Antioxidant peptides

Characterization of antioxidant and angiotensin-converting enzyme inhibitory peptides derived from cauliflower by-products by multidimensional liquid chromatography and bioinformatics

In the present paper, bioactive peptides from cauliflower by-products (leaves and stems) were investigated. Alcalase® protein hydrolysis time and pH conditions were optimized, then the hydrolysates were fractionated by preparative RP-HPLC into 12 fractions. Each fraction was tested for the ABTS (2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)), and DPPH (2,2-diphenyl-1-picrylhydrazyl) radical scavenging activity and for ACE (angiotensin-converting enzyme) inhibitor activity.

Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in tetradesmus obliquus microalgae

Microalgae are unicellular marine organisms that have promoted complex biochemical pathways to survive in greatly competitive marine environments. They could contain significant amounts of high-quality proteins which, because of their structural diversity, contain a range of yet undiscovered novel bioactive peptides. In this work, a peptidomic platform was developed for the separation and identification of bioactive peptides in protein hydrolysates.

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