67 results about "Clostridium organisms" patented technology

The present invention relates generally to the 18-membered macrocyclic antimicrobial agents called Tiacumicins, specifically, OPT-80 (which is composed almost entirely of the R-Tiacumicin B), pharmaceutical compositions comprising OPT-80, and methods using OPT-80. In particular, this compound is a potent drug for the treatment of bacterial infections, specifically C. difficile infections.

The invention relates to a method for a tetanus toxin receptor binding domain Hc to be subjected to high-level soluble expression in Escherichia coli through nucleotide sequence optimization. According to the sequencing result of a domestic C.Tetani virulent strain CMCC64008, the tetanus toxin receptor binding domain Hc sequence is analyzed and optimized, the optimized sequence is SEQ ID No.1 and the coded protein sequence is SEQ ID No.2. The synthesized Hc gene is linked into an expression vector pET32a(+) after undergoing double enzyme digestion, the recombinant Hc is subjected to high soluble expression in Escherichia coli and the target protein accounts for about 46% of the total protein in the supernatant undergoing bacteriociasis. After QFF column purification, phenyl hydrophobic column purification and SP column purification, the purity of the target protein can be more than 95% and the yield thereof is more than 300mg / L. The recombinant protein prepared by the method of the invention has good immunogenicity, can induce the mice to produce high-titre protective antibodies and can resist attack of high-dose lethal toxins. The method has extensive application prospect in large-scale high-level preparation of the tetanus toxin recombinant subunit vaccine Hc.

The invention relates to HSDH (hydroxysteroid dehydrogenase), in particular to a gene S1-a-1 of novel 7 alpha-HSDH. A nucleotide sequence of the gene is shown as SEQ ID NO.2, the novel 7 alpha-HSDH is encoded, a nucleotide sequence of the novel 7 alpha-HSDH is shown as SEQ ID NO.1, the novel 7 alpha-HSDH can be used for catalyzing CDCA (chenodeoxycholic acid) and TCDCA (taurochenodeoxycholic acid) to generate 7K-LCA (7-ketone lithocholic acid) and T7K-LCA (taurine-7-ketone lithocholic acid), wherein the catalytic activity of the novel 7 alpha-HSDH for CDCA is about 5 times of that of 7 alpha-HSDH of Sardinia clostridium, and the catalytic activity of the novel 7 alpha-HSDH for TCDCA is about over 2.5 times of that of 7 alpha-HSDH of Sardinia clostridium, therefore, the novel 7 alpha-HSDH has a great industrial application value.

A fixable oxycarbide and a microorganism capable of performing fermentation reaction and a preparation method and application thereof are characterized in that the preparation method includes: (a) providing a first parental generation bacterial strain capable of fixing the oxycarbide; (b) providing a second parental generation bacterial strain capable of performing the fermentation reaction; (c) respectively preparing the first parental generation bacterial strain and the second parental generation bacterial strain into a first protoplast and a second protoplast; (d) fusing the first protoplast and the second protoplast so as to provide a fused bacterial strain; and (e) cultivating the fused bacterial strain so as to obtain an object bacterial strain which can be used for producing organic compounds (such as organic acids and alcohols). A specific sample of the object bacterial strain is Colstridium tyrobutyricum strian ITRI02001 and is stored in Deutsche Sammlung von Mikroorganismen und Zellkulturen (DSMZ). The storage number is DSM 32077.

The invention discloses recombinant alpha protein for inhibiting clostridium perfringens infection and a preparation method and application thereof. The recombinant alpha protein is shown in (a) or (b) or (c), wherein the protein in (a) is composed of amino acid sequences shown as SEQ ID No.2; the protein in (b) is composed of amino acid sequences shown at the sites No.51-No.353 of SEQ ID No.2; the fusion protein in (c) is obtained by fusing protein tags at carboxyl terminals or / and amino terminals of the protein shown in (a) or (b). The recombinant alpha protein enables animals to have a higher serum antibody level and resist attack of clostridium perfringens after the animals are immunized with the recombinant alpha protein. The recombinant alpha protein is good in solubility and easy to purify and can serve as a diagnostic antigen to be prepared into a monoclonal antibody or be used for further research on protein functions and conformation relations.

The present invention provides a method for the biological production of n-butanol at high yield from a fermentable carbon source. In one aspect of the present invention, a process for the conversion of glucose to n-butanol is achieved by the use of a recombinant organism comprising a host C. acetobutlicum transformed i) to eliminate the butyrate pathway ii) to eliminate the acetone pathway iii) to eliminate the lactate pathway and iv) to eliminate the acetate pathway. In another aspect of the present invention, the hydrogen flux is decreased and the reducing power redirected to n-butanol production by attenuating the expression of the hydrogenase gene. Optionally the n-butanol produced can be eliminated during the fermentation by gas striping and further purified by distillation.