A bacteria referred to here as Bacillus subtilis 6A-1 is provided, compositions thereof and processes for use of the bacteria, spores, cells, extracts and enzymes. The compositions which comprise the bacteria, spores, cells, extracts and/or enzymes are capable of degrading polysaccharides. Such compositions are capable of degrading cellulose, including plant-produced cellulose, microcrystalline cellulose and carboxymethyl cellulose. The bacteria produces at least two cellulose-degrading protein fractions. Cellulose degrading activity continues across pH2 to pH13.

Disclosed are soluble hybrid Fc receptor (FcR) polypeptide compositions and related methods of using such polypeptides to treat IgG-mediated and immune complex-mediated inflammation. Also disclosed are related compositions and methods for producing the soluble hybrid FcR polypeptides.

The present disclosure relates to an isolated anti-FcRn antibody, which is an antibody binding to FcRn (stands for neonatal Fc receptor, also called FcRP, FcRB or Brambell receptor) that is a receptor with a high affinity for IgG or a fragment thereof, a method of preparing thereof, a composition for treating autoimmune disease, which comprises the antibody, and a method of treating and diagnosing autoimmune diseases using the antibody. The FcRn-specific antibody according to the present disclosure binds to FcRn non-competitively with IgG to reduce serum pathogenic auto-antibody levels, and thus can be used for the treatment of autoimmune diseases.

The present invention relates to a cell culture method for adjusting the proportion of G0, G1, G2, and high-mannose galactosylation variants in a population of a recombinant protein produced by a culture of cells in a cell culture medium by supplementing the cell culture medium with manganese at one or more days of the cell culture method duration.

The present invention relates to a new isolated polypeptide comprising an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, 99% or 100% identity to the full length amino acid sequence set forth in SEQ ID NO:1, and having a polyester degrading activity, and uses thereof.

The inventive subject matter relates to the methods for the induction of immunity and prevention of diarrhea resulting from Escherichia coli. The inventive subject matter also relates to the use Escherichia coli adhesins as immunogens and to the construction of conformationally stability and protease resistant Escherichia coli adhesin constructs useful for inducing immunity to Escherichia coli pathogenic bacteria. The methods provide for the induction of B-cell mediated immunity and for the induction of antibody capable of inhibiting the adherence and colonization of Escherichia coli, including enterotoxigenic Escherichia coli, to human cells.

Mutated fucosidases are provided demonstrating improved properties in terms of thermal stability and transfucosidase synthetic performance compared with a wild type transfucosidase isolated from Bifidobacterium longum subsp. infantis.

Provided are a fungus-sourced high-temperature acid -glucosidase as well as a coding gene, and an application thereof. The provide -glucosidase has the optimal pH value of 4.5 and the optimal temperature of 75 C., and maintains over 90% enzyme activity in the optimal condition after being processed at 60 C. for 1 h. The re-engineering yeast strain GS115/bgl3A of the coding gene comprising the -glucosidase has high fermentation level.

Genetically encoded, photocleavable proteins are derived from a fluorescent protein. Upon illumination, the proteins photocleave and spontaneously dissociate into two or more fragments or release one end of an internal loop.

It relates to a LfliZ gene and its application. The sequence of gene LfliZ is shown in SEQ ID NO.1. This invention also relates to the recombinant protein LfliZ encoded by LfliZ gene and its application in preparation of 2, 3-cNMPs. The recombinant LfliZ protein encoded by gene LfliZ can bind four kinds of 2, 3-cNMPs during its expression in Escherichia coli. Four kinds of 2, 3-cNMPs can be prepared simultaneously from the recombinant E. coli by extracting the recombinant protein LfliZ. The yield of 2, 3-cNMPs reaches 2.5 mg/L fermentation broth by the method in the present invention, indicating that this method has a good application potential.