A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking

Li, Haitao; Chen, Xiaoyan; Guo, Yan; Hou, Tao; Hu, Jun

doi:10.1590/fst.66121

Cited by 5 publications

(5 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…(2023) reported significant inhibition of ACE activity by leucine. Furthermore, highly active ACEIPs isolated from egg white protein (Adli et al., 2023; Li et al., 2022; Yu et al., 2023), squid muscle protein (Fan & Wu, 2021), and silkworm pupa protein (Liang et al., 2018) contain leucine. The characteristics of the active peptides identified in this study align with the structural features of peptides with high ACE inhibitory activity.…”

Section: Discussionmentioning

confidence: 99%

Identification of angiotensin‐converting enzyme inhibitory peptides from peanut meal (Arachis hypogaea Linn) fermented by Lactobacillus pentosus using MALDI‐TOF–MS and LC–MS/MS

Li,

Guan,

Shi

et al. 2024

Food Frontiers

View full text Add to dashboard Cite

This study focused on the production of angiotensin‐converting enzyme inhibitory peptides (ACEIPs) from peanut meal (Arachis hypogaea Linn) fermented by Lactobacillus pentosus. The fermentation process was optimized using the response surface methodology with ACE inhibitory activity as the experimental indicator. ACEIPs were further purified after fermentation using ultrafiltration and Sephadex G‐25 gel chromatography. The effect of different molecular weights (ranging from 0.5 to 1.5 kDa) of ACEIP on ACE inhibitory activity was investigated, and a maximum inhibitory rate of 48.83% was achieved. The content of ACEIP was 78.95%. Amino acid analysis revealed that the hydrophobic amino acids accounted for 43.09% of the total content. Among the identified amino acids, glutamic acid had the highest content of 14.94%, followed by leucine and aspartic acid. Matrix‐assisted laser desorption/ionization time‐of‐flight–mass spectrometry (MS) and liquid chromatography–tandem MS were used to identify the molecular weights of the selected ACEIPs, yielding six ACEIPs with good stability and high hydrophilicity. Flexible docking of the six ACEIPs with ACE was simulated using AutoDock Vina (v1.5.7). The result showed that the ACEIPs formed 11, 8, 7, 9, 7, and 6 hydrogen bonds with ACE residues, and the lowest binding energies between them were −9.8, −8.1, −9.0, −9.3, −8.2, and−9.1 kcal/mol, respectively. Among them, GFGINAENNHRIF exhibited superior ACE inhibitory activity and binding stability.

show abstract

Section: Discussionmentioning

confidence: 99%

Identification of angiotensin‐converting enzyme inhibitory peptides from peanut meal (Arachis hypogaea Linn) fermented by Lactobacillus pentosus using MALDI‐TOF–MS and LC–MS/MS

Li,

Guan,

Shi

et al. 2024

Food Frontiers

View full text Add to dashboard Cite

show abstract

“…The types and amounts of these amino acids play an important role in the overall antioxidant ability of peptides. Some studies seemingly suggest that peptides containing Tyr and Trp at the C-terminal can show strong free radical-scavenging ability, while amino acids such as Ser and Ile can show high free radical-scavenging ability at both the N-terminal and the C-terminal of the peptide (Li et al, 2022;Nisov et al, 2020). The increase of these special functional amino acids among the proteolysis products of burley tobacco is an important reason for the improvement of its antioxidant capacity.…”

Section: Discussionmentioning

confidence: 99%

Proteolysis of burley tobacco-leaf extracts and antioxidant activity of the hydrolysates

et al. 2023

View full text Add to dashboard Cite

Burley tobacco-leaf protein extracted by alkali and precipitated by acid was hydrolyzed enzymatically, and optimum protease and hydrolysis parameters were determined. Pepsin was best and gave the highest hydrolysis rate (15.55%). As per results of the single-factor test, optimum hydrolysis conditions were: temperature 37 °C, pH 2, and an [E]/[S] ratio of 5%. These hydrolysis conditions were optimized by an orthogonal experiment that rendered the same results as the single factor experiment. The ratio of essential to total amino acids and that of essential to non-essential amino acids contained in the burley tobacco-leaf protease hydrolysate were higher than the FAO/WHO standard values of 0.4 and 0.6, among which hydrophobic amino acid content was the highest, followed by negatively and positively charged amino acid contents. In vitro antioxidant experiments showed that the scavenging rates of DPPH, superoxide anion, and hydroxyl radicals of tobacco-leaf protein hydrolysates were higher than those before hydrolysis. Further, the hydroxyl radical-scavenging rate was the most significant, and total antioxidant capacity was improved. The nutritive value of the burley tobacco-leaf protein hydrolysate improved upon pepsin-mediated hydrolysis, and the antioxidant activity was better. These results provide a theoretical basis for further development and utilization of tobacco protein resources.

show abstract

“…Bioactive peptides hydrolyzed from protein are the general term for 2-peptides to complex peptides composed of amino acids. Modern nutritional studies have pointed out that bioactive peptides hydrolyzed from protein can be more effectively absorbed by the body, thereby playing a specific role or improving the growth of intestinal flora to provide probiotic effects (Ji et al, 2022;Li et al, 2022;Tekle et al, 2022;Wei et al, 2022). For example, Ruann J. S. de Castro and Hélia H. Sato found that soy protein isolate hydrolysate had a 7-fold enhanced antioxidant activity compared with soy protein isolate (Castro & Sato, 2014).…”

Section: Frontier Research Direction Of Ebnmentioning

confidence: 99%

Recent advances in edible bird's nests and edible bird's nest hydrolysates

et al. 2022

View full text Add to dashboard Cite

Edible bird's nest is built by swiftlet during breeding using salivary gland secretions, which have rich nutritional value, such as anti-aging, immunomodulatory, and antioxidant activity. As a result, the global demand for edible bird's nests has increased significantly. Swiftlet farmers, consumers, traders, and authorities are increasingly concerned about obtaining safe and highquality edible bird's nests. On the other hand, subject to the limitations of the number of swiftlet populations and the ecological environment, exploring new food processing technologies to improve the utilization efficiency of edible bird's nest nutrition has also become the research frontier. Therefore, this study introduced the origin and classification of edible bird's nests in detail, presented the current situation of the edible bird's nest industry and the corresponding review measures of various countries, reviewed the efficacies of edible bird's nest, and introduced the new form of edible bird's nest utilization: edible bird's nest hydrolysates and their efficacies.

show abstract

A pivotal peptide (Ile-Leu-Lys-Pro) with high ACE- inhibitory activity from duck egg white: identification and molecular docking

Cited by 5 publications

References 48 publications

Identification of angiotensin‐converting enzyme inhibitory peptides from peanut meal (Arachis hypogaea Linn) fermented by Lactobacillus pentosus using MALDI‐TOF–MS and LC–MS/MS

Identification of angiotensin‐converting enzyme inhibitory peptides from peanut meal (Arachis hypogaea Linn) fermented by Lactobacillus pentosus using MALDI‐TOF–MS and LC–MS/MS

Proteolysis of burley tobacco-leaf extracts and antioxidant activity of the hydrolysates

Recent advances in edible bird's nests and edible bird's nest hydrolysates

Contact Info

Product

Resources

About