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At the Nippi Research Institute of Biomatrix, we are focusing not only on product development but also on fundamental collagen research. Post-translational modification of collagen is one of our very important themes. Proteins are synthesized by combining 20 types of amino acids based on genetic information (translation); not only that, but by modifying amino acids, new functions are created, or the functions are reduced. Collagen is a protein that has great potential for improved functionality through such modifications. Nippi has reported several research results on collagen hydroxylation, glycosylation,
cross-linking and glycation.
In studies of amino acids, modified collagen is often decomposed to some extent before analysis. For the research, the enzyme protease that decomposes collagen according to a fixed rule is an important tool. While researching proteases at the Nippi Research Institute of Biomatrix, Nippi focused on two proteases that act on collagen. One is gingipain, a collagenase produced by periodontal disease bacteria, which does harm by breaking down collagen in the gums. The other is zingibain, which is a major collagenase contained in ginger. These two enzymes are similar in that they break down collagen, but their properties and origins are completely different. While investigating the structure and properties of the degraded peptides after these two enzymes act on collagen, we found that ginger-originated zingibain produces peptides with unique characteristics. This is when we started to develop a new peptide product by applying zingibain.
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