Provided herein are compositions and methods for producing milk proteins in plants, which allow for safe, sustainable and humane production of milk proteins for commercial use, such as use in food compositions. The disclosure provides recombinant fusion proteins comprising a milk protein, or fragment thereof and a structured mammalian, avian, plant, or fungal protein, or fragment thereof. The disclosure also provides methods for producing the recombinant fusions proteins, and food compositions comprising the same.

The present invention features compositions and methods for editing deleterious mutations associated with hemoglobinopathies, such as sickle cell disease (SCD). In particular embodiments, the invention provides methods for correcting mutations in a beta globin polynucleotide using modified adenosine base editors termed “ABE8” having unprecedented levels (e.g., >60-70%) of efficiency.

Provided herein are compositions and methods for producing milk proteins in plants, which allow for safe, sustainable and humane production of milk proteins for commercial use, such as use in food compositions. The disclosure provides recombinant fusion proteins comprising a milk protein, or fragment thereof and a structured mammalian, avian, plant, or fungal protein, or fragment thereof. The disclosure also provides methods for producing the recombinant fusions proteins, and food compositions comprising the same.

According to one aspect, the present disclosure provides a method of identifying a substrate of a transglutaminase using a peptide array comprising a plurality of peptides. The method includes the steps of contacting the peptides in the peptide array with the transglutaminase, allowing the transglutaminase to bind to the peptides, and identifying the substrate of the transglutaminase.

Disclosed herein are methods and compositions for targeted cleavage of a genomic sequence, targeted alteration of a genomic sequence, and targeted recombination between a genomic region and an exogenous polynucleotide homologous to the genomic region. The compositions include fusion proteins comprising a cleavage domain (or cleavage half-domain) and an engineered zinc finger domain and polynucleotides encoding same. Methods for targeted cleavage include introduction of such fusion proteins, or polynucleotides encoding same, into a cell. Methods for targeted recombination additionally include introduction of an exogenous polynucleotide homologous to a genomic region into cells comprising the disclosed fusion proteins.

Systems and methods for purification and concentration of autologous alpha-2 macroglobulin (A2M) from whole blood and or recombinant A2M are provided. Also provided are methods of treating wounds with A2M. Methods for utilizing A2M in combination with other treatments (e.g., platelets and other growth factors) are provided in addition to combinations with exogenous drugs or carriers. Also provided is a method of producing recombinant A2M wild type or variants thereof where the bait region was modified to enhance the inhibition characteristics of A2M and/or to prolong the half-life of the protein for treating wounds.

Provided are methods for producing food products comprising recombinant components, and compositions used in and food products produced by such methods.

The present invention relates to a method for providing an alpha-lactalbumin fraction and a beta-lactoglobulin fraction from a whey material obtained from milk, the method comprising the steps of: (i) providing the whey material; (ii) contacting the whey material with a chromatographic support allowing beta-lactoglobulin to be retained by the chromatographic support; (iii) obtaining a permeate fraction from the chromatographic support comprising the alpha-lactalbumin fraction; (iv) optionally washing the chromatographic support; and (v) obtaining a retentate fraction from the chromatographic support comprising the beta-lactoglobulin fraction; wherein the whey material provided in step (i) has been depleted, or substantially depleted from at least one whey protein, such as at least 2 whey proteins, e.g. at least 3 whey proteins.

A biodegradable hydrogel has been made based on high concentrations of whey protein isolate (WPI). WPI gels of different compositions were fabricated by thermally inducing gelation of high-concentration suspensions of protein, and characterized for compressive strength and modulus, hydration swelling and drying properties, mechanical behavior change due to polysaccharide additives, and intrinsic pore network structure. The gels were shown to be compatible with bone cells and could be used as bone tissue scaffolds. In addition, WPI fibers were produced by electrospinning. Several additives could be incorporated into the WPI gels, including structural additives, growth factors, amino acids, etc. The WPI hydrogels can be made with glycerol to increase flexibility and stability. The hydrogels could be used for tissue regeneration, food protection, controlled-release applications (including drug encapsulation, dietary supplement release, attractant release in lures, nutrient release to plants (fertilizers), column packing for compound separation, and membrane development.

A method for screening host cells expressing a target protein is provided. The method includes the following steps: providing an expression vector, the expression vector including a promoter, a gene encoding a target protein and an FTH1 gene; transfecting the host cells with the expression vector; culturing the host cells in a medium; and adding iron ions to the medium, and screening the surviving host cells to obtain the host cells expressing the target protein. An expression vector and a method for establishing a cell line stably expressing an exogenous recombinant gene are also provided.