Disclosed herein are methods for efficiently isolating collagen form a collagen source. The methods are inexpensive and do not require the use of proteolytic enzymes, decolorizing agents, antibacterial and antifungal agents, and the like. Further, the collagen produced by the methods described herein is substantially free of odor and discoloration. Still further, the collagen produced by the methods described herein is suitable to be used in cosmetics, food products, and pharmaceuticals or nutritional supplements.

The present invention relates to a composition comprising elastin, said composition having an improved oil and water binding capacity and improved emulsification properties. The composition of the present invention is specifically suitable for use in food and pet food applications as protein supplement or as replacement of specific texturizing ingredients.

The present invention relates to a composition comprising elastin, said composition having an improved oil and water binding capacity and improved emulsification properties. The composition of the present invention is specifically suitable for use in food and pet food applications as protein supplement or as replacement of specific texturizing ingredients.

A turkey collagen hydrolysate composition is prepared from turkey collagen sources, wherein the composition has: a protein concentration of from about 80 wt % to 100 wt %; a protein molecular weight distribution wherein from about 80% to 100% of the protein in the turkey collagen hydrolysate composition has a molecular weight of from about 500 to about 15,000 Daltons; a protein solubility of from about 97% to 100% at a pH selected from the group consisting of pH 7.0, pH 3.4, pH 5, and all of pH 7.0, pH 5, and pH 3.4; and a protein amino acid content of 3 to 25 glycine (g/100 g sample), 0.5 to 15 hydroxyproline (g/100 g sample), 1 to 18 proline (g/100 g sample), 0.02 to 4 taurine (g/100 g sample), and 0.05 to 3 tryptophan (g/100 g sample). Methods of preparing turkey collagen hydrolysate compositions are described.

The present invention provides methods for extraction of amino acid-rich fractions from keratin-containing biological materials, and to amino acid-rich protein fractions generated by the methods described herein. The methods involve forming a reaction mixture with keratin containing material at a pH of 1.1 to 6.9. The reaction mixture is exposed to an energy source, such as microwaves, sufficient to degrade the keratin. The amino acid mixture which is subsequently extracted is substantially insoluble.

The present invention provides methods for extraction of amino acid-rich fractions from keratin-containing biological materials, and to amino acid-rich protein fractions generated by the methods described herein. The methods involve forming a reaction mixture with keratin containing material at a pH of 1.1 to 6.9. The reaction mixture is exposed to an energy source, such as microwaves, sufficient to degrade the keratin. The amino acid mixture which is subsequently extracted is substantially insoluble.

Disclosed is a method for manufacturing compounds of interest from at least one mineralized connective tissue, the compounds of interest including at least collagen. The manufacturing method includes a solid/liquid extraction step in which the at least one mineralized connective tissue is mixed with an eluent suitable for extracting the compounds of interest from the at least one mineralized connective tissue to the eluent. This extraction step includes successive operations of adjusting the pH of the eluent, separated by a time interval; each of which pH adjustment operations includes an addition of an acid in the mineralized connective tissue/eluent mixture, to reduce the pH of the eluent until reaching a pH value lower than or equal to 5.5, preferably lower than or equal to 4, preferably ranging from 2 to 4.

Disclosed is a method for manufacturing compounds of interest from at least one mineralized connective tissue, the compounds of interest including at least collagen. The manufacturing method includes a solid/liquid extraction step in which the at least one mineralized connective tissue is mixed with an eluent suitable for extracting the compounds of interest from the at least one mineralized connective tissue to the eluent. This extraction step includes successive operations of adjusting the pH of the eluent, separated by a time interval; each of which pH adjustment operations includes an addition of an acid in the mineralized connective tissue/eluent mixture, to reduce the pH of the eluent until reaching a pH value lower than or equal to 5.5, preferably lower than or equal to 4, preferably ranging from 2 to 4.

A keratin hydrolysate including at least 94% by weight of free amino acids relative to the total weight of the amino acids of the hydrolysate. The keratin hydrolysate includes at least 93% of free valine relative to the total weight of valine in the hydrolysate, at least 90% free isoleucine relative to the total weight of isoleucine in the hydrolysate, and at least 95% of free leucine relative to the total weight of leucine in the hydrolysate. A method for producing the keratin hydrolysate, a composition comprising the hydrolysate and an animal feed containing the hydrolysate are also disclosed.

The method of the invention comprises the production of highly digestible hydrolysed keratinaceous material comprising the steps of (i) partly hydrolysing keratinaceous material with heat and pressure and (ii) optionally drying the resultant partly hydrolysed material comprising at least partly insoluble material and (iii) subjecting the optionally dried partly hydrolysed keratinaceous material to a chemical hydrolysis step with acid or base to obtain a highly digestible hydrolysed material, and (iv) purifying the highly digestible material. The invention further provides highly digestible keratinaceous material with an amino acid composition reflecting the amino acid composition of the raw material, wherein the amount of de-carboxylated amino acids is less than 500 ppm. Preferably all of the highly digestible material has a molecular weight lower than 10000 dalton, and preferably more than 95 wt % of the highly digestible keratinaceous material has a molecular weight of less than 5000 dalton.