scholarly journals Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity, Antioxidant Properties, Phenolic Content and Amino Acid Profiles of Fucus spiralis L. Protein Hydrolysate Fractions

Marine Drugs ◽  
2017 ◽  
Vol 15 (10) ◽  
pp. 311 ◽  
Author(s):  
Lisete Paiva ◽  
Elisabete Lima ◽  
Ana Neto ◽  
José Baptista
Keyword(s):  
Phenolic Content ◽  
Protein Hydrolysate ◽  
Antioxidant Properties ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Amino Acid Profiles ◽  
Fucus Spiralis ◽  
Ace Inhibitory

scholarly journals Effect ofJatropha curcasPeptide Fractions on the Angiotensin I-Converting Enzyme Inhibitory Activity

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Maira R. Segura-Campos ◽  
Fanny Peralta-González ◽  
Arturo Castellanos-Ruelas ◽  
Luis A. Chel-Guerrero ◽  
David A. Betancur-Ancona
Keyword(s):  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Gel Filtration ◽  
Ace Inhibition ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Hypertension is one of the most common worldwide diseases in humans. Angiotensin I-converting enzyme (ACE) plays an important role in regulating blood pressure and hypertension. An evaluation was done on the effect of Alcalase hydrolysis of defattedJatropha curcaskernel meal on ACE inhibitory activity in the resulting hydrolysate and its purified fractions. Alcalase exhibited broad specificity and produced a protein hydrolysate with a 21.35% degree of hydrolysis and 34.87% ACE inhibition. Ultrafiltration of the hydrolysate produced peptide fractions with increased biological activity (24.46–61.41%). Hydrophobic residues contributed substantially to the peptides’ inhibitory potency. The 5–10 and <1 kDa fractions were selected for further fractionation by gel filtration chromatography. ACE inhibitory activity (%) ranged from 22.66 to 45.96% with the 5–10 kDa ultrafiltered fraction and from 36.91 to 55.83% with the <1 kDa ultrafiltered fraction. The highest ACE inhibitory activity was observed inF2 ( μg/mL) from the 5–10 kDa fraction andF1 ( μg/mL) from the <1 kDa fraction. ACE inhibitory fractions fromJatrophakernel have potential applications in alternative hypertension therapies, adding a new application for theJatrophaplant protein fraction and improving the financial viability and sustainability of a Jatropha-based biodiesel industry.

scholarly journals Angiotensin-I-Converting Enzyme Inhibitory Activity and Antioxidant Properties of Cryptides Derived from Natural Actomyosin of Catla catla Using Papain

2018 ◽  
Vol 2018 ◽  
pp. 1-8 ◽  
Author(s):  
Krishnamoorthy Elavarasan ◽  
Bangalore Aswathnarayan Shamasundar
Keyword(s):  
Inhibitory Activity ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Catla Catla ◽  
Major Protein ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Natural actomyosin (NAM) from the freshwater fish Catla catla was extracted and hydrolyzed using papain enzyme at different enzyme-to-substrate ratios (0.5%, 1.0%, 2.0%, 5.0%, and 10%) to obtain the cryptides with different degrees of hydrolysis (DH). Derived cryptides were evaluated for bioactive properties such as angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant properties. The pattern of hydrolysis of NAM as a function of time revealed that major protein components such as myosin and actin were hydrolyzed within 10 min of hydrolysis. The cryptides obtained with the DH of 29.4% had significantly higher ACE inhibitory activity and linoleic acid peroxidation inhibitory activity (P<0.05). A higher DPPH free radical-scavenging activity and ferric-reducing power were exhibited by the NAM cryptide mixture obtained with the DH of 17.38 and 26.2%, respectively. The natural actomyosin could be a potential precursor to produce the cryptides with therapeutical and antioxidant properties.

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

2005 ◽  
Vol 10 (3) ◽  
pp. 239-243 ◽  
Author(s):  
Rohan Karawita ◽  
Pyo-Jam park ◽  
Nalin Siriwardhana ◽  
Byong-Tae Jeon ◽  
Sang-Ho Moon ◽  
...  
Keyword(s):  
Cervus Elaphus ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Velvet Antler ◽  
Ace Inhibitory

scholarly journals Effect of Different Proteases on the Degree of Hydrolysis and Angiotensin I-Converting Enzyme-Inhibitory Activity in Goat and Cow Milk

Biomolecules ◽  
2018 ◽  
Vol 8 (4) ◽  
pp. 101 ◽  
Author(s):  
Guowei Shu ◽  
Jie Huang ◽  
Chunju Bao ◽  
Jiangpeng Meng ◽  
He Chen ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Goat Milk ◽  
Cow Milk ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Angiotensin I-converting enzyme (ACE) peptides are bioactive peptides that have important value in terms of research and application in the prevention and treatment of hypertension. While widespread literature is concentrated on casein or whey protein for production of ACE-inhibitory peptides, relatively little information is available on selecting the proper proteases to hydrolyze the protein. In this study, skimmed cow and goat milk were hydrolyzed by four commercial proteases, including alkaline protease, trypsin, bromelain, and papain. Angiotensin I-converting enzyme-inhibitory peptides and degree of hydrolysis (DH) of hydrolysates were measured. Moreover, we compared the difference in ACE-inhibitory activity between cow and goat milk. The results indicated that the DH increased with the increase in hydrolysis time. The alkaline protease-treated hydrolysates exhibited the highest DH value and ACE-inhibitory activity. Additionally, the ACE-inhibitory activity of hydrolysates from goat milk was higher than that of cow milk-derived hydrolysates. Therefore, goat milk is a good source to obtain bioactive peptides with ACE-inhibitory activity, as compared with cow milk. A proper enzyme to produce ACE-inhibitory peptides is important for the development of functional milk products and will provide the theoretical basis for industrial production.

Novel angiotensin-I-converting enzyme inhibitory peptides derived from recombinant human αs1-casein expressed in Escherichia coli

1999 ◽  
Vol 66 (3) ◽  
pp. 431-439 ◽  
Author(s):  
YOO-KYEONG KIM ◽  
SUN YOON ◽  
DAE-YEUL YU ◽  
BO LÖNNERDAL ◽  
BONG-HYUN CHUNG
Keyword(s):  
Escherichia Coli ◽  
Amino Acid Sequences ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Treatment Of Hypertension ◽  
Ace Inhibitory

Recombinant human αs1-casein expressed in Escherichia coli was purified and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides, A-II, B-II and C, were isolated and their amino acid sequences identified as Tyr–Pro–Glu–Arg (residues 8–11), Tyr–Tyr–Pro–Gln–Ile–Met–Gln–Tyr (residues 136–143) and Asn–Asn–Val–Met–Leu–Gln–Trp (residues 164–170) respectively. ACE inhibitory activities were measured for the corresponding synthetic peptides, and the ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of A-II, B-II and C estimated to be 132·5, 24·8 and 41·0 μmol/l respectively. Peptides A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These ACE inhibitory peptides may prove useful for oral administration in the treatment of hypertension.

Sign in / Sign up

Export Citation Format

Share Document