The present disclosure is directed to a lysin-AMP polypeptide construct comprising: (a) a first component comprising the polypeptide sequence of: (i) SEQ ID NO: 118 (GN202); or (ii) a polypeptide having lysin activity and having at least 80% sequence identity with the polypeptide sequence of SEQ ID NO: 118 (GN202); or (iii) an active fragment of SEQ ID NO: 118 (GN202); and (b) a second component comprising the polypeptide sequence of at least one antimicrobial peptide (AMP), wherein the at least one AMP comprises SEQ ID NO: 114 (FIRL). Exemplary lysin-AMP polypeptides, such as GN370 (SEQ ID NO: 44) as well as methods of treating bacterial infections using the present lysin-AMP polypeptide constructs are also disclosed.

Disclosed herein are stability-enhanced formulations that comprise a therapeutic protein and a stability-improving amount of a stabilizing excipient, wherein the stabilized-enhanced formulation is characterized by an improved stability parameter in comparison to a control formulation otherwise identical to the stability-enhanced formulation but lacking the stabilizing excipient. Further disclosed herein are methods of improving stability of therapeutic formulations or improving parameters of protein-related processes.

Crystal nucleation, and associated articles, systems, and methods, are generally described.

Disclosed is a method for recovering a desired fermentation product from a fermentation broth where the desired product has precipitated during the fermentation.

The present invention relates to a polynucleotide variant encoding a glycosyltransferase variant, and to nucleic acid constructs, vectors and host cells comprising said polynucleotide variant. The invention also relates to methods of producing a polypeptide of interest in host cells comprising said polynucleotide and/or glycosyltransferase variant.

A method of improving protein functionality includes obtaining a protein such as protein contained within exclusion bodies contained within bacteria or yeast used for the recombinant expression of the protein. The exclusion bodies are solubilized using a chaotropic agent such as guanidine or urea. The protein is then subject to denaturation conditions and optionally purified. A liquid containing the denatured protein is loaded into a vessel that is angled relative to horizontal. The vessel is then rotated in the angled configuration at a rate within that is less than 10,000 RPM for period of time. Refolded protein is formed by the high shear conditions formed in the thin film of fluid formed in the inner surface of the rotating vessel. Refolding can be performed in a batch mode or a continuous mode. The process may be scaled up for industrial applications by using multiple vessels.

The present invention relates to animal feed compositions comprising polypeptides having lysozyme activity and polypeptides having phytase activity and uses thereof.

Provided are methods for linking polypeptides (including peptides and proteins) to other moieties using radical imitated thiol-ene chemistries, for example, modifying a polypeptide by introducing reactive thiol groups and reacting the thiol groups with olefin-containing reagents or alkyne-containing reagents under conditions that support radical thiol-ene or thiol-yne reactions. The reactive thiol groups have greater activity for radical thiol-ene reactions that a cysteine thiol group, including thiol groups that are separated from the peptide backbone by at least two carbon atoms, for example, the thiol group of a homocysteine residue. Also provided are compositions and biomaterials containing the linked polypeptides, for example, peptide and protein conjugates, and thiol-ene based biocompatible hydrogel polymers, and their uses in the medical field.

The present invention relates to methods of improving digestibility in ruminants using ruminant feed comprising polypeptides having muramidase activity

The present invention relates to animal feed compositions comprising polypeptides having muramidase activity and polypeptides having xylanase activity and uses thereof.