A comparative analysis of anti-lipidemic potential of soybean (Glycine max) protein hydrolysates obtained from different ripening stages: Identification, and molecular interaction mechanisms of novel bioactive peptides

Alnuaimi, Amna; Ajayi, Feyisola Fisayo; Hamdi, Marwa; Mudgil, Priti; Kamal, Hina; Gan, Chee Yuen; Maqsood, Sajid

doi:10.1016/j.foodchem.2022.134192

Cited by 24 publications

(12 citation statements)

References 37 publications

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“…Among the four peptides predicted to be highly antioxidant, the sequence AGDAHWTY is reported to have the lowest isoelectric point, whereas ALPPGAVHW is the one with the lowest steric hindrance. Although verification of bioactivity should be carried out employing synthetic peptides, these analyses show the potential of in silico tools in the economic and fast characterization of bioactive peptides . The isoelectric point and amphiphacity of peptides are also important, for instance, when considering their antioxidant potential if used in an emulsion, as they can be at the interface between oil and water, stabilizing it …”

Section: Resultsmentioning

confidence: 99%

“…Although verification of bioactivity should be carried out employing synthetic peptides, these analyses show the potential of in silico tools in the economic and fast characterization of bioactive peptides. 41 The isoelectric point and amphiphacity of peptides are also important, for instance, when considering their antioxidant The web server PASTA 2.0 (http://protein.bio.unipd.it/pasta2/) was implicated in computing the tendency of peptide self-aggregation specific to the possible region at sequence (with the recorded number starting from the N-terminus). For peptide discrimination, the optimal thresholds were switched to top = 1 and energy <−5 PEU (1 PEU (Pasta Energy Unit) = 1.192 kcal/mol).…”

Section: Bioavailable Peptidesmentioning

confidence: 99%

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Identification of the Bioavailable Peptidome of Chia Protein Hydrolysate and the In Silico Evaluation of Its Antioxidant and ACE Inhibitory Potential

Villanueva,

Rivero-Pino,

Martin

et al. 2024

J. Agric. Food Chem.

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The incorporation of novel, functional, and sustainable foods in human diets is increasing because of their beneficial effects and environmental-friendly nature. Chia (Salvia hispanica L.) has proved to be a suitable source of bioactive peptides via enzymatic hydrolysis. These peptides could be responsible for modulating several physiological processes if able to reach the target organ. The bioavailable peptides contained in a hydrolysate obtained with Alcalase, as functional foods, were identified using a transwell system with Caco-2 cell culture as the absorption model. Furthermore, 20 unique peptides with a molecular weight lower than 1000 Da and the higher statistical significance of the peptide-precursor spectrum match (−10 log P) were assessed by in silico tools to suggest which peptides could be those exerting the demonstrated bioactivity. From the characterized peptides, considering the molecular features and the results obtained, the peptides AGDAHWTY, VDAHPIKAM, PNYHPNPR, and ALPPGAVHW are anticipated to be contributing to the antioxidant and/or ACE inhibitor activity of the chia protein hydrolysates.

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Section: Resultsmentioning

confidence: 99%

Section: Bioavailable Peptidesmentioning

confidence: 99%

Identification of the Bioavailable Peptidome of Chia Protein Hydrolysate and the In Silico Evaluation of Its Antioxidant and ACE Inhibitory Potential

Villanueva,

Rivero-Pino,

Martin

et al. 2024

J. Agric. Food Chem.

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“…Controlled enzymatic hydrolysis facilitates the modification of the size charge, size, and conformational structure of the proteins, hence altering their functional and bioactive characteristics (e.g., digestibility, decrease of allergenicity, solubility, progression of bioactivities, etc.). 41 The degree of hydrolysis, the native protein state, specificity of the enzyme, physiological conditions (pH, E/S ratio, incubation temperature, ionic strength, and reaction time), and the method of enzyme inactivation (acidification, filtration, and heating) are the key variables that require an optimized and controlled method that could impact the functionalities of resulting bioactive peptides. In this context, protein hydrolysates were prepared using bromelain enzyme at various reaction times (2, 4, 6, 8, and 10 h) with different end DHs.…”

Section: Determination Of the Degree Of Hydrolysis (Dh %)mentioning

confidence: 99%

Improved Bioactivity and Functional Qualities of Millet Protein Enzyme Hydrolysates by Ultrasonication

Rao,

Mounika,

Shanmugam

2024

Ind. Eng. Chem. Res.

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Ultrasound (US)-extracted browntop millet protein isolates (UBMPIs) were modified by combined US pretreatment (at 200 W and different time levels 0, 5, 10, 15, and 20 min) and controlled bromelain hydrolysis, and functionalities and bioactive properties of BMPH (BMP hydrolysates) and UBMPH (USpretreated BMPH) were investigated. Compared with the controls, browntop millet protein isolates (BMPI) and BMPH, UBMPH-15 (US pretreated at 200 W for 15 min) was capable of significantly enhanced degrees of hydrolysis (65.68%), emulsifying activity (20.26 m 2 /g), free sulfhydryl content (9.09 μM/g), and protein digestibility (84.13%). However, UBMPH-10 also showed higher hydrophobicity (18.13 μg/g), solubility (88.02%), and foaming capacity (18.52%). In addition, UBMPH-15 and UBMPH-10 enhanced the in vitro antidiabetic activity with inhibition toward αamylase (0.47 mg/mL) and α-glucosidase (0.68 mg/mL), respectively. Moreover, UBMPH-15 showed the highest antilipidemic activity with greater inhibition of cholesteryl esterase (0.34 mg/mL) and lipase (0.51 mg/mL) and displayed significant scavenging activity of 2,2-diphenyl-1-picrylhydrazyl (DPPH) free radicals (73.43%). All these results suggest that UBMPHs could be potential sources of bioactive hydrolysates with enhanced antilipidemic, antidiabetic, and antioxidant activities.

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“…Food proteins are also susceptible to hydrolysis during food processing, especially during ripening and fermentation, which can directly influence the profile of generated BAPs. This has been observed in both plant proteins (e.g., in different ripening stages of soybean ( Glycine max L.) [ 27 ]) and animal-origin proteins (e.g., in different cheeses [ 28 , 29 ]).…”

Section: Production Of Baps and Hydrolysatesmentioning

confidence: 99%

Bioactive Antimicrobial Peptides from Food Proteins: Perspectives and Challenges for Controlling Foodborne Pathogens

et al. 2023

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Bioactive peptides (BAPs) derived from food proteins have been extensively studied for their health benefits, majorly exploring their potential use as nutraceuticals and functional food components. These peptides possess a range of beneficial properties, including antihypertensive, antioxidant, immunomodulatory, and antibacterial activities, and are naturally present within dietary protein sequences. To release food-grade antimicrobial peptides (AMPs), enzymatic protein hydrolysis or microbial fermentation, such as with lactic acid bacteria (LAB), can be employed. The activity of AMPs is influenced by various structural characteristics, including the amino acid composition, three-dimensional conformation, liquid charge, putative domains, and resulting hydrophobicity. This review discusses the synthesis of BAPs and AMPs, their potential for controlling foodborne pathogens, their mechanisms of action, and the challenges and prospects faced by the food industry. BAPs can regulate gut microbiota by promoting the growth of beneficial bacteria or by directly inhibiting pathogenic microorganisms. LAB-promoted hydrolysis of dietary proteins occurs naturally in both the matrix and the gastrointestinal tract. However, several obstacles must be overcome before BAPs can replace antimicrobials in food production. These include the high manufacturing costs of current technologies, limited in vivo and matrix data, and the difficulties associated with standardization and commercial-scale production.

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A comparative analysis of anti-lipidemic potential of soybean (Glycine max) protein hydrolysates obtained from different ripening stages: Identification, and molecular interaction mechanisms of novel bioactive peptides

Cited by 24 publications

References 37 publications

Identification of the Bioavailable Peptidome of Chia Protein Hydrolysate and the In Silico Evaluation of Its Antioxidant and ACE Inhibitory Potential

Identification of the Bioavailable Peptidome of Chia Protein Hydrolysate and the In Silico Evaluation of Its Antioxidant and ACE Inhibitory Potential

Improved Bioactivity and Functional Qualities of Millet Protein Enzyme Hydrolysates by Ultrasonication

Bioactive Antimicrobial Peptides from Food Proteins: Perspectives and Challenges for Controlling Foodborne Pathogens

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