Antioxidative and ACE inhibitory activities of protein hydrolysates from zebra blenny (Salaria basilisca) in alloxan-induced diabetic rats

2014 ◽  
Vol 49 (5) ◽  
pp. 890-897 ◽  
Author(s):  
Naourez Ktari ◽  
Rim Nasri ◽  
Kais Mnafgui ◽  
Khaled Hamden ◽  
Olfa Belguith ◽  
...  
Keyword(s):  
Diabetic Rats ◽  
Protein Hydrolysates ◽  
Inhibitory Activities ◽  
Ace Inhibitory

scholarly journals Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Asif Wali ◽  
Haile Ma ◽  
Muhammad Shahnawaz ◽  
Khizar Hayat ◽  
Jian Xiaong ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Inhibitory Activity ◽  
Surface Hydrophobicity ◽  
Protein Hydrolysates ◽  
Ace Inhibitory Activity ◽  
Power Ultrasound ◽  
Inhibitory Activities ◽  
Rapeseed Protein Hydrolysates ◽  
Thermal Stability Of ◽  
Ace Inhibitory

The effects of power ultrasound pretreatments on the degree of hydrolysis (DH), angiotensin-I-converting enzyme (ACE) inhibitory activity, amino acid composition, surface hydrophobicity, protein solubility, and thermal stability of ACE inhibition of rapeseed protein hydrolysates were evaluated. Ultrasonic pretreatments before enzymolysis in terms of power and exposure time increased the DH and ACE inhibitory activities over the control (without sonication). In this study, maximum DH 22.07% and ACE inhibitory activity 72.13% were achieved at 600 W and 12 min pretreatment. Compared to the hydrolysates obtained without sonication, the amino acid profile of ultrasound pretreated hydrolysates showed significant changes particularly in the proline content and hydrophobic amino acids with an increased rate of 2.47% and 6.31%, respectively. Ultrasound pretreatment (600 watts, 12 min) improved functional properties of protein hydrolysates over control by enhancing surface hydrophobicity and solubility index with an increased rate of 130.76% and 34.22%. Moreover, the stability test showed that the ACE inhibitory activity remains stable against heat treatments. However, extensive heat, prolonged heating time, and alkaline conditions were not in the favor of stability test, while under mild heat and acidic conditions their ACE inhibitory activities were not significantly different from unheated samples.

Antioxidant, anticancer and ACE-inhibitory activities of bioactive peptides from wheat germ protein hydrolysates

2019 ◽  
Vol 32 ◽  
pp. 100450 ◽  
Author(s):  
Zohreh Karami ◽  
Seyed Hadi Peighambardoust ◽  
Javad Hesari ◽  
Behrouz Akbari-Adergani ◽  
David Andreu
Keyword(s):  
Wheat Germ ◽  
Bioactive Peptides ◽  
Protein Hydrolysates ◽  
Inhibitory Activities ◽  
Ace Inhibitory

scholarly journals Angiotensin Converting Enzyme Inhibitory Activity of Blue Lupin (Lupinus angustifolius) Proteins

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 492-492
Author(s):  
Chin Yee ◽  
Chew Yee ◽  
Amin Ismail ◽  
Toh Theng ◽  
Azrina Azlan
Keyword(s):  
Inhibitory Activity ◽  
Extraction Procedure ◽  
Protein Hydrolysates ◽  
Water Soluble ◽  
Lupin Protein ◽  
Significant Difference ◽  
Ic50 Values ◽  
Inhibitory Activities ◽  
Ace Activity ◽  
Ace Inhibitory

Abstract Objectives To evaluate the ACE inhibitory activity of protein hydrolysates derived from lupin Methods Methods used are spectrophotometer to assay the ACE activity, electrophoresis for estimation of protein molecular weight, and HPLC for determining products of ACE activity. Results The results revealed that the lupin flour was abundant in protein (43.3 g/100 g). Results from sequential Osborne extraction procedure showed that lupin protein comprised of 46% salt-soluble globulin, 27% water-soluble albumin, 18% alkaline-soluble glutelin and 7% alcohol-soluble prolamin fractions. Furthermore, lupin protein was rich in lysine but limiting in methionine. Hydrolysates prepared using Alcalase exhibited higher ACE inhibitory activities compared with those prepared using Flavourzyme, showing IC50 values ranging from 0.10 to 0.21 mg/mL. However, there was no significant difference in IC50 values between the hydrolysates prepared using Alcalase for 4, 10 and 16 h of hydrolysis times. Conclusions The results suggested that globulin was the major contributing protein fraction on ACE inhibitory effect in lupin protein. The lupin protein hydrolysates with potent ACE inhibitory activities can be incorporated into the daily diet to prevent hypertension. Funding Sources Ministry of Education Malaysia.

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