Collagen is made from many sources which are bovine hide, bone, pigskin or fish bones and fish skin. The alternative from bovine or porcine is marine sources and they are not associated with the prisons related to risk of Bovine Spongiform Encefalopathy. The manufacturing of collagen hydrolysates is in controlled hydrolysis process to obtain soluble peptides. Washing, homogenizing and demineralizing the raw material with diluted mineral acid or alkaline. The raw material is extracted in several stages with warm water. Further enzymatic degradation of gelatin results in a final product which is collagen hydrolysate. Enzymatic hydrolysis is the most appropriate method for preparation of tailor-made peptides. Ultra filtration is the most efficient procedure to remove residual high-molecular weight peptides and proteins or to reduce the antigen content of hypoallergenic formulas.
Several analysis for the quality controlled of collagen are the osmolarity, analysis of the hydrolysis degree, the molecular weight distribution, the total nitrogen, amino acid composition and the presence of toxic compounds. But for protein hydrolysate qualitative analysis use different techniques based on spectrophotometric, chromatographic and
electrophoretic methods.