Antioxidant and angiotensin I-converting enzyme (ACE) inhibitory peptides of rainbow trout (Oncorhynchus mykiss) viscera hydrolysates subjected to simulated gastrointestinal digestion and intestinal absorption

نویسندگان

چکیده

The objective of this work was to evaluate in vitro bioaccessibility, intestinal absorption, antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities peptides from rainbow trout viscera hydrolysate (H). Rainbow Viscera (V) hydrolyzed by Alcalase® 2.4L a degree hydrolysis (DH) 44.8 ± 2.5% achieved. its were subjected simulated gastrointestinal digestion (SGID) absorption across Caco-2/TC7 cell monolayers. After the with SGID V, species between 60.6 kDa 13.0 decreased, causing an increase less than 6.51 kDa. H did not modify oxygen radical absorbance capacity (ORAC) or ACE values but caused significant decrease hydroxyl (HORAC) (30.2%). It also produced ABTS cation (ABTS assay) scavenging activity ferric reducing power (FRAP) (9.46% 20.2%, respectively). Bioactive stable after they partially able cross monolayer, which demonstrates their possible potential act inside organism.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

Hypertension is an important factor in cardiovascular diseases. Angiotensin-I-converting enzyme (ACE) inhibitors like synthetic drugs are widely used to control hypertension. ACE-inhibitory peptides from food origins could be a good alternative to synthetic drugs. A number of plant-based peptides have been investigated for their potential ACE inhibitor activities by using in vitro and in vivo a...

متن کامل

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes

The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine enzymes) and ex vivo digestion (with human gastrointestinal enzymes). Secondly, to evaluate the ACE...

متن کامل

Angiotensin-I Converting Enzyme (ACE) Inhibitory and Anti-Oxidant Activities of Sea Cucumber (Actinopyga lecanora) Hydrolysates

In recent years, food protein-derived hydrolysates have received considerable attention because of their numerous health benefits. Amongst the hydrolysates, those with anti-hypertensive and anti-oxidative activities are receiving special attention as both activities can play significant roles in preventing cardiovascular diseases. The present study investigated the angiotensin-I converting enzy...

متن کامل

Rainbow Trout, Oncorhynchus mykiss

Rainbow trout are classified as Oncorhynchus mykiss, and as such belong to the same genus as Pacific salmon, and to the family Salmonidae, which includes Atlantic salmon (Salmo salar), various trout (Salvelinus sp.), Arctic char (Salvelinus alpinus), Arctic grayling (Thymallus arcticus) and whitefish (Coregonus sp.). Rainbow trout are native to areas around the North Pacific Ocean, from souther...

متن کامل

The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Lebensmittel-Wissenschaft & Technologie

سال: 2022

ISSN: ['1096-1127', '0023-6438']

DOI: https://doi.org/10.1016/j.lwt.2021.112834