scholarly journals Sulfur-containing acylamino acids. I. Syntheses and angiotensin I converting enzyme-inhibitory activities of sulfur-containing N-mercaptoalkanoyl amino acids.

1987 ◽  
Vol 35 (6) ◽  
pp. 2382-2387 ◽  
Author(s):  
TAKETOSHI KOMORI ◽  
KATSUMI ASANO ◽  
YASUTO SASAKI ◽  
HIROMI HANAI ◽  
RUMI SEO ◽  
...  
Keyword(s):  
Amino Acids ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Inhibitory Activities ◽  
Sulfur Containing

scholarly journals Production of Protein Hydrolysate Containing Antioxidant and Angiotensin -I-Converting Enzyme (ACE) Inhibitory Activities from Tuna (Katsuwonus pelamis) Blood

Processes ◽  
2020 ◽  
Vol 8 (11) ◽  
pp. 1518
Author(s):  
Natthaphon Mongkonkamthorn ◽  
Yuwares Malila ◽  
Suthasinee Yarnpakdee ◽  
Sakunkhun Makkhun ◽  
Joe M. Regenstein ◽  
...  
Keyword(s):  
Amino Acids ◽  
Radical Scavenging ◽  
Sensory Properties ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Antioxidant Power ◽  
Angiotensin I Converting Enzyme ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Tuna blood (TB) was subjected to enzymatic hydrolysis. The effects of the relationship of hydrolysis time (30–180 min) and enzyme concentration (0.5–3.0% w/w protein) on the degree of hydrolysis (DH), yield, antioxidant and angiotensin-I-converting enzyme (ACE) inhibitory activities were determined. The response surface methodology (RSM) showed that TB hydrolysis’s optimum conditions were hydrolysis for 180 min and Alcalase, Neutrase or Flavourzyme at 2.81%, 2.89% or 2.87% w/w protein, respectively. The hydrolysates with good DH (40–46%), yield (3.5–4.6%), the IC50 of DPPH (0.8–1.6 mg/mL) and ABTS (1.0–1.4 mg/mL) radical scavenging activity, ferric reducing antioxidant power (FRAP) value (0.28–0.65 mmol FeSO4/g) and IC50 of ACE inhibitory activity (0.15–0.28 mg/mL) were obtained with those conditions. The TB hydrolysate using Neutrase (TBHN) was selected for characterization in terms of amino acid composition, peptide fractions and sensory properties. The essential, hydrophobic and hydrophilic amino acids in TBHN were ~40%, 60% and 20% of total amino acids, respectively. The fraction of molecular weight <1 kDa showed the highest antioxidant and ACE inhibitory activities. Fishiness and bitterness were the main sensory properties of TBHN. Fortification of TBHN in mango jelly at ≤ 0.5% (w/w) was accepted by consumers as like moderately to like slightly, while mango jelly showed strong antioxidant and ACE inhibitory activities. TBHN could be developed for natural antioxidants and antihypertensive peptides in food and functional products.

scholarly journals Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 3822
Author(s):  
Azis Boing Sitanggang ◽  
Jessica Eka Putri ◽  
Nurheni Palupi ◽  
Emmanuel Hatzakis ◽  
Elvira Syamsir ◽  
...  
Keyword(s):  
Systematic Review ◽  
Amino Acids ◽  
Reaction Time ◽  
Hydrolytic Activity ◽  
Converting Enzyme ◽  
Enzymatic Preparation ◽  
Angiotensin I ◽  
Velvet Bean ◽  
Angiotensin I Converting Enzyme ◽  
Aspergillus Sp

The Angiotensin-I-converting enzyme (ACE) is a peptidase with a significant role in the regulation of blood pressure. Within this work, a systematic review on the enzymatic preparation of Angiotensin-I-Converting Enzyme inhibitory (ACEi) peptides is presented. The systematic review is conducted by following PRISMA guidelines. Soybeans and velvet beans are known to have high protein contents that make them suitable as sources of parent proteins for the production of ACEi peptides. Endopeptidase is commonly used in the preparation of soybean-based ACEi peptides, whereas for velvet bean, a combination of both endo- and exopeptidase is frequently used. Soybean glycinin is the preferred substrate for the preparation of ACEi peptides. It contains proline as one of its major amino acids, which exhibits a potent significance in inhibiting ACE. The best enzymatic treatments for producing ACEi peptides from soybean are as follows: proteolytic activity by Protease P (Amano-P from Aspergillus sp.), a temperature of 37 °C, a reaction time of 18 h, pH 8.2, and an E/S ratio of 2%. On the other hand, the best enzymatic conditions for producing peptide hydrolysates with high ACEi activity are through sequential hydrolytic activity by the combination of pepsin-pancreatic, an E/S ratio for each enzyme is 10%, the temperature and reaction time for each proteolysis are 37 °C and 0.74 h, respectively, pH for pepsin is 2.0, whereas for pancreatin it is 7.0. As an underutilized pulse, the studies on the enzymatic hydrolysis of velvet bean proteins in producing ACEi peptides are limited. Conclusively, the activity of soybean-based ACEi peptides is found to depend on their molecular sizes, the amino acid residues, and positions. Hydrophobic amino acids with nonpolar side chains, positively charged, branched, and cyclic or aromatic residues are generally preferred for ACEi peptides.

Angiotensin I-Converting Enzyme Inhibitory Activities of Extracts from Commercial Chinese Style Fermented Soypaste

2010 ◽  
Vol 44 (2) ◽  
pp. 167-172 ◽  
Author(s):  
Feng-Juan LI ◽  
Li-Jun YIN ◽  
Yong-Qiang CHENG ◽  
Masayoshi SAITO ◽  
Kohji YAMAKI ◽  
...  
Keyword(s):  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Inhibitory Activities
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