypertriglyceridemia. The antibody can be used in assay of the protein, the partial peptide or its salt. The protein, the partial peptide or its salt is useful as a reagent for the screening for candidate medical compounds.

The present invention relates generally to the use of recombinant adeno-associated viruses (rAAV) for gene delivery and more specifically to the use of rAAV to deliver antibody genes to target cells in mammals. Administration of rAAV encoding antibodies that neutralize the HIV-1 virus is exemplified.

A high temperature alpha-amylase and a high efficiency preparation method of the mutant thereof belongs to the fermentation engineering field. The invention provides a method for high efficiently secreting expressing a high temperature alpha-amylase and mutant thereof with alpha-amylase activity through a bacillus, especially a bacillus licheniformis mutant strain as a host cell. The synthesis and secretion level of the high temperature alpha-amylase or mutant thereof of the recombinant strain of the invention reaches 18-25mg/mL during fed-batch fermentation and is 3-4.5 times of the original strain high temperature alpha-amylase synthesis level. The high temperature alpha-amylase of the invention is useful for reducing the fermentation manufacture cost of the industrial enzyme, simplifying the fermentation manufacture process and reducing fermentation industrial environment pressure.

Provided are means for evaluating and identifying putative substrates of the twin arginine translocation (Tat) secretory pathway in Streptomyces and other bacterial species. Also provided, therefore, are simple ways to express, secrete and purify correctly folded heterologous proteins on a large scale using host microorganisms, such as, Streptomyces and the Tat pathway therein. Many of the thus-produced proteins are of significant therapeutic value in the pharmaceutical and biochemical industries, particularly when they can be secreted from the host in fully-folded active form. Accordingly, there are further provided the heterologous proteins produced by the Tat secretion pathway using the foregoing methods, and the computer algorithm used to identify the Tat signal sequence and putative substrates.

The invention provides alginate lyase, host cells capable of secreting alginate lyase and application of the alginate lyase and the host cells. The alginate lyase has any one of amino acid sequences shown as (I) and (II): (I) an amino acid sequence shown as SEQ ID NO. 1; (II) an amino acid sequence obtained by carrying out substitution, deletion or addition of 1 to 20 amino acid residues on the amino acid sequence shown as SEQ ID NO. 1; the obtained amino acid sequence has the activity of the alginate lyase. According to the alginate lyase, whole genes of the alginate lyase are truncated to reduce the molecular weight, so that the expression amount of the host cells on the alginate lyase is remarkably improved; the secreted alginate lyase has high activity, good stability and strong degradation capability on sodium alginate.

The invention relates to the field of genetic engineering and the field of protein secretion expression and provides a method for constructing a pichia pastoris engineered strain used for preparing dextranase. The method comprises the following steps: (1) designing an oligonucleotides primer and taking lipomyces 1390 genome DNA as a template; cloning to obtain dextranase genes; (2) utilizing a secretion expression carrier pPIC9K to insert the dextranase genes into multi-cloning sites (EcoRI and NotI) of the pPIC9K so as to construct an integral secretion-type expression carrier pPIC9K-139; and(3) linearizing the reconstructed expression carrier pPIC9K-139 so as to realize the high-efficiency secretion expression of the dextranase, and obtaining the reconstructed pichia pastoris engineeredstrain GS115-139 by means of selection. The method successfully realizing the effective expression of the dextranase genes in pichia pastoris, constructs the engineered strain which can efficiently secrete and express the dextranase, and realizes the expansion of a fermentation process of the dextranase.

The present invention is directed to a recombinant E. coli Nissle 1917 (EcN) cell transformed with a nucleic acid coding for a defensin protein or a derivative thereof. The invention is further directed to a pharmaceutical composition comprising this cell and a pharmaceutically acceptable carrier as well as a method of producing a recombinant E. coli Nissle 1917 cell and its use in the treatment of Crohn's disease.

The invention discloses a lignin biological resource utilization method. According to the method, lignin can serve as a fermentation auxiliary substrate, continuous high-density culture is implemented, and the lignin can be degraded into substances such as acetic acid, vanillin, guaiacol, veratryl alcohol and phenolic compounds by fungal complex floras. The lignin can be applied to the fungal complex floras and mass efficient production of active substances of the fungal complex floras. Culture conditions and culture medium components of the fungal complex floras are optimized, the biodegradation rate and the conversion efficiency of the lignin are improved, so that the degradation rate of the lignin is not lower than 40%, and the concentration of a degradation product is 10-100mg/L. An efficient resource utilization method is provided for degradation and conversion of the lignin.

The invention relates to a lactococcus lactis food-level double-screening marker secretory expression vector and a construction method thereof. The vector comprises a melA gene, a nisI fused gene double selection marker containing a P32 promoter, a replicor of a plasmid pWV01, a multiple cloning site, a P32 promoter for secretory expression and a part of sequence of enterococcus faecalis Usp45 secretory protein. The invention also discloses an application of NN1-1 as an exogenous protein expression vector, including recombinant lactococcus lactis of endoglucanase (end-1) constructed for secretory expression of fibrobacter succinogenes with NN1-1 as a vector.

The invention provides construction of TRAIL (Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand) recombinant bacille calmette guerin (rBCG), and relates to a shuttle expression vector comprising a signal peptide fragment of a major secretory antigen Ag85B of BCG and a gene fragment of a TRAIL and a construction method thereof. The obtained shuttle expression vector pMV261-Ag85B-TRAIL is used for constructing rBCGTRAIL, and can be applied to preparation of TRAIL rBCG for treating superficial bladder tumors, preventing postoperative recurrence thereof and preventing tuberculosis. The rBCG has dual functions of TRAIL and BCG, so that cooperative and synergistic actions of the TRAIL and BCG can be better brought into play; rBCG-TRAIL can secrete TRAIL, and the using amount of the rBCG-TRAIL can be lower than that of the BCG under the condition that the same or better immune effect is achieved, so that the toxic or side effect is reduced; and the rBCG-TRAIL can directly secrete TRAIL efficiently on a certain part, so that tumor cells can be killed in cooperation with the rBCG-TRAIL, and high cost caused by the use of a foreign cell factor is avoided.