Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates

TL;DR: Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides were identified in silico within camel milk proteins as well as bovine milk proteins using a design of experiments and enzyme to substrate ratio.

TL;DR: The potential mechanisms of bioactive peptides on key enzymes and proteins, such as α‐amylase, α‐glucosidase, glucagon‐like peptides and dipeptidyl peptidase‐IV, that participate in glycaemic level control from the intake of carbohydrates to blood glucose regulation were overviewed.

TL;DR: In this paper, differences in protein degradation and peptide generation were studied for beta-lactoglobulin and alpha(S1)-casein from commercially available dairy products before, during, and after in vitro digestion.

TL;DR: Feather hydrolysates displayed in vitro antioxidant properties, and optimal antioxidant activities were observed in cultures with 50 g l(-1) feathers, at initial pH 8.0, after 48 hours growth at 30°C.

TL;DR: While proteins and peptides have excellent potential as food antioxidants, issues such as allergenicity and bitter off-flavors as well as their ability to alter food texture and color need to be addressed.

TL;DR: Control of hyperglycemia remains the best way to improve endothelial function and to prevent atherosclerosis and other cardiovascular complications of diabetes.

TL;DR: In this paper, the role of peptides derived from the digestion of milk proteins has been investigated and the results suggest that the hydrolysates from milk proteins could be used as natural antioxidants in enhancing antioxidant properties of functional foods.

TL;DR: This overview provides the latest developments about novel antioxidants, particularly phenolic derivatives, peptides/protein hydrolysates, phospholipids and polysaccharides, and their role in food quality preservation and human health promotion.