Customization: | Available |
---|---|
CAS No.: | 54249-88-6 |
Formula: | N/a |
Still deciding? Get samples of US$ 50/Piece
Request Sample
|
Suppliers with verified business licenses
Audited by an independent third-party inspection agency
DPP IV (Dipepty Peptidase IV) CAS 54249-88-6 Food Additives Nutrition
Dipeptidyl Peptidase IV (DPP-IV) is a serine exopeptidase that plays a crucial role in glucose homeostasis by degrading incretin hormones such as glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP) . This enzyme is a therapeutic target for type 2 diabetes, and its inhibition can improve postprandial hyperglycemia by increasing the levels of these hormones, which in turn stimulates insulin secretion from the pancreas .
DPP-IV is a type II transmembrane glycoprotein and a member of the S9 family of prolyl oligopeptidases. It is synthesized as a precursor with a signal peptide that serves as a membrane anchoring domain. The enzyme is highly expressed on endothelial cells, epithelial cells, and lymphocytes, and it is also present in a soluble form in plasma .
In the context of food additives, DPP-IV inhibitory peptides have been derived from various food sources, including milk, fish, eggs, and plants, through enzymatic hydrolysis. These peptides have the potential to serve as natural and functional food ingredients for glycemic regulation . The bioavailability and hypoglycemic effects of these peptides are of particular interest, as they could provide a natural alternative to synthetic DPP-IV inhibitors used in diabetes treatment .
The production of DPP-IV inhibitory peptides typically involves enzymatic hydrolysis of food proteins, followed by separation and identification of the active peptides. Structure-activity relationship (SAR) studies have shown that peptides with proline or alanine at the second position of the N-terminus exhibit strong DPP-IV inhibitory activity . These peptides must be stable in the gastrointestinal tract and have good cellular permeability to be effective as glycemic regulators