Antihypertensive effect of angiotensin-converting enzyme inhibitory peptides from silver carp (Hypophthalmichthys molitrix) hydrolysate in spontaneously hypertensive rats

نویسندگان

  • Jin-Chao Wu
  • Miao Yu
چکیده

In order to utilize silver carp (Hypophthalmichthys molitrix), which is abundant and very cheap fresh-water fish in China, defatted silver carp muscle was hydrolysed by compound protease to achieve angiotensin-converting enzyme (ACE) inhibitory peptides. The protein hydrolysates were fractionated into low and high molecular weight fractions using an ultrafiltration (UF) membrane system. The ACE-inhibitory activity tests showed that the low molecular weight fraction was more effective. Most of the peptides in low molecular weight fraction ranged from 600 to 1600 Da. Anti-hypertensive effects of silver carp ACE-inhibitory peptides on spontaneously hypertensive rats (SHR) following oral administration was determined as the tail systolic blood pressure significantly decreased after peptides ingestion.

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Antihypertensive effect of rice protein hydrolysate with in vitro angiotensin I-converting enzyme inhibitory activity in spontaneously hypertensive rats.

Angiotensin I-converting enzyme (ACE) plays a crucial role in the regulation of blood pressure as well as cardiovascular function. ACE catalyzes the conversion of angiotensin I to vasoconstrictor angiotensin II, and also inactivates the antihypertensive vasodilator bradykinin. Inhibition of ACE mainly results an overall antihypertensive effect. Food protein-derived peptides can have ACE-inhibit...

متن کامل

Angiotensin I-Converting Enzyme Inhibitor Derived from Cross-Linked Oyster Protein

Following cross-linking by microbial transglutaminase, modified oyster proteins were hydrolyzed to improve inhibitory activity against angiotensin-converting enzyme (ACE) inhibitory activity with the use of a single protease, or a combination of six proteases. The oyster hydrolysate with the lowest 50% ACE inhibitory concentration (IC50) of 0.40 mg/mL was obtained by two-step hydrolysis of the ...

متن کامل

Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats.

Sesame peptide powder (SPP) exhibited angiotensin I-converting enzyme (ACE) inhibitory activity, and significantly and temporarily decreased the systolic blood pressure (SBP) in spontaneously hypertensive rats (SHRs) by a single administration (1 and 10 mg/kg). Six peptide ACE inhibitors were isolated and identified from SPP. The representative peptides, Leu-Val-Tyr, Leu-Gln-Pro and Leu-Lys-Tyr...

متن کامل

Vasodilating effect of di-peptides in thoracic aortas from spontaneously hypertensive rats.

In this study, we found that antihypertensive di-peptide Val-Tyr (VY) showed a vascular relaxation effect in KCl-induced contraction of thoracic aorta rings from 18-week-old spontaneously hypertensive rats among di-peptides of VY, Ile-Tyr, and Tyr-Val irrespective of their angiotensin I-converting enzyme inhibitory activity. The effect was endothelium-independent, and was closely associated wit...

متن کامل

Amaranth Protein Hydrolysates Efficiently Reduce Systolic Blood Pressure in Spontaneously Hypertensive Rats.

Alcalase is the enzyme of choice to release antihypertensive peptides from amaranth proteins, but the hydrolysis conditions have not been optimized yet. Furthermore, in vivo assays are needed to confirm such a hypotensive effect. Our aim was to optimize the hydrolysis of amaranth protein with alcalase and to test in vivo the hypotensive effect of the hydrolysates. A response surface analysis wa...

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

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2013