In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties

Famuwagun, Akinsola A.; Alashi, Adeola M.; Gbadamosi, Saka O.; Taiwo, Kehinde A.; Oyedele, D. J.; Adebooye, O. C.; Aluko, Rotimi E.

doi:10.31883/pjfns/130401

Cited by 14 publications

(12 citation statements)

References 61 publications

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“…Our results also showed that peptides with lower molecular weight had a better inhibitory activity, which was consistent with the literature indicating that <1 kDa fractions showed the highest inhibition . Previous research has shown that peptides with lower molecular weight could be absorbed easier by the gastrointestinal tract and display better biological activity . Thus, in this study, peptide fractions with molecular weight <1 kDa were recognized as the most efficient α-glucosidase inhibitors.…”

Section: Resultssupporting

confidence: 91%

“…25 Previous research has shown that peptides with lower molecular weight could be absorbed easier by the gastrointestinal tract and display better biological activity. 19 Thus, in this study, peptide fractions with molecular weight <1 kDa were recognized as the most efficient α-glucosidase inhibitors. α-Glucosidase Inhibitory Activity of WGPs on Everted Intestine Sleeves.…”

Section: ■ Results and Discussionmentioning

confidence: 65%

“…α-Glucosidase Inhibition Assay. The α-glucosidase inhibition assays were conducted as previously described with a slight modification: 19 100 μL of α-glucosidase solution (0.2 U/mL, PBS buffer, pH 6.8) was premixed with 50 μL of sample solution with different concentrations in potassium phosphate buffer (0.1 M, pH 6.8). Following incubation at 37.0 °C for 20 min, 100 μL of α-pnitrophenyl glucopyranoside (α-pNPG, 1.5 mM) substrate was added to initialize the reactions.…”

Section: ■ Methodsmentioning

confidence: 99%

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Molecular Mechanism for the α-Glucosidase Inhibitory Effect of Wheat Germ Peptides

Liu

Wen

et al. 2021

J. Agric. Food Chem.

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Wheat germ peptides (WGPs) have various benefits to human health, while their antidiabetes mechanism remains unknown. In this study, the α-glucosidase inhibition activity of WGPs was identified, exhibiting an IC50 value of 6.87 mg/mL. By further filtrating them into five groups according to molecular weight (M w), the fraction with M w < 1 kDa displayed the highest inhibitory activity with an IC50 of 2.10 mg/mL. The addition of 2 mg/mL WGPs with M w < 1 kDa effectively reduced the glucose-releasing rate on everted intestine sleeves. By virtual screening and HPLC-QTOF-MS/MS, LDLQR, AGGFR, and LDNFR were identified and synthesized for the first time, and their IC50 values were 8.59, 8.66, and 9.21 mM, respectively. Molecular docking and amino acid composition analysis results showed that the high content of C-terminal Arg residues in the peptides could be the essential reason for their α-glucosidase inhibition activity. This study paved a way to utilize WGPs as potential antidiabetes ingredients for the food industry.

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Section: Resultssupporting

confidence: 91%

Section: ■ Results and Discussionmentioning

confidence: 65%

Section: ■ Methodsmentioning

confidence: 99%

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Molecular Mechanism for the α-Glucosidase Inhibitory Effect of Wheat Germ Peptides

Liu

Wen

et al. 2021

J. Agric. Food Chem.

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“…The IC 50 of BH in DPPH assay was lower than that of salmon by-product hydrolysates prepared using Alcalase, Flavorzyme, Neutrase, Protamex and trypsin, which ranged from 3.62 to 4.95 mg/mL, while it was higher than that of the hydrolysate obtained using pepsin, which was 1.63 mg/mL [Ahn et al, 2014]. The release of bioactive peptides during the hydrolysis depends on enzyme specificity [Famuwagun et al, 2020]. In turn, the DH strongly correlates with the bioactivities of peptides generated during the hydrolysis because it affects the amino acid composition, in addition to the sizes and structures of these peptides [Jang et al, 2016].…”

Section: Antioxidant Activities Of Bhmentioning

confidence: 82%

“…They can perform other physiological functions in the human body, such as antihypertensive and antithrombotic activities, in addition to their effective activity against lipid peroxidation and free radicals [Chi et al, 2014;. The properties of hydrolysates and peptides resulting from enzymolysis make them potentially useful in the prevention, treatment, and amelioration of several diseases, in addition to extending the shelf life of food products [Famuwagun et al, 2020].…”

Section: Introductionmentioning

confidence: 99%

Antioxidant Activity of Hybrid Sturgeon (<i>Huso dauricus</i> × <i>Acipenser schrenckii</i>) Protein Hydrolysate Prepared Using Bromelain, Its Fractions and Purified Peptides

Noman¹,

Wang²,

Zhang³

et al. 2022

Pol. J. Food Nutr. Sci.

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Protein hydrolysates could be a natural and safer source of antioxidant peptides. The purpose of this study was to optimize the hydrolysis of Huso dauricus × Acipenser schrenckii sturgeon proteins using bromelain and purify antioxidant peptides from hydrolysate. The degree of hydrolysis of 18.69% was obtained under the optimal conditions and hydrolysate had 94.76% solubility, 902 nm particle size and high antioxidant activity. The IC 50 for DPPH • and ABTS •+ scavenging activity were 3.14 and 3.81 mg/mL, respectively. The fraction of hydrolysate with a molecular weight of <1 kDa exhibited the highest antiradical activity against DPPH • with IC 50 of 2.10 mg/mL. In turn, the IC 50 of the most active fraction after the Sephadex G-15 separation was 1.77 mg/mL. The reverse phase high performance liquid chromatography (RP-HPLC) was used to purify the peptides from this fraction. The peptide with histidine, leucine and glycine (MW of 0.2955 kDa) exhibited the highest antioxidant activity (IC 50 of 1.33 mg/mL). The obtained fractions and peptides with antioxidant activity could be used as natural substitutes for synthetic antioxidants, especially in food and pharmaceuticals.

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Protein identification and potential bioactive peptides from pumpkin (Cucurbita maxima) seeds

Lin,

Tejano,

Panjaitan

et al. 2024

Food Science & Nutrition

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Pumpkin is an economically important crop all over the world. Approximately, 18%–21% of pumpkins, consisting of peels and seeds by‐products, are wasted during processing. In addition, the seeds are rich in protein and have the potency of bioactive peptide production. This study aims to recognize the proteins and investigate the potential bioactive peptides from pumpkin (Cucurbita maxima) seeds. Pumpkin seeds were subjected to hot air drying (HAD) at 55°C for 12 h and freeze‐drying (FD) at −80°C for 54 h before they were powdered, analyzed, and precipitated by isoelectric point to obtain pumpkin seed protein isolates (PSPI). PSPI comprised 11S globulin subunit beta, 2S seed storage albumin, and chaperonin CPN60‐1. To generate hydrolysate peptides, PSPI was hydrolyzed using papain, pepsin, and bromelain. FD group pepsin hydrolysates had the highest peptide content of 420.83 mg/g. ACE inhibition and DPP‐IV inhibition activity were analyzed for each enzymatic hydrolysate. The pepsin hydrolyzed sample exhibited the highest ACE inhibition of 70.26%, and the papain hydrolyzed sample exhibited the highest DPP‐IV inhibition of 30.51%. The simulated gastrointestinal digestion (SGID) conducted by pepsin and pancreatin increased ACE inhibitory activity from 76.93% to 78.34%, and DPP‐IV inhibited activity increased from 58.62% to 77.13%. Pepsin and papain hydrolysates were fractionated using ultrafiltration to measure ACE and DPP‐IV inhibition activity. The highest free radical scavenging abilities were exhibited by the <1 kDa hydrolysate fractions with 78.34% ACE inhibitory activities and 79.55% DPP‐IV inhibitory activities. This research revealed that pumpkin seeds had the potency to produce bioactive peptides.

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In Vitro Characterization of Fluted Pumpkin Leaf Protein Hydrolysates and Ultrafiltration of Peptide Fractions: Antioxidant and Enzyme-Inhibitory Properties

Cited by 14 publications

References 61 publications

Molecular Mechanism for the α-Glucosidase Inhibitory Effect of Wheat Germ Peptides

Molecular Mechanism for the α-Glucosidase Inhibitory Effect of Wheat Germ Peptides

Antioxidant Activity of Hybrid Sturgeon (<i>Huso dauricus</i> × <i>Acipenser schrenckii</i>) Protein Hydrolysate Prepared Using Bromelain, Its Fractions and Purified Peptides

Protein identification and potential bioactive peptides from pumpkin (Cucurbita maxima) seeds

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