The presence of bioactive peptides has already been reported in many foods such as milk, fermented products, plant and marine proteins. Bioactive peptides are sequences between 2 and 20 amino acids that can inhibit chronic diseases by modulating and improving physiological functions, so these peptides contribute in holding the consumer health. Also, bioactive peptides can affect pro-health or functional properties of food products. Fractionation of the protein hydrolysate revealed a direct relationship between their structure and functional activity. So, this review focuses on different factors effecting on bioactive peptide structures, biological and functional properties such as antihypertensive, antioxidative, hypocholesterolemic, water-holding capacity, foaming capacity, emulsifying properties and solubility. Also, this review looks at the identified bioactive peptides from food protein sources as potential ingredients of health promoting functional foods.

Bioactive food derived peptides: a review on correlation between structure of bioactive peptides and their functional properties

Background In recent years, the antioxidant capacity of plant protein-derived peptides has been depicted in a growing number of studies. Plant proteins have been considered as the new source of antioxidant peptides, which not only save energy but also strengthen treatment of oxidation-related diseases and delay the oxidation of food, thus improve the quality of life. Although reports of the preparation, structure, and activity of antioxidant peptides has increased tremendously and some antioxidant peptides have been commercialized. However, research on antioxidant peptides derived from plant proteins still lacks a systematic review and evaluation. Scope and approach This review summarizes recent advances in plant protein-derived antioxidant peptides, mainly including: (i) Preparation, purification, identification and application of plant protein-derived antioxidant peptides by enzymatic hydrolysis; (ii) Influencing factors, evaluation methods and mechanism of antioxidant protein hydrolysates or peptides; (iii) Future research prospects and existing problems. Key findings and conclusions The conventional purification and identification of antioxidant peptides are expensive and time-consuming. In order to overcome this problem, computer-aided mathematical models (molecular docking, QSAR research, etc.), bioinformatics tools and real-time updated protein databases have been widely explored and studied. In addition, future research should focus on large-scale commercial production of plant protein-derived antioxidant peptides, comprehensive study of structure-activity relationship of antioxidant peptides, deep understanding of antioxidant mechanism, and verification of health benefits in vivo. This review provides a timely reference for the development of new antioxidant peptides in functional foods and nutritional supplements.

Plant protein-derived antioxidant peptides: Isolation, identification, mechanism of action and application in food systems: A review

Green extraction methods are being developed using modern technology where less or no organic solvents are used to minimize environmental and health impacts and to maximize the yield of desired polyphenols by selective extraction. Advanced methods such as microwave assisted, ultrasound assisted, pulsed electric field assisted and enzyme assisted extractions, as well as pressurized liquid and supercritical fluid extractions are given more emphasis. The theory behind some advanced extractions methods is described. A brief review of applications of extractions from various parts of plants such as roots, fruits, seeds, leaves, vegetables, barks, etc. are provided.

Green extraction methods of food polyphenols from vegetable materials

Use of Alcalase in the production of bioactive peptides: A review.

Bioactive peptides derived from plant origin by-products: Biological activities and techno-functional utilizations in food developments - A review

Hydrolysates of wheat germ protein prepared with Alcalase, pepsin or proteinase K had significant antioxidant activities and the ability to decrease A549 cell viability in a concentration-dependent manner. Hydrolysates were fractionated using RP-HPLC and the antioxidant activity of fractions was evaluated as ABTS radical scavenging activity. Fractions with the highest activities were further analyzed using LC/ESI-MS/MS. Two peptides, KELPPSDADW and SSDEEVREEKELDLSSNE of the pepsin hydrolysates, three peptides, TVGGAPAGRIVME, VGGIDEVIAK and GNPIPREPGQVPAY of the Alcalase hydrolysates, and two peptides SGGSYADELVSTAK and MDATALHYENQK of the proteinase K hydrolysates were identified as the main components. Replicates of these peptides were made using solid phase synthesis and further biological activities, including antioxidant, ACE inhibitory and cytotoxic activities were evaluated. Peptides with the highest activities were KELPPSDADW (antioxidant), SGGSYADELVSTAK (ACE inhibitory) and SSDEEVREEKELDLSSNE (cytotoxic).

Antioxidant, anticancer and ACE-inhibitory activities of bioactive peptides from wheat germ protein hydrolysates

Food-derived bioactive peptides are being used as important functional ingredients for health-promoting foods and nutraceuticals in recent times in order to prevent and manage several diseases thanks to their biological activities. Bioactive peptides are specific protein fractions, which show broad applications in cosmetics, food additives, nutraceuticals, and pharmaceuticals as antimicrobial, antioxidant, antithrombotic, and angiotensin-I-converting enzyme (ACE)-inhibitory ingredients. These peptides can preserve consumer health by retarding chronic diseases owing to modulation or improvement of the physiological functions of human body. They can also affect functional characteristics of different foods such as dairy products, fermented beverages, and plant and marine proteins. This manuscript reviews different aspects of bioactive peptides concerning their biological (antihypertensive, antioxidative, antiobesity, and hypocholesterolemic) and functional (water holding capacity, solubility, emulsifying, and foaming) properties. Moreover, the properties of several bioactive peptides extracted from different foods as potential ingredients to formulate health promoting foods are described. Thus, multifunctional properties of bioactive peptides provide the possibility to formulate or develop novel healthy food products.

A Review on Health-Promoting, Biological, and Functional Aspects of Bioactive Peptides in Food Applications.

In present study, response surface methodology was used to optimize extraction condition of phenolic compounds from licorice root by microwave application. Investigated factors were solvent (ethanol 80 %, methanol 80 % and water), liquid/solid ratio (10:1–25:1) and time (2–6 min). Experiments were designed according to the central composite rotatable design. The results showed that extraction conditions had significant effect on the extraction yield of phenolic compounds and antioxidant capacities. Optimal condition in microwave assisted method were ethanol 80 % as solvent, extraction time of 5–6 min and liquid/solid ratio of 12.7/1. Results were compared with those obtained by soxhlet extraction. In soxhlet extraction, Optimum conditions were extraction time of 6 h for ethanol 80 % as solvent. Value of phenolic compounds and extraction yield of licorice root in microwave assisted (MAE), and soxhlet were 47.47 mg/g and 16.38 %, 41.709 mg/g and 14.49 %, respectively. These results implied that MAE was more efficient extracting method than soxhlet.

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Optimization of microwave assisted extraction (MAE) and soxhlet extraction of phenolic compound from licorice root

Wheat germ protein hydrolysate (WGPH) was obtained by proteinase K digestion, in order to produce bioactive antioxidant and antihypertensive peptides. Response surface methodology (RSM) was used to optimize hydrolysis conditions (enzyme-to-substrate ratio, time, and temperature) for antioxidant activity of hydrolysates. The crude WGPH produced in this way significantly inhibited angiotensin-I converting enzyme (ACE) in a concentration-dependent manner. It was next fractionated by reversed-phase semi-preparative High Performance Liquid Chromatography (HPLC) into 12 fractions that were examined for antioxidant and antihypertensive activities. Fractions with antioxidant and ACE-inhibitory activities were then submitted to further analysis by nano-LC-ESI-MS-MS. Among the various peptides identified, MDATALHYENQK (IC50 : 293.3 ± 6.5 µg/ml) and SGGSYADELVSTAK (IC50 : 265.5 ± 8.3 µg/ml) displayed antioxidant activity and VALTGDNGHSDHVVHF (IC50 : 189.3 ± 4.05 µg/ml), VDSLLTAAK (IC50 : 159.7 ± 0.33 µg/ml), MDATALHYENQK (IC50 : 303.6 ± 2.47 µg/ml), IGGIGTVPVGR (IC50 : 125.7 ± 2.3 µg/ml) and SGGSYADELVSTAK (IC50 : 128.2 ± 1.17 µg/ml) showed good ACE-inhibitory activity. PRACTICAL APPLICATIONS: Wheat milling industries produce massive amounts of wheat germ as by-product that can be converted into valuable compounds. The present research indicates that proteinase K is useful to hydrolyze wheat germ proteins in a search for bioactive peptides with antioxidant and ACE-inhibitory properties. The identified peptides can be regarded as functional food additives, or nutraceuticals to improve human health.

Z Karami

Papers

Bioactive food derived peptides: a review on correlation between structure of bioactive peptides and their functional properties

Antioxidant, anticancer and ACE-inhibitory activities of bioactive peptides from wheat germ protein hydrolysates

A Review on Health-Promoting, Biological, and Functional Aspects of Bioactive Peptides in Food Applications.

Optimization of microwave assisted extraction (MAE) and soxhlet extraction of phenolic compound from licorice root

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion