pea protein

Journal of Food Science, 1973

Journal of Agricultural and Food Chemistry, 1998

The effect of bovine serum albumin (BSA) was investigated on the antioxidant activity of phenolic compounds, grape extracts, and red wines in a lecithin-liposome system oxidized at 37°C with copper. In the absence of BSA, the phenolic compounds inhibited hydroperoxide formation in decreasing order: ferulic acid, epicatechin, catechin, rutin, malvidin, caffeic acid, quercetin, and propyl gallate. Hexanal formation was inhibited in the following decreasing order: ferulic acid, epicatechin, catechin, malvidin, caffeic acid, quercetin, rutin, and propyl gallate. Gallic acid and delphinidin promoted hydroperoxide and hexanal formation. In the presence of 20% BSA, liposome oxidation was much slower. Ferulic acid followed by malvidin and rutin were the most efficient in inhibiting lipid and protein oxidation. Two grape extracts and two red wines inhibited hydroperoxide and hexanal formation more efficiently without BSA. With BSA, the red wines were more active than the grape extracts in inhibiting lipid oxidation but were not different in inhibiting protein carbonyls.

2018

Oxidative reactions in food systems during processing and storage constitute a significant problem that determines the nutritional and sensory qualities of the food product as well as the textural and functional properties. Proteins and lipids, as essential components of foods, are highly prone to oxidative degradation that results in undesired modifications in food systems. Although lipid oxidation as a topic has been given a widespread attention, protein oxidation and its consequences in foods have been studied relatively recently. In particular, co-oxidation of food proteins and lipids, in terms of their interactions within the complex mechanism of oxidative reactions, has been gathering interest only lately. The behavior of proteins from various food sources and technological pre-treatments as well as the outcomes of this behavior under oxidative conditions in the presence of lipids is a much required subject on which to focus both by academia and industry. This study investigat...

Journal of Agricultural and Food Chemistry, 2010

The amino acid composition and antioxidant activities of peptide fractions obtained from HPLC separation of a pea protein hydrolysate (PPH) were studied. Thermolysin hydrolysis of pea protein isolate and ultrafiltration (3 kDa molecular weight cutoff membrane) yielded a PPH that was separated into five fractions (F1-F5) on a C 18 reverse phase HPLC column. The fractions that eluted later from the column (F3-F5) contained higher contents hydrophobic and aromatic amino acids when compared to fractions that eluted early or the original PPH. Fractions F3-F5 also exhibited the strongest radical scavenging and metal chelating activities; however, hydrophobic character did not seem to contribute to reducing power of the peptides. In comparison to glutathione, the peptide fractions had significantly higher (p < 0.05) ability to inhibit linoleic acid oxidation and chelate metals. In contrast, glutathione had significantly higher (p < 0.05) free radical scavenging properties than the peptide fractions.

Oxidative stress due to the excess of radical oxygen species (ROS) contribute to the development of different diseases. The use of antioxidants may prevent the development of these diseases by counteracting ROS levels. There is an increasing interest in natural antioxidants as they are safer for consumers than synthetic antioxidants. In this work, reducing power, free radical scavenging and cellular antioxidant activities of chickpea peptides fractions have been investigated. Peptide sequences included in fractions with antioxidant activity were identified. Main sequences, ALEPDHR, TETWNPNHPEL, FVPH and SAEHGSLH, corresponded to legumin, the main seed protein. Most peptides contained histidine, which has shown antioxidant activity. Two peptides also included tryptophan and phenylalanine, in which the phenolic group could also serve as hydrogen donor. These results show that legumin is a source of antioxidant peptides of high interest for food and pharmaceutical industries to develop new nutraceuti-cals and functional foods.

Process Biochemistry, 2018

In this study, proteins from Thai brown rice (Khao Dawk Mali 105) were separated into albumin (2.18 %), globulin (3.98 %), glutelin (84.23 %), and prolamin (9.61 %) fractions, and were hydrolysed with various bromelain concentrations and hydrolysis times. Liquid chromatographyelectrospray ionization/mass spectrometry (LC-ESI-MS/MS) was conducted to assess the composition, molecular weight (MW) distribution, and sequence of the resulting peptides, and showed that most peptides have a MW below 2000 Da (60-70 %). Glutelin fraction hydrolysates exhibited the highest 2,2'-azino-bis 3-ethylbenzthiazoline-6-sulfonic (ABTS •+) radical-scavenging (0.69 ± 0.04 µM trolox) and copper chelating (4.12 ± 0.01 mg ethylenediaminetetraacetic acid; EDTA) activities, which was further fractionated into six fractions using reversed-phase highperformance liquid chromatography. The fourth fraction showed the highest ABTS •+ scavenging (1.08 ± 0.03 mM trolox) and copper chelating (5.00 ± 0.02 mg EDTA) activity. LC-MS/MS analysis revealed that the peptides with MW less than 1500 Da and hydrophobic or aromatic Nterminal residues, such as SPFWNINAHS, MPVDVIANAYR, VVYFDQTQAQA, and VEVGGGARAP, possibly contributed to the highest antioxidant activity in fourth fraction.

Current Research in Food Science, 2021

Preventing lipid oxidation, especially with the polyunsaturated fat-based products, is a major concern in sectors as agri-food and cosmetic. Even though the efficiency of synthetic antioxidants has been recognized, both consumers and manufacturers are looking for more innovative, healthy and quality products while rejecting synthetic additives due to their concern about safety, along with their environmental impact issues. In this context, plant biomass, which have shown to be rich in compounds, have raised interest for the isolation of novel naturally occurring antioxidants. Among their myriad of molecules, bioactive peptides, which are biologically active sequence of amino acid residues of proteins, seem to be of a great interest. Therefore, the number of identified amino acids sequences of bioactive peptides from plant biomass with potential antioxidant action is progressively increasing. Thus, this review provides a description of 129 works that have been made to produce bioactive peptides (hydrolysate, fraction and/or isolate peptide) from 55 plant biomass, along with the procedure to examine their antioxidant capacity (until 2019 included). The protein name, the process, and the method to concentrate or isolate antioxidant bioactive peptides, along with their identification and/or specificity were described. Considering the complex, dynamic and multifactorial physico-chemical mechanisms of the lipid oxidation, an appropriate in-vitro methodology should be better performed to efficiently probe the antioxidant potential of bioactive peptides. Therefore, the results were discussed, and perspective for antioxidant applications of bioactive peptides from plant biomass was argued.

International Journal of Food Science & Technology, 2008

Crude rice bran protein (CRBP) was prepared by alkaline extraction and then treated with 0.6 m HCl to remove phytic acid. The phytate-free rice bran protein (PFRBP) was hydrolysed with proteases M, N, S, P and pepsin under optimal conditions. Hydrolysates obtained from various hydrolysis periods were subjected to analysis for their degree of hydrolysis (DH) and functional properties. The hydrolysates were fractionated by reversed-phase column chromatography on Kaseigel ODS resin (120-140 lm) using a stepwise gradient of aqueous ethanol, and their activities were measured. The 40% ethanol fraction of protease P 4 h-hydrolysate was separated by successive reversed-phase high-performance liquid chromatography and the amino acid sequences of isolated antioxidative peptides were determined by a protein sequencer and matrix-assisted laser desorption ionisation-time of flight mass spectrometry. Crude rice bran protein had higher antioxidative activity than PFRBP, due to the presence of phytic acid. Phytate contents of rice bran, CRBP and PFRBP were 2.5%, 1.42% and 0%, respectively. The activity of PFRBP increased upon protease digestion. Protease M hydrolysates showed the highest DH, but the lowest antioxidative activity. Hydrolysates with DH below 10% had higher antioxidative activity than those above 20%. This result indicates that the antioxidative activity of the hydrolysates is inherent to their characteristics amino acid sequences of peptides depending on the protease specificities.

Free Radicals in Human Health and Disease, 2014

The search for natural antioxidants is an ongoing endeavour as an aid to combat the harmful effects of free radicals. Research advances in the past few decades have shown that, by controlled enzymatic hydrolysis, natural antioxidants can be produced from food proteins. In this chapter, the role of certain antioxidative peptides derived from food proteins is discussed in relation to their prospect in the prevention of oxidative stress. The molecular diversity of these food peptides is described together with their pharmacological effects and mechanisms of action in relation to antioxidation. The production of these peptides and the elucidation of their antioxidative peptides are also presented. Owing to their therapeutic potential, antioxidative peptides derived from food proteins can be incorporated as ingredients in functional foods, nutraceuticals and pharmaceuticals, where their biological activities may inhibit product oxidation or assist in the control and prevention of diseases induced by free radicals. However, further insightful research is needed to overcome certain scientific challenges and thereby increase and promote consumer acceptance of these natural antioxidants.

Polish Journal of Food and Nutrition Sciences

Hydrolysates were produced using Alcalase (AH), chymotrypsin (CH), pepsin (PH), and trypsin (TH), and also fluted pumpkin leaf protein isolate (FLI) as a substrate. AH had the lowest degree of hydrolysis (16.37%) but exhibited overall superior antioxidant and enzyme inhibitory properties. Therefore, it was fractionated by membrane ultrafiltration to give <1, 1-3, 3-5, 5-10, and >10 kDa peptide fractions. Gel permeation chromatography showed that the molecular weight of the FLI was 19.77 kDa and that of the hydrolysates was below 7.5 kDa. The hydrolysate peptides had a high content of hydrophobic amino acids but low levels of sulfur-containing amino acids, when compared to protein of FLI. Peptide sequence analysis showed that the hydrolysates consisted of dipeptides, tripeptides, and tetrapeptides with molecular weights below 500 Da. The hydrolysates were also stronger inhibitors of linoleic acid oxidation, α-amylase, α-glucosidase, and angiotensin converting enzyme (ACE) than FLI. Among the fractions, the <1 and 1-3 kDa were the most effective free radical scavengers and metal chelators in addition to their strong inhibitory activities against α-amylase, α-glucosidase, and ACE. We conclude that the AH and low molecular weight peptide fraction (<3 kDa) could find applications in formulating foods with various bioactive properties.