Gelatin (Hydrolyzed Collagen)
Hydrolyzed collagen and proteins, which are the constituents of gelatins, have been used in cooking for over 100 years and have been known for their ability to strengthen fingernails and improve hair condition. Knox gelatin was the earliest commercial gelatin used as a food product.
Hydrolyzed collagen is produced from bone and cartilage. Typically, the bone is crushed or ground, defatted, soaked in hydrochloric acid to remove the calcium, soaked in alkali (sodium hydroxide) to break the bonds in the collagen, and then dehydrated. The resulting end product is the dry powder that can be reconstituted into gelatin.
Hydrolyzed collagen is still used as a gelatin food product. It is also used in making the capsule coating for many of today's medicines.
Gelatin improves nail and hair quality and stimulates their growth.
Please note that this section reports on claims that have NOT yet been substantiated through scientific studies.
Hydrolyzed collagen is claimed to possibly protect the body's lean muscle mass, improve the symptoms of arthritis, encourage the body to burn fat rather than protein and carbohydrates and thus encourage weight loss.
Hydrolyzed collagen is a foodstuff, an edible product derived from animal proteins, and can be eaten in amounts consistent with a normal daily protein intake.
Women who are pregnant or breast-feeding should consult a physician before taking any dietary supplements.
There are no known side effects associated with hydrolyzed collagen as an edible product.
Topical application, as used in skin and hair care products such as shampoo, can cause contact dermatitis in sensitive individuals.
There are no known significant food or drug interactions.
Hydrolyzed collagen consists of degraded animal protein. The protein is broken down into peptides (short chains of amino acids) and free amino acids. When ingested, the peptides are further broken down into free amino acids. Amino acids then become the building blocks for protein in the body.
Gelatin however, is an incomplete protein. Four amino acids -- glycine, proline, hydroxyproline, and glutamic acid -- typically constitute approximately 70 percent of the amino acid content of gelatin. Tryptophan is essentially absent, with hydroxylysine, methionine, histidine, tyrosine, and cystine making up less than one percent each of the amino acid content.
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