Isolation and characterization of antihypertensive peptides from soy bean protein

Mujtaba, Nosheen; Jahan, Nazish; Sultana, Bushra; Zia, Muhammad Anjum

doi:10.1590/s2175-97902020000419061

Cited by 6 publications

(4 citation statements)

References 23 publications

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“…Bioactive peptides have been found in abundance in both animal and plant sources. Plants possess different ACE inhibitory peptides which can be obtained by enzymatic hydrolysis [ 11 , 12 ]. The peanut, cottonseed, and chickpea are not only the most important crops broadly used as nutrient sources for animals and humans, but they also possess natural ACE inhibitory activity [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

[Retracted] Biologically Synthesized Peptides Show Remarkable Inhibition Activity against Angiotensin‐Converting Enzyme: A Promising Approach for Peptide Development against Autoimmune Diseases

Mujtaba

Jahan

Jamal

et al. 2022

BioMed Research International

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Angiotensin-converting enzyme (ACE) regulates several biological functions besides its vital role in immune functions. ACE is elevated in immune cells in inflammatory diseases including atherosclerosis, granuloma, chronic kidney disease, and also autoimmune diseases, like multiple sclerosis, rheumatoid arthritis, and type I diabetes. No significant information prevails in the literature regarding the isolation, identification, and profiling of potential ACE inhibitory peptides. In the present study, indigenous crop varieties like seeds (peanut, corn, oat, sunflower, chickpea, parsley, cottonseed, papaya, sesame, and flaxseed) were used to evaluate their ACE inhibition activity. Variables including hydrolysis time, enzyme-to-substrate ratio (E/S), pH, and temperature were standardized to acquire the most suitable and optimum ACE inhibition activity. Seeds of cotton, chickpea, and peanuts displayed remarkably maximum ACE inhibition activity than other plants. The study disclosed that maximum ACE inhibitory activity (86%) was evaluated from cottonseed at pH 8.0, temperature of 45°C, hydrolysis time of 2 hrs, and enzyme to the substrate (E/S) ratio of 1 : 5 followed by peanuts (76%) and chickpea (55%). SDS-PAGE confirmed that vicilin protein is present in cottonseed and peanut seed while cruciferin and napin proteins are present in chickpeas. LC-MS/MS analysis disclosed potential novel peptides in hydrolyzed cottonseed that can be ascribed as potential ACE inhibitors which have never been reported and studied earlier. The current study further showed that cottonseed peptides due to their promising ACE inhibitory activity can be a valuable source in the field of ACE inhibitor development.

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Section: Introductionmentioning

confidence: 99%

[Retracted] Biologically Synthesized Peptides Show Remarkable Inhibition Activity against Angiotensin‐Converting Enzyme: A Promising Approach for Peptide Development against Autoimmune Diseases

Mujtaba

Jahan

Jamal

et al. 2022

BioMed Research International

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“…The inhibitory properties of ACE are related to peptides consisting of hydrophobic amino acids (Daskaya-Dikmen et al 2017), such as proline, glycine, phenylalanine and leucine. Other studies have also revealed that the antihypertensive effect of bioactive peptides is due to the presence of the amino acids valine, histidine, proline, tryptophan or methionine in the peptide sequence (Mujtaba et al 2021). Proline existed in the bioactive peptide can effectively interact with amino acid residues at the ACE active site.…”

Section: Lactococcus Lactismentioning

confidence: 99%

Edamame protein hydrolysis using Lactococcus lactis, Lactobacillus bulgaricus and Lactobacillus paracasei produce short peptides with higher antioxidant potential

et al. 2022

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Abstract. Anggraeni SL, Jayus J, Ratnadewi AAI, Nurhayati N. 2022. Edamame protein hydrolysis using Lactococcus lactis, Lactobacillus bulgaricus and Lactobacillus paracasei produce short peptides with higher antioxidant potential. Biodiversitas 23: 3604-3613. The high demand for protein sources for functional vegetable foods, especially proteins that have ACE (Angiotensin-Converting Enzyme) inhibitory activity has encouraged efforts to meet this need through exploration of potential protein sources and the development of food processing technology to modify the protein into derivative compounds in the form of short peptides to promote higher bioactivity than the native protein. This research focused on the hydrolysis of edamame proteins into shorter peptides through a fermentation process using a group of Lactic Acid Bacteria (LABs), that is Lactococcus lactis, Lactobacillus bulgaricus and L. paracasei, to gain a higher functional activity of its protein hydrolysate. Edamame milk was fermented with that LABs as starter culture until 24 hours at 37ºC. The activity of the protease released by the LABs was confirmed using the agar diffusion method based on the emergence of a clear zone surrounding the culture, while the antioxidant activity was confirmed with the ABTS and hydroxyl radical scavenging methods. The results exhibited that the population density of starter culture in edamame milk reached 108 CFU/mL, and the pH decreased from 6.75 to 4.15. All LABs used in fermentation were able to hydrolyze protein as indicated by the increasing degree of hydrolysis and changes in protein profile of SDS-PAGE analysis. In addition, when compared to the unfermented edamame milk, the protein hydrolysate from LABs fermentation showed an increase of ABTS and hydroxyl radical inhibitory activity, in which the highest IC50 values ??of 8.96 and 13.33 g/mL of each were found in edamame milk fermented by Lc. lactis InaCC B187. An increase in ACE inhibitory activity was also observed in edamame milk fermented using this microbe (9.80 g/µL). These findings indicate that Lc. lactis InaCC B187, L. delbrueckii subspecies bulgaricus FNCC41, and L. paracasei InaCC B145 have the potency as an effective starter culture to increase bioactive peptides in edamame soybeans potential for functional food sources.

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“…The production of bioactive peptides depends on hydrolysis conditions such as type of enzyme, temperature, pH, time and enzyme‐to‐substrate ratio (Mujtaba et al ., 2021). By applying the appropriate combination of those hydrolysis conditions, it is possible to obtain optimal degree of hydrolysis influencing the ultimate bioactivity of the generated peptides (Ali Redha et al ., 2022).…”

Section: Introductionmentioning

confidence: 99%

In silico bioactivity analysis of peptide fractions derived from brewer's spent grain hydrolysates

Aguilar‐Toalá,

Cruz‐Narváez,

Quintanar‐Guerrero

et al. 2024

Int J of Food Sci Tech

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SummaryBrewer's spent grain is an agro‐industrial waste of barley malt from the manufacture of beer, which is rich in protein. Thus, this by‐product of the beer industry could be utilised to obtain bioactive peptides through enzymatic hydrolysis. The present study aimed to evaluate potential bioactivities (anti‐inflammatory, antidiabetic, antioxidant, antimicrobial) of peptide sequences identified in 5‐kDa peptide fractions derived from brewer's spent grain hydrolysates. Two experimental hydrolysates (run 5 and run 21) were selected based on their higher degree of hydrolysis (>55%), which were subjected to peptide sequence identification and used for in silico analysis. A total of fifty peptide sequences were identified between both runs. In silico analysis identified seventeen and thirteen multifunctional peptides in runs 5 and 21, respectively, which showed between two and four potential bioactivities. Interestingly, one peptide sequence (DLPPER) showed four potential bioactivities and, according to the Docking analysis, showed better Vina scores towards the protein's targets DPP‐IV (antidiabetic) and glucocorticoid receptor (anti‐inflammatory). These results demonstrate that peptides from brewer's spent grain hydrolysates may contribute to improving human health by offering potential protection against some chronic‐related diseases; however, further follow‐up in vitro and in vivo studies are needed to evaluate its actual capability.

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Isolation and characterization of antihypertensive peptides from soy bean protein

Cited by 6 publications

References 23 publications

[Retracted] Biologically Synthesized Peptides Show Remarkable Inhibition Activity against Angiotensin‐Converting Enzyme: A Promising Approach for Peptide Development against Autoimmune Diseases

[Retracted] Biologically Synthesized Peptides Show Remarkable Inhibition Activity against Angiotensin‐Converting Enzyme: A Promising Approach for Peptide Development against Autoimmune Diseases

Edamame protein hydrolysis using Lactococcus lactis, Lactobacillus bulgaricus and Lactobacillus paracasei produce short peptides with higher antioxidant potential

In silico bioactivity analysis of peptide fractions derived from brewer's spent grain hydrolysates

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