Agro-industrial by-products containing considerable amounts of protein (10-50%) such as soybean meal, rice bran and coconut pulp are promising bioactive peptide sources with annual disposal rate of 800 million tons in the world. More recently, plant by-products rich in protein content have been studied under various prisms that include recovery techniques, peptide production methods, determination of technological benefits and functional properties, and their applications in foods. The researches in bioactive peptides provide evidence over the techno-functional properties and the health benefits are highly dependent upon their amino acid sequences, molecular weights, conformations and surface properties. Research findings compared bioactive properties of the obtained peptides with respect to their amino acid sequences and also reported that hydrophobic/hydrophilic properties have direct effect on both functional and health effects. In addition, the resultant properties of the peptides could be affected by the conducted extraction method (alkaline, enzymatic, ultrasound assisted, microwave assisted, etc.), extraction solvent, precipitation and purification techniques and even by the final drying process (spray, freeze, vacuum, etc.) which may alter molecular weights, conformations and surface properties. Latest studies have investigated solubility, emulsifying, foaming, water/oil holding capacity and surface properties and also antioxidant, antimicrobial, anticarcinogenic, hypocholesterolemic, antihypertensive, immunomodulatory and opioid activities of bioactive peptides obtained from plant by-products. Moreover, the application of the bioactive peptides into different food formulations has been a recent trend of functional food development. These bioactive peptides' bitter taste and toxicity are possible challenges in some cases that need to be resolved before their wider utilization.Copyright © 2020 Elsevier Ltd. All rights reserved.

The prevalence of diabetes is growing worldwide with an increasing morbidity and mortality associated with the development of diabetes complications. Free radical production is a normal biological process that is strictly controlled and has been shown to be important in normal cellular homeostasis, and in the bodies response to pathogens. However, there are several mechanisms leading to excessive free radical production that overcome the normal protective quenching mechanisms. Studies have shown that many of the diabetes complications result from excessive free radical generation and oxidative stress, and it has been shown that chronic hyperglycemia is a potent inducer for free radical production, generated through several pathways and triggering multiple molecular mechanisms. An understanding of these processes may help us to improving our preventive or therapeutic strategies. In this review, the major molecular pathways involved in free radical generation induced by hyperglycemia are described.© 2018 Wiley Periodicals, Inc.

Low molecular weight peptides obtained from ultrafiltration (UF) of giant squid (Dosidicus gigas) muscle protein were studied for their antioxidative effects in different in vitro oxidative systems. The most potent two peptides, Asn-Ala-Asp-Phe-Gly-Leu-Asn-Gly-Leu-Glu-Gly-Leu-Ala (1307 Da) and Asn-Gly-Leu-Glu-Gly-Leu-Lys (747 Da), exhibited their antioxidant potential to act as chain-breaking antioxidants by inhibiting radical-mediated peroxidation of linoleic acid, and their activities were closer to highly active synthetic antioxidant, butylated hydroxytoluene. Addition of these peptides could enhance the viability of cytotoxic embryonic lung fibroblasts significantly (P<.05) at a low concentration of 50 microg/ml, and it was presumed due to the suppression of radical-induced oxidation of membrane lipids. Electron spin trapping studies revealed that the peptides were potent scavengers of free radicals in the order of carbon-centered (IC(50) 396.04 and 304.67 microM), hydroxyl (IC(50) 497.32 and 428.54 microM) and superoxide radicals (IC(50) 669.34 and 573.83 microM). Even though the exact molecular mechanism for scavenging of free radicals was unclear, unusually high hydrophobic amino acid composition (more than 75%) of giant squid muscle peptides was presumed to be involved in the observed activities.

Oxidative stress, inflammation, and hypertension are recognized risk factors for non-communicable diseases. Because of the preventable character of these factors, the searching of dietary compounds with counteracting effects against them would provide a new framework for the development of novel multifunctional foods or nutraceuticals. Lunasin is a naturally occurring soybean peptide with chemopreventive and anti-inflammatory properties. Upon oral intake, lunasin is susceptible to the action of digestive enzymes during its transit through gastrointestinal tract. In spite of its cleavage into smaller peptides, these fragments have been suggested to contribute on the health beneficial effects attributed to lunasin. To confirm this hypothesis, the multifunctionality of lunasin derived-fragments was investigated. In vitro, peptides corresponding to the N-terminal and central regions of lunasin were demonstrated to inhibit angiotensin converting enzyme and to scavenge peroxyl and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid (ABTS) radicals. Moreover, lunasin and fragments released during its gastrointestinal digestion exerted potent protective effects on cell viability and oxidative status in macrophages RAW264.7 challenged with chemicals tert-butylhydroperoxide and hydrogen peroxide. These peptides were also able to reduce the nitric oxide production in pro-inflammatory lipopolysaccharide-induced macrophages. These results confirm the promising role of lunasin and its derived-fragments as protective agents against oxidative damage and inflammation-associated diseases.Copyright © 2019 Elsevier Ltd. All rights reserved.

Open tetrapyrroles termed phycobilins represent the major photosynthetic accessory pigments of several cyanobacteria and some eukaryotic algae such as the Glaucophyta, Cryptophyta and Rhodophyta. These pigments are covalently bound to so-called phycobiliproteins which are in general organized into phycobilisomes on the thylakoid membranes.In this work we first briefly describe the physico-chemical properties, biosynthesis, occurrence, in vivo localization and roles of the phycobilin pigments and the phycobiliproteins. Then the potential applications and uses of these pigments, pigment-protein complexes and related products by the food industry (e.g., as LinaBlue® or the so-called spirulina extract used as coloring food), by the health industry or as fluorescent dyes are critically reviewed.In addition to the stability, bioavailability and safety issues of purified phycobilins and phycobiliproteins, literature data about their antioxidant, anticancer, anti-inflammatory, immunomodulatory, hepatoprotective, nephroprotective and neuroprotective effects, and their potential use in photodynamic therapy (PDT) are also discussed.Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.org.

We examined the angiotensin I-converting enzyme (ACE) inhibitory activity and antihypertensive effect of the hot water extract of wakame, Undaria pinnatifida. Ten dipeptides were isolated from the extract by several steps of chromatography, and their amino acid sequences were Tyr-His, Lys-Trp, Lys-Tyr, Lys-Phe, Phe-Tyr, Val-Trp, Val-Phe, Ile-Tyr, Ile-Trp, and Val-Tyr. Both single administration and repeated oral administration of synthetic Tyr-His, Lys-Tyr, Phe-Tyr, and Ile-Tyr significantly decreased blood pressure in spontaneously hypertensive rats.

C-Phycocyanin (C-PC), the major light harvesting biliprotein from Spirulina platensis is of greater importance because of its various biological and pharmacological properties. It is a water soluble, non-toxic fluorescent protein pigment with potent anti-oxidant, anti-inflammatory and anti-cancer properties. In the present study the effect of highly purified C-PC was tested on growth and multiplication of human chronic myeloid leukemia cell line (K562). The results indicate significant decrease (49%) in the proliferation of K562 cells treated with 50 microM C-PC up to 48 h. Further studies involving fluorescence and electron microscope revealed characteristic apoptotic features like cell shrinkage, membrane blebbing and nuclear condensation. Agarose electrophoresis of genomic DNA of cells treated with C-PC showed fragmentation pattern typical for apoptotic cells. Flow cytometric analysis of cells treated with 25 and 50 microM C-PC for 48 h showed 14.11 and 20.93% cells in sub-G0/G1 phase, respectively. C-PC treatment of K562 cells also resulted in release of cytochrome c into the cytosol and poly(ADP) ribose polymerase (PARP) cleavage. These studies also showed down regulation of anti-apoptotic Bcl-2 but without any changes in pro-apoptotic Bax and thereby tilting the Bcl-2/Bax ratio towards apoptosis. These effects of C-PC appear to be mediated through entry of C-PC into the cytosol by an unknown mechanism. The present study thus demonstrates that C-PC induces apoptosis in K562 cells by cytochrome c release from mitochondria into the cytosol, PARP cleavage and down regulation of Bcl-2.

Peptide toxins from venomous animals are natural resources with diverse biological functions and therapeutic potential towards human diseases. For venomous scorpions, many valuable peptide toxins have been discovered from Buthidae scorpions, but few works were done about non-buthidae scorpions. Here, we cloned and characterized the first disulfide-bridged toxin peptide St20 from the non-buthidae scorpion Scorpiops tibetanus. St20 has a putative 23-residue signal peptide, followed by a presumed 34-residue mature peptide including 8 cysteines. Sequence alignments and structural analysis suggested that St20 is a new member of α-KTx23 scorpion toxin subfamily with a conserved CSα/β structural fold. Functional studies showed that St20 inhibited human T lymphocyte surface marker CD69 expression and cytokine IL-2 secretion. Beside this, St20 inhibited two important pro-inflammatory factors TNF-α and IFN-γ secretion in the activated human T lymphocyte. Animal experiments showed that the delayed-type hypersensitivity response in rat autoimmune disease model was ameliorated in the present of peptide toxin St20. Together, our results showed that St20 is the first disulfide-bridged toxin peptide from the non-buthidae scorpion Scorpiops tibetanus with immunosuppressive and anti-inflammatory activities, suggesting that toxins from non-buthidae scorpions might be a new source of peptide drug discovery towards human diseases.Copyright © 2017 Elsevier Ltd. All rights reserved.

To clarify the antioxidant, anti-glycation and immunomodulatory capacities of fermented blue-green algae Aphanizomenon flos-aquae (AFA), hot aqueous extract suspensions made from 10% AFA were fermented by Lactobacillus plantarum AN7 and Lactococcus lactis subsp. lactis Kushiro-L2 strains isolated from a coastal region of Japan. The DPPH and O radical scavenging capacities and Fe-reducing power were increased in the fermented AFA. The increased DPPH radical scavenging capacity of the fermented AFA was fractionated to mainly < 3 kDa and 30-100 kDa. The increased O radical scavenging capacities were fractionated to mainly < 3 kDa. Anti-glycation activity in BSA-fructose model rather than BSA-methylglyoxal model was increased by the fermentation. The increased anti-glycation activity was fractionated to mainly 30-100 kDa. The NO concentration in the murine macrophage RAW264.7 culture media was high with the fermented AFA. The increased immunomodulation capacity was also fractionated to mainly 30-100 kDa. These results suggest that the fermented AFA is a more useful material for health foods and supplements.