Research

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16 pages, 3526 KiB

Open AccessArticle

Engineering Concanavalin B to Release Bioactive Peptides against Metabolic Syndrome

by Diego Armando Maldonado-Torres, G. Janet Jara-Romero, Flor de Fátima Rosas-Cárdenas, D. Alejandro Fernández-Velasco and Silvia Luna-Suárez

Foods 2021, 10(7), 1554; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10071554 - 05 Jul 2021

Viewed by 1852

Abstract

Metabolic syndrome is a severe public health issue characterized by multiple metabolic disturbances. Current treatments prescribe a particular drug for each of them, producing multiple side effects. As a first step towards a more integral approach, we applied our recently described methodology to [...] Read more.

Metabolic syndrome is a severe public health issue characterized by multiple metabolic disturbances. Current treatments prescribe a particular drug for each of them, producing multiple side effects. As a first step towards a more integral approach, we applied our recently described methodology to design single proteins, based in the Concanavalin B scaffold (1CNV), that contain several bioactive peptides (BPs), including antioxidant and lipid-lowering activities as well as inhibitors of dipeptidyl peptidase IV (DPPIV) and the angiotensin converting enzyme. Modified Concanavalin (CNV44), the designed protein that showed the best in silico properties, was expressed in high yields in E. coli and purified to homogeneity. After in vitro digestion with gastrointestinal enzymes, all the biological activities tested where higher in CNV44 when compared to the non-modified protein 1CNV, or to other previous reports. The results presented here represent the first in vitro evidence of a modified protein with the potential to treat metabolic syndrome and open the venue for the design of proteins to treat other non-communicable diseases. Full article

(This article belongs to the Special Issue Advances in Functional and Bioactive Potentials of Food Proteins and Peptides)

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12 pages, 1553 KiB

Open AccessArticle

Combined Effects of Amino Acids in Garlic and Buna-Shimeji (Hypsizygus marmoreus) on Suppression of CCl₄-Induced Hepatic Injury in Rats

by Yusuke Yamaguchi, Yushi Hirata, Takeshi Saito and Hitomi Kumagai

Foods 2021, 10(7), 1491; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10071491 - 27 Jun 2021

Cited by 3 | Viewed by 1879

Abstract

The combination of the garlic-derived amino acid, S-allyl-l-cysteine sulfoxide (ACSO), and ornithine or arginine on CCl₄-induced hepatic injury was examined. After investigating the effectiveness of the mixture of ACSO and ornithine or arginine in preventing hepatic injury in [...] Read more.

The combination of the garlic-derived amino acid, S-allyl-l-cysteine sulfoxide (ACSO), and ornithine or arginine on CCl₄-induced hepatic injury was examined. After investigating the effectiveness of the mixture of ACSO and ornithine or arginine in preventing hepatic injury in vivo, an extract rich in ACSO and ornithine was prepared by converting arginine in garlic to ornithine by arginase from Hypsizygus marmoreus (buna-shimeji), after screening the productivity of ornithine among 12 kinds of mushrooms. Co-administration of ACSO with ornithine or arginine suppressed the increase in aspartate transaminase, alanine transaminase, and thiobarbituric acid reactive substance, and the decrease in glutathione S-transferase and cytochrome p450 2E1 activities after CCl₄ injection more effectively than a single administration of ACSO. All extracts prepared from garlic and buna-shimeji with low and high contents of ACSO and arginine or ornithine significantly suppressed CCl₄-induced hepatic injury in rats. Considering that ACSO is tasteless, odourless, and enhances taste, and ornithine has a flat or sweet taste and masks bitterness, the extract rich in ACSO and ornithine from garlic and buna-shimeji could be considered a potential antioxidant food material that can be added to many kinds of food to prevent hepatic injury. Full article

(This article belongs to the Special Issue Advances in Functional and Bioactive Potentials of Food Proteins and Peptides)

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22 pages, 1230 KiB

Open AccessArticle

Effect of Protease Type and Peptide Size on the In Vitro Antioxidant, Antihypertensive and Anti-Diabetic Activities of Eggplant Leaf Protein Hydrolysates

by Akinsola A. Famuwagun, Adeola M. Alashi, Saka O. Gbadamosi, Kehinde A. Taiwo, Durodoluwa Oyedele, Odunayo C. Adebooye and Rotimi E. Aluko

Foods 2021, 10(5), 1112; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10051112 - 18 May 2021

Cited by 20 | Viewed by 2855

Abstract

Solanum macrocarpon (eggplant) leaf protein isolate (ELI) was hydrolyzed using four different enzymes to produce hydrolysates from alcalase (AH), chymotrypsin (CH) pepsin (PH) and trypsin (TH). CH had an overall stronger antioxidant property and was separated using ultrafiltration membranes into <1, 1–3 and [...] Read more.

Solanum macrocarpon (eggplant) leaf protein isolate (ELI) was hydrolyzed using four different enzymes to produce hydrolysates from alcalase (AH), chymotrypsin (CH) pepsin (PH) and trypsin (TH). CH had an overall stronger antioxidant property and was separated using ultrafiltration membranes into <1, 1–3 and 3–5 kDa peptide fractions. Gel-permeation chromatography confirmed conversion of the ELI (average of 22 kDa) into protein hydrolysates that contained smaller peptides (<6 kDa). A total of 23 peptides consisting of tri and tetrapeptides were identified from the CH, which is a wider spectrum when compared to seven for AH and four each for TH and PH. CH exhibited stronger scavenging activities against DPPH and hydroxyl radicals. CH and TH exhibited the strongest inhibitions against angiotensin-converting enzyme. In contrast, AH was the strongest inhibitor of α-amylase while AH and PH had strong inhibitory activities against α-glucosidase when compared with other hydrolysates. Ultrafiltration fractionation produced peptides that were stronger (p < 0.05) scavengers of DPPH, and hydroxyl radicals, in addition to better metal-chelating and enzyme inhibition agents. The study concluded that the eggplant protein hydrolysates and the UF fractions may find applications in tackling oxidative stress-related diseases and conditions involving excessive activities of the metabolic enzymes. Full article

(This article belongs to the Special Issue Advances in Functional and Bioactive Potentials of Food Proteins and Peptides)

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17 pages, 3962 KiB

Open AccessArticle

Multifunctional Tyrosinase Inhibitor Peptides with Copper Chelating, UV-Absorption and Antioxidant Activities: Kinetic and Docking Studies

by Pei-Gee Yap and Chee-Yuen Gan

Foods 2021, 10(3), 675; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10030675 - 22 Mar 2021

Cited by 12 | Viewed by 3889

Abstract

Nature-derived tyrosinase inhibitors are of great industrial interest. Three monophenolase inhibitor peptides (MIPs) and three diphenolase inhibitor peptides (DIPs) from a previous study were investigated for their in vitro tyrosinase inhibitory effects, mode of inhibition, copper-chelating activity, sun protection factor (SPF) and antioxidant [...] Read more.

Nature-derived tyrosinase inhibitors are of great industrial interest. Three monophenolase inhibitor peptides (MIPs) and three diphenolase inhibitor peptides (DIPs) from a previous study were investigated for their in vitro tyrosinase inhibitory effects, mode of inhibition, copper-chelating activity, sun protection factor (SPF) and antioxidant activities. DIP1 was found to be the most potent tyrosinase inhibitor (IC₅₀ = 3.04 ± 0.39 mM), which could be due to the binding interactions between its aromatic amino acid residues (Y2 and D7) with tyrosinase hotspots (H85, V248, H258, H263, F264, R268, V283 and E322) and its ability to chelate copper ion within the substrate-binding pocket. The conjugated planar rings of tyrosine and tryptophan may interact with histidine within the active site to provide stability upon enzyme-peptide binding. This postulation was later confirmed as the Lineweaver–Burk analysis had identified DIP1 as a competitive inhibitor and DIP1 also showed 36.27 ± 1.17% of copper chelating activity. In addition, DIP1 provided the highest SPF value (11.9 ± 0.04) as well as ferric reducing antioxidant power (FRAP) (5.09 ± 0.13 mM FeSO₄), 2,2′–azinobis(3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS) (11.34 ± 0.90%) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) (29.14 ± 1.36%) free radical scavenging activities compared to other peptides. These results demonstrated that DIP1 could be a multifunctional anti-tyrosinase agent with pharmaceutical and cosmeceutical applications. Full article

(This article belongs to the Special Issue Advances in Functional and Bioactive Potentials of Food Proteins and Peptides)

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15 pages, 2704 KiB

Open AccessArticle

A Novel Machine Learning Strategy for the Prediction of Antihypertensive Peptides Derived from Food with High Efficiency

by Liyang Wang, Dantong Niu, Xiaoya Wang, Jabir Khan, Qun Shen and Yong Xue

Foods 2021, 10(3), 550; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10030550 - 06 Mar 2021

Cited by 11 | Viewed by 2572

Abstract

Strategies to screen antihypertensive peptides with high throughput and rapid speed will doubtlessly contribute to the treatment of hypertension. Food-derived antihypertensive peptides can reduce blood pressure without side effects. In the present study, a novel model based on the eXtreme Gradient Boosting (XGBoost) [...] Read more.

Strategies to screen antihypertensive peptides with high throughput and rapid speed will doubtlessly contribute to the treatment of hypertension. Food-derived antihypertensive peptides can reduce blood pressure without side effects. In the present study, a novel model based on the eXtreme Gradient Boosting (XGBoost) algorithm was developed and compared with the dominating machine learning models. To further reflect on the reliability of the method in a real situation, the optimized XGBoost model was utilized to predict the antihypertensive degree of the k-mer peptides cutting from six key proteins in bovine milk, and the peptide–protein docking technology was introduced to verify the findings. The results showed that the XGBoost model achieved outstanding performance, with an accuracy of 86.50% and area under the receiver operating characteristic curve of 94.11%, which were better than the other models. Using the XGBoost model, the prediction of antihypertensive peptides derived from milk protein was consistent with the peptide–protein docking results, and was more efficient. Our results indicate that using the XGBoost algorithm as a novel auxiliary tool is feasible to screen for antihypertensive peptides derived from food, with high throughput and high efficiency. Full article

(This article belongs to the Special Issue Advances in Functional and Bioactive Potentials of Food Proteins and Peptides)

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17 pages, 2057 KiB

Open AccessArticle

Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides

by Siriporn Chunkao, Wirote Youravong, Chutha T. Yupanqui, Adeola M. Alashi and Rotimi E. Aluko

Foods 2020, 9(10), 1406; https://0-doi-org.brum.beds.ac.uk/10.3390/foods9101406 - 03 Oct 2020

Cited by 19 | Viewed by 3004

Abstract

An iron-binding mung bean protein hydrolysate (MBPH) was prepared using a continuous enzymatic membrane reactor followed by peptide separation on anion-exchange (AEC) and reverse-phase HPLC (RP-HPLC) columns. Amino acid sequences of peptides present in the RP-HPLC fraction with the strongest iron-binding capacity were [...] Read more.

An iron-binding mung bean protein hydrolysate (MBPH) was prepared using a continuous enzymatic membrane reactor followed by peptide separation on anion-exchange (AEC) and reverse-phase HPLC (RP-HPLC) columns. Amino acid sequences of peptides present in the RP-HPLC fraction with the strongest iron-binding capacity were identified using mass spectrometry, and ten peptides of 5–8 amino acids synthesized for antioxidant characterization. Five fractions (AF1– AF5) with higher iron-binding capacity (88.86 ± 6.43 to 153.59 ± 2.18 mg/g peptide) when compared to the MBPH (36.81 ± 0.93 mg/g peptide) were obtained from AEC. PAIDL had the significantly (p < 0.05) highest iron-binding capacity, but LLLLG and LLGIL showed the strongest metal chelating activity. However, PAIDL (46.63%) and LLGIL (81.27%) had significantly (p < 0.05) better DPPH radical scavenging activity than the other peptides. PAIDL and LLGIL were also the most effective (p < 0.05) hydroxyl radical neutralizers with an effective concentration that scavenged 50% (EC₅₀) values of 0.09 and 0.37 mM, respectively. PAIDL and AIVIL showed the lowest EC₅₀ values of 0.07 mM each for superoxide radical scavenging activity. We conclude that short chain length in combination with leucine as the C-terminal amino acid residue contributed to the strong antioxidant properties of peptides in this study. Full article

(This article belongs to the Special Issue Advances in Functional and Bioactive Potentials of Food Proteins and Peptides)

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23 pages, 1342 KiB

Open AccessArticle

Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides

by Pei-Gee Yap and Chee-Yuen Gan

Foods 2020, 9(9), 1312; https://0-doi-org.brum.beds.ac.uk/10.3390/foods9091312 - 18 Sep 2020

Cited by 17 | Viewed by 4637

Abstract

Active fragments (bioactive peptides) from the chicken egg white proteins were expected to exert tyrosinase inhibitory activities in which skin hyperpigmentation could be prevented. Egg white was hydrolyzed by trypsin, chymotrypsin and the combination of both enzymes. The enzyme treatments achieved >50% degree [...] Read more.

Active fragments (bioactive peptides) from the chicken egg white proteins were expected to exert tyrosinase inhibitory activities in which skin hyperpigmentation could be prevented. Egg white was hydrolyzed by trypsin, chymotrypsin and the combination of both enzymes. The enzyme treatments achieved >50% degree of hydrolysis (DH) at substrate-to-enzyme (S/E) ratio of 10–30 (w/w) and hydrolysis time of 2–5 h. A crossed D-optimal experimental design was then used to determine the optimal enzyme composition, S/E ratio and hydrolysis time in order to yield hydrolysates with strong monophenolase and diphenolase inhibitory activities. The optimized conditions 55% trypsin, 45% chymotrypsin, S/E 10:1 w/w and 2 h achieved 45.9% monophenolase activity inhibition whereas 100% trypsin, S/E 22.13:1 w/w and 3.18 h achieved 48.1% diphenolase activity inhibition. LC/MS and MS/MS analyses identified the peptide sequences and the subsequent screening had identified 7 peptides (ILELPFASGDLLML, GYSLGNWVCAAK, YFGYTGALRCLV, HIATNAVLFFGR, FMMFESQNKDLLFK, SGALHCLK and YFGYTGALR) as the potential inhibitor peptides. These peptides were able to bind to H85, H94, H259, H263, and H296 (hotspots for active residues) as well as F92, M280 and F292 (stabilizing residues) of tyrosinase based on structure-activity relationship analysis. These findings demonstrated the potential of egg white-derived bioactive peptides as skin health therapy. Full article

(This article belongs to the Special Issue Advances in Functional and Bioactive Potentials of Food Proteins and Peptides)

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Review

Jump to: Research

21 pages, 762 KiB

Open AccessReview

Production, Purification, and Potential Health Applications of Edible Seeds’ Bioactive Peptides: A Concise Review

by Mrinal Samtiya, Sovon Acharya, Kush Kumar Pandey, Rotimi E. Aluko, Chibuike C. Udenigwe and Tejpal Dhewa

Foods 2021, 10(11), 2696; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10112696 - 04 Nov 2021

Cited by 16 | Viewed by 3452

Abstract

Edible seeds play a significant role in contributing essential nutritional needs and impart several health benefits to improve the quality of human life. Previous literature evidence has confirmed that edible seed proteins, their enzymatic hydrolysates, and bioactive peptides (BAPs) have proven and potential [...] Read more.

Edible seeds play a significant role in contributing essential nutritional needs and impart several health benefits to improve the quality of human life. Previous literature evidence has confirmed that edible seed proteins, their enzymatic hydrolysates, and bioactive peptides (BAPs) have proven and potential attributes to ameliorate numerous chronic disorders through the modulation of activities of several molecular markers. Edible seed-derived proteins and peptides have gained much interest from researchers worldwide as ingredients to formulate therapeutic functional foods and nutraceuticals. In this review, four main methods are discussed (enzymatic hydrolysis, gastrointestinal digestion, fermentation, and genetic engineering) that are used for the production of BAPs, including their purification and characterization. This article’s main aim is to provide current knowledge regarding several health-promoting properties of edible seed BAPs in terms of antihypertensive, anti-cancer, antioxidative, anti-inflammatory, and hypoglycemic activities. Full article

(This article belongs to the Special Issue Advances in Functional and Bioactive Potentials of Food Proteins and Peptides)

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17 pages, 1015 KiB

Open AccessReview

Peptide–Mineral Complexes: Understanding Their Chemical Interactions, Bioavailability, and Potential Application in Mitigating Micronutrient Deficiency

by Xiaohong Sun, Roghayeh Amini Sarteshnizi, Ruth T. Boachie, Ogadimma D. Okagu, Raliat O. Abioye, Renata Pfeilsticker Neves, Ikenna Christian Ohanenye and Chibuike C. Udenigwe

Foods 2020, 9(10), 1402; https://0-doi-org.brum.beds.ac.uk/10.3390/foods9101402 - 02 Oct 2020

Cited by 48 | Viewed by 5397

Abstract

Iron, zinc, and calcium are essential micronutrients that play vital biological roles to maintain human health. Thus, their deficiencies are a public health concern worldwide. Mitigation of these deficiencies involves micronutrient fortification of staple foods, a strategy that can alter the physical and [...] Read more.

Iron, zinc, and calcium are essential micronutrients that play vital biological roles to maintain human health. Thus, their deficiencies are a public health concern worldwide. Mitigation of these deficiencies involves micronutrient fortification of staple foods, a strategy that can alter the physical and sensory properties of foods. Peptide–mineral complexes have been identified as promising alternatives for mineral-fortified functional foods or mineral supplements. This review outlines some of the methods used in the determination of the mineral chelating activities of food protein-derived peptides and the approaches for the preparation, purification and identification of mineral-binding peptides. The structure–activity relationship of mineral-binding peptides and the potential use of peptide–mineral complexes as functional food ingredients to mitigate micronutrient deficiency are discussed in relation to their chemical interactions, solubility, gastrointestinal digestion, absorption, and bioavailability. Finally, insights on the current challenges and future research directions in this area are provided. Full article

(This article belongs to the Special Issue Advances in Functional and Bioactive Potentials of Food Proteins and Peptides)

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