Collagen peptides are small
protein fragments derived from collagen, a structural protein found in the
skin, bones, and connective tissues of animals. The preparation of collagen peptides
involves breaking down the collagen into smaller peptides using various
techniques. These techniques include chemical methods, enzymatic methods,
thermal degradation methods, and the combined application of these methods. The
molecular weight ranges of collagen peptides prepared by different technologies
vary greatly.
One of the earliest
techniques used for the preparation of collagen peptides is the
second-generation biological enzymatic hydrolysis method. This method involves
using animal skin and bone as raw materials and hydrolyzing the collagen into
small peptides under the catalysis of biological enzymes. The reaction
conditions are mild and no harmful by-products are generated during the
production process. However, the molecular weight distribution of the
hydrolyzed peptides is wide and uneven. Before 2010, this method was widely
used in the field of collagen peptide preparation.
The third-generation
preparation technology involves combining biological enzymatic hydrolysis with
membrane separation methods. Using animal skin, bone, etc. as raw materials,
collagen is hydrolyzed into small peptides under the catalysis of proteolytic
enzymes. The molecular weight distribution is then controlled by membrane
filtration. The reaction conditions are mild and no harmful by-products are
generated during the production process. Additionally, the molecular weight of
the product polypeptide has a narrow distribution and controllable molecular
weight. This technology has been applied in succession around 2015.
The fourth-generation
preparation technology involves separating peptide preparation by collagen
extraction and enzymatic hydrolysis. Based on research into the thermal
stability of collagen, the collagen is extracted near its critical thermal
denaturation temperature. The extracted collagen is then hydrolyzed with
biological enzymes and the molecular weight distribution is controlled by
membrane filtration. This method allows for greater control over the molecular
weight distribution of the resulting peptides.
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