Influence of ultrasonic pretreatment on structural properties and biological activities of lupin protein hydrolysate

Fadimu, Gbemisola J.; Farahnaky, Asgar; Gill, Harsharn; Truong, Tuyen

doi:10.1111/ijfs.15549

Cited by 19 publications

(25 citation statements)

References 49 publications

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“…The activity (%) of AH and TH obtained in this study against α -amylase and α -glucosidase was higher than the results obtained by Fadimu et al [ 31 ] from lupine protein hydrolysates using Protamex. According to Chandrasekaran and de Mejia [ 32 ], the inhibitory activity of α -glucosidase varies depending on the structure of the peptide, with IC 50 ranging from 1.78 mg/mL to 8.74 mg/mL for the isolated peptide from germinated chickpea protein hydrolysates.…”

Section: Resultscontrasting

confidence: 89%

Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases

AL‐Bukhaiti

Al-Dalali

Noman

et al. 2022

Foods

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Optimization of the enzymolysis process for preparing peanut protein hydrolysates using alcalase and trypsin was performed by employing the central composite design (CCD) of response surface methodology (RSM). The independent variables were solid-to-liquid ratio (S/L), enzyme-to-substrate ratio (E/S), pH, and reaction temperature, while the response variables were degree of hydrolysate (DH), α-amylase, and α-glucosidase inhibitory activity. The highest DH (22.84% and 14.63%), α-amylase inhibition (56.78% and 40.80%), and α-glucosidase inhibition (86.37% and 86.51%) were obtained under optimal conditions, which were S/L of 1:26.22 and 1:30 w/v, E/S of 6% and 5.67%, pH of 8.41 and 8.56, and temperature of 56.18 °C and 58.75 °C at 3 h using alcalase (AH) and trypsin (TH), respectively. Molecular weight distributions of peanut protein hydrolysates were characterized by SDS-PAGE, which were mostly ˂10 kDa for both hydrolysates. Lyophilized AH and TH had IC50 values of 6.77 and 5.86 mg/mL for α-amylase inhibitory activity, and 6.28 and 5.64 mg/mL for α-glucosidase inhibitory activity. The IC50 of AH and TH against DPPH radical was achieved at 4.10 and 3.20 mg/mL and against ABTS radical at 2.71 and 2.32 mg/mL, respectively. The obtained hydrolysates with antidiabetic activity could be utilized as natural alternatives to synthetic antidiabetics, particularly in food and pharmaceutical products.

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Section: Resultscontrasting

confidence: 89%

Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases

AL‐Bukhaiti

Al-Dalali

Noman

et al. 2022

Foods

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“…There was no effect from beverages matrix, as well as functional supplements, which may suggest that a key role in this activity plays bioactive peptides driven by lentil proteins. It was previously shown in many studies, e.g., hydrolysate prepared from lupin protein using Protamex enzyme [57]. Such a mechanism is also supported by our previous study concerning protein digestibility, in particular, no effect of additives on this feature [23].…”

Section: Resultssupporting

confidence: 86%

The Protein-Rich Powdered Beverages Stabilized with Flax Seeds Gum—Antioxidant and Antiproliferative Properties of the Potentially Bioaccessible Fraction

2022

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The functional beverages market is one of the fastest-growing sectors of functional food production. An innovative recipe for powdered fruit and vegetable drinks fortified with lentil proteins (AGF) and stabilized with flax seed gums (FSG) was developed. The study focused on the analysis of potentially bioaccessible fractions from the produced beverages in terms of their antioxidant, antiproliferative activities and physicochemical properties. The contents of bioactive components were tailored by the incorporation of lyophilized fruits and vegetables, the FSG and the AGF. Digestion in vitro effectively released phenolics from all matrices. The highest contents of potentially bioavailable polyphenols were recorded for the AGF based beverages enriched with 5% of FSG and green-leafy vegetables (58 mg/100 mL) and those with lyophilized fruit (54 mg/100 mL). The reducing power of the beverages was mainly affected by the presence of the AGF, while the FSG and lyophilized fruit improved the chelating power. The digests applied in the concentrations mimicking physiological concentrations showed antiproliferative properties against gastric and colon adenocarcinoma—they seemed to be tailored by bioactive peptides and phenolics, respectively. The addition of the FSG improved the stability of the beverages increasing the time required for a reduction of 20% of the initial optical density by 16- and 28-times in the beverages without additives or enriched with vegetables. Both, the AGF and FSG stabilize the beverages after rehydration and are sources of bioaccessible antioxidant and anticancer components, which create their functionality.

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“…The highest α-amylase inhibitory activity was observed in unfractionated hydrolysates generated using alcalase (ACT) (IC50 value = 1.66 mg/mL), followed by unfractionated hydrolysates from flavourzyme (FCT) (IC50 value = 1.98 mg/mL). This result is in accordance with previous studies which reported that hydrolysates generated using alcalase had significantly higher α-amylase inhibitory (lower IC50 value) ability than those prepared using flavourzyme, based on IC50 values [4,10].…”

Section: Inhibition Of the α-Amylase Inhibitory Activitysupporting

confidence: 93%

In-Silico Analysis and Antidiabetic Effect of α-Amylase and α-Glucosidase Inhibitory Peptides from Lupin Protein Hydrolysate: Enzyme-Peptide Interaction Study Using Molecular Docking Approach

Fadimu

Farahnaky

Gill

et al. 2022

Foods

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The use of natural ingredients for managing diabetes is becoming more popular in recent times due to the several adverse effects associated with synthetic antidiabetic medications. In this study, we investigated the in vitro antidiabetic potential (through inhibition of α-glucosidase (AG) and α-amylase (AA)) of hydrolysates from lupin proteins pretreated with ultrasound and hydrolyzed using alcalase (ACT) and flavourzyme (FCT). We further fractionated ACT and FCT into three molecular weight fractions. Unfractionated ACT and FCT showed significantly (p < 0.05) higher AG (IC50 value = 1.65 mg/mL and 1.91 mg/mL) and AA (IC50 value = 1.66 mg/mL and 1.98 mg/mL) inhibitory activities than their ultrafiltrated fractions, where lower IC50 values indicate higher inhibitory activities. Then, ACT and FCT were subjected to peptide sequencing using LC-MS-QTOF to identify the potential AG and AA inhibitors. Molecular docking was performed on peptides with the highest number of hotspots and PeptideRanker score to study their interactions with AG and AA enzymes. Among the peptides identified, SPRRF, FE, and RR were predicted to be the most active peptides against AG, while AA inhibitors were predicted to be RPR, PPGIP, and LRP. Overall, hydrolysates prepared from lupin proteins using alcalase and flavourzyme may be useful in formulating functional food for managing diabetics.

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Influence of ultrasonic pretreatment on structural properties and biological activities of lupin protein hydrolysate

Cited by 19 publications

References 49 publications

Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases

Response Surface Modeling and Optimization of Enzymolysis Parameters for the In Vitro Antidiabetic Activities of Peanut Protein Hydrolysates Prepared Using Two Proteases

The Protein-Rich Powdered Beverages Stabilized with Flax Seeds Gum—Antioxidant and Antiproliferative Properties of the Potentially Bioaccessible Fraction

In-Silico Analysis and Antidiabetic Effect of α-Amylase and α-Glucosidase Inhibitory Peptides from Lupin Protein Hydrolysate: Enzyme-Peptide Interaction Study Using Molecular Docking Approach

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