The present application relates to arenaviruses expressing prostate cancer-related antigens. In particular, described herein is a modified arenavirus particle which is engineered to carry a heterologous open reading frame (ORF) encoding a prostate cancer-related antigen or an antigenic fragment thereof, wherein the prostate cancer-related antigen is selected from the group consisting of: prostatic acid phosphatase (PAP), prostate specific antigen (PSA), and prostate-specific membrane antigen (PSMA). Also described herein are arenavius genome segments or S segments encoding the prostate cancer-related antigen or an antigenic fragment thereof, cDNA, DNA expression vector, a pharmaceutical composition comprising such an arenavirus particle, methods of generating such an arenavirus particle and treating prostate cancer using such an arenavirus particle, and a kit for such usage.

The present invention provides a recombinant strain, construction method thereof and a method for producing acid phosphatase using the recombinant strain. In the invention, the phosphatase gene is obtained from Pseudomonas aeruginosa by a molecular biology method, the constructed expression plasmid is transformed into E. coli BL21 (DE3). The purified enzyme and whole cells were used for the conversion of ascorbic acid to ascorbic acid-2-phosphate. Ascorbic acid-2-phosphate can be efficiently produced by controlling the ratio of substrates. When the conversion reaction is performed at pH 4.5 under 40 C. for 8 h, the output of ascorbic acid-2-phosphate reaches 54.8 g/L, the conversion is 42.9% and the space time yield is 6.9 g/L/h.

The purpose of the present invention is to provide a monoclonal antibody that is useful in specifically assaying tartrate resistant acid phosphatase 5b (TRACP-5b). A hybridoma producing a monoclonal antibody against TRACP-5b, said monoclonal antibody showing higher reactivity with TRACP-5b than with tartrate resistant acid phosphatase 5a (TRACP-5a) and, therefore, being specific to TRACP-5b, is obtained by cell fusion using, as an antigen, human recombinant TRACP-5b purified from silkworm silk gland. By using this monoclonal antibody, TRACP-5b in a specimen can be highly sensitively and specifically detected.

The application provides a polypeptide comprising the sequence SLMTNLAAL (SEQ ID NO: 8), Ser 13 to Leu 21 of amino acid sequence shown in FIG. 1 or SEQ ID No 1, and having HLA-A2 haplotype binding activity, or a polynucleotide encoding said polypeptide. Vaccines containing the polypeptide or polynucleotides encoding the polypeptide are also provided.

A method for enzymatic sulfurylation of a substrate is provided which includes the steps of reacting the substrate with 3-phosphoadenosine-5-phosphosulfate (PAPS) in a medium containing a bacterium belonging to the family Enterobacteriaceae to produce a sulfated derivative of the substrate, and collecting the sulfated derivative from the medium, wherein the bacterium has been modified to produce, at least, a protein having sulfotransferase activity, and to attenuate expression of an aphA gene, a cysQ gene, or a cpdB gene, or a combination of these.

Provided herein are methods, compositions, and non-naturally occurring microbial organism for preparing compounds such as1-butanol, butyric acid, succinic acid, 1,4-butanediol, 1-pentanol, pentanoic acid, glutaric acid, 1,5-pentanediol, 1-hexanol, hexanoic acid, adipic acid, 1,6-hexanediol, 6-hydroxy hexanoic acid, ?-Caprolactone, 6-amino-hexanoic acid, ?-Caprolactam, hexamethylenediamine, linear fatty acids and linear fatty alcohols that are between 7-25 carbons long, linear alkanes and linear ?-alkenes that are between 6-24 carbons long, sebacic acid and dodecanedioic acid comprising: a) converting a C.sub.N aldehyde and pyruvate to a C.sub.N+3 ?-hydroxyketone intermediate through an aldol addition; and b) converting the C.sub.N+3 ?-hydroxyketone intermediate to the compounds through enzymatic steps, or a combination of enzymatic and chemical steps.

A phytase having improved thermostability is disclosed. The phytase has a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is one of mutations A to D. The mutation A is to substitute amino acids at positions 143 and 262 with cysteine, the mutation B is to substitute amino acids at positions 259 and 312 with cysteine, the mutation C is to substitute amino acids at positions 205 and 257 with cysteine, and the mutation D is to substitute amino acids at positions 264 and 309 with cysteine.

The invention is directed to non-natural yeast able to secrete significant amounts of glucoamylase into a fermentation media. The glucoamylase can promote degradation of starch material generating glucose for fermentation to a desired bioproduct, such as ethanol. The glucoamylase can be provided in the form of a glucoamylase fusion protein having a S. cerevisiae mating factor alpha 2 (Sc MF2) or repressible acid phosphatase (Sc PHO5) secretion signal.

The present invention provides a recombinant strain, construction method thereof and a method for producing acid phosphatase using the recombinant strain. In the invention, the phosphatase gene is obtained from Pseudomonas aeruginosa by a molecular biology method, the constructed expression plasmid is transformed into E. coli BL21 (DE3). The purified enzyme and whole cells were used for the conversion of ascorbic acid to ascorbic acid-2-phosphate. Ascorbic acid-2-phosphate can be efficiently produced by controlling the ratio of substrates. When the conversion reaction is performed at pH4.5 under 40 C. for 8 h, the output of ascorbic acid-2-phosphate reaches 54.8 /L, the conversion is 42.9% and the space time yield is 6.9 g/L/h.

Provided herein, inter alia, are methods for improving the growth of cells (such as probiotic cells or recombinant cells) by culturing the cells in a liquid media comprising one or more enzymes that hydrolyze at least one nucleoside triphosphate present in the media. Cells cultured in accordance with these methods exhibit improved growth compared to cells cultured in media that does not comprise one or more enzymes that hydrolyze at least one nucleoside triphosphate.