Abstract
Angiotensin Converting Enzyme Inhibition with Antiradicalar Activity of Thornback Ray Gelatin Hydrolysate: Determination and Separation of Peptide Fractions
Highlights
Several fish processing by-products, that are usually eliminated as organic wastes, causing environmental problem, may contain high-quality functional compounds, such as collagen
The aim of the present work was to separate the Thornback Ray Gelatin Hydrolysate (TRGH)-Alcalase by gel filtration and Reverse-Phase (RP) HPLC into fractions that differ in hydrophobicity followed by measurement of their antioxidant and Angiotensin Converting Enzyme (ACE) inhibition activities
Preparation and characterization of hydrolysate from thornback ray skin gelatin The enzymatic hydrolysis of proteins is an efficient method for producing peptides containing improved nutritional properties and bioactivities [25]
Summary
Several fish processing by-products, that are usually eliminated as organic wastes, causing environmental problem, may contain high-quality functional compounds, such as collagen. The nutritional and medical benefits of these compounds suggest that they could be used, after processing, as ingredients in functional foods [1]. Much attention has been focused on the identification and characterization of the structure, composition and, sequence of bioactive peptides. Active peptides play an important role in metabolic regulation and modulation. These peptides can be used as functional food ingredients, or nutraceuticals and pharmaceuticals to improve human health and prevent disease. The importance of fish as a source of novel bioactive substances is growing rapidly [2]
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