Food Protein-derived Bioactive Peptides Research Articles

Potential of Food Protein-Derived Bioactive Peptides against Sarcopenia: A Comprehensive Review.

Sarcopenia is an age-related progressive muscle disorder characterized by accelerated loss of muscle mass, strength, and function, which are important causes of physiological dysfunctions in the elderly. At present, the main alleviating method includes protein supplements to stimulate synthesis of muscle proteins. Food protein-derived peptides containing abundant branched-chain amino acids have a remarkable effect on the improvement of sarcopenia. Understanding the underlying molecular mechanism and clarifying the structure-activity relationship is essential for the mitigation of sarcopenia. This present review recaps the epidemiology, pathogenesis, diagnosis, and treatment of sarcopenia, which facilitates a comprehensive understanding of sarcopenia. Moreover, the latest research progress on food-derived antisarcopenic peptides is reviewed, including their antisarcopenic activity, molecular mechanism as well as structural characteristics. Food-derived bioactive peptides can indeed alleviate/mitigate sarcopenia. These antisarcopenic peptides play a pivotal role mainly by activating the PI3K/Akt/mTOR and MAPK pathways and inhibiting the ubiquitin-proteasome system and AMPK pathway, thus promoting the synthesis of muscle proteins and inhibiting their degradation. Antisarcopenic peptides alleviate sarcopenia via specific peptides, which may be absorbed into the circulation and exhibit their bioactivity in intact forms. The present review provides a theoretical reference for mitigation and prevention of sarcopenia by food protein-derived bioactive peptides.

Food protein-derived bioactive peptides for the management of nutrition related chronic diseases.

Dietary intervention via modifications of dietary pattern or supplementations of naturally derived bioactive compounds has been considered as an efficient approach in management of nutrition related chronic diseases. Food protein-derived bioactive peptide is representative of natural compounds which show the potential to prevent or mitigate nutrition related chronic diseases. In the past decades, substantial research has been conducted concentrating on the characterization, bioavailability, and activity assessment of bioactive peptides. Although various activities of bioactive peptides have been reported, the activity testes of most peptides were only conducted in cells and animal models. Some clinical trials of bioactive peptides were also reported but only limited to antihypertensive peptides, antidiabetic peptides and peptides modulating blood lipid profile. Hereby, clinical evidence of bioactive peptides in management of nutrition-related chronic diseases is summarized in this chapter, which aims at providing implications for the clinical studies of bioactive peptides in the future.

Current Evidence on the Bioavailability of Food Bioactive Peptides.

Food protein-derived bioactive peptides are recognized as valuable ingredients of functional foods and/or nutraceuticals to promote health and reduce the risk of chronic diseases. However, although peptides have been demonstrated to exert multiple benefits by biochemical assays, cell culture, and animal models, the ability to translate the new findings into practical or commercial uses remains delayed. This fact is mainly due to the lack of correlation of in vitro findings with in vivo functions of peptides because of their low bioavailability. Once ingested, peptides need to resist the action of digestive enzymes during their transit through the gastrointestinal tract and cross the intestinal epithelial barrier to reach the target organs in an intact and active form to exert their health-promoting properties. Thus, for a better understanding of the in vivo physiological effects of food bioactive peptides, extensive research studies on their gastrointestinal stability and transport are needed. This review summarizes the most current evidence on those factors affecting the digestive and absorptive processes of food bioactive peptides, the recently designed models mimicking the gastrointestinal environment, as well as the novel strategies developed and currently applied to enhance the absorption and bioavailability of peptides.

The Potential of Food Protein-Derived Bioactive Peptides against Chronic Intestinal Inflammation.

Inflammation can cause various chronic diseases like inflammatory bowel diseases. Various food protein-derived bioactive peptides (BAPs) with anti-inflammatory activity have the potential to manage these diseases. The aim of this paper is to overview the mechanisms and the molecular targets of BAPs to exert anti-inflammatory activity. In this review, the in vitro and in vivo effects of BAPs on intestinal inflammation are highlighted. The mechanism, pathways, and future perspectives of BAPs as the potential sources of therapeutic treatments to alleviate intestinal inflammation are provided, including nuclear factor-κB, mitogen-activated protein kinase, Janus kinase-signal transducer and activator of transcription, and peptide transporter 1 (PepT1), finding that PepT1 and gut microbiota are the promising targets for BAPs to alleviate the intestinal inflammation. This review provides a comprehensive understanding of the role of dietary BAPs in attenuating inflammation and gives a novel direction in nutraceuticals for people or animals with intestinal inflammation.

Identification of immunomodulatory peptides from zein hydrolysates

Food protein-derived bioactive peptides have been recognized as a promising candidate for the development of functional foods or nutraceuticals. Peptides exhibiting antioxidant, anti-proliferative and anti-hypertensive activities have been characterized from corn proteins while the knowledge on the presence of immunomodulatory peptides in corn proteins is limited. The objective of this study was to identify the immunomodulatory peptides from corn proteins using interleukin 6 (IL-6) in human macrophage-like U937 cells as the marker. Results indicated that zein protein hydrolysate digested by thermolysin showed a high yield of peptides with potent activity, which was then used for further fractionation by RP-HPLC. We identified five peptides using LC–MS/MS, among which, peptide FLPFNQL showed the highest activity reducing IL-6 production by 57.7% ± 6.1%.

Egg and Soy-Derived Peptides and Hydrolysates: A Review of Their Physiological Actions against Diabetes and Obesity.

Type 2 diabetes and obesity are two chronic conditions associated with the metabolic syndrome and their prevalences are increasing worldwide. The investigation of food protein-derived bioactive peptides that can improve the pathophysiology of diabetes or obesity while causing minimal side effects is desired. Egg and soy proteins generate bioactive peptides with multiple biological effects, exerting nutritional and physiological benefits. This review focuses on the anti-diabetic and anti-obesity effects of egg- and soy-derived peptides and hydrolysates in vivo and in vitro relevant to these conditions. Studies using the intact protein were considered only when comparing the results with the hydrolysate or peptides. In vivo evidence suggests that bioactive peptides from egg and soy can potentially be used to manage elements of glucose homeostasis in metabolic syndrome; however, the mechanisms of action on glucose and insulin metabolism, and the interaction between peptides and their molecular targets remain unclear. Optimizing the production of egg- and soy-derived peptides and standardizing the physiological models to study their effects on diabetes and obesity could help to clarify the effects of these bioactive peptides in metabolic syndrome-related conditions.

Bioactive Properties of Maillard Reaction Products Generated From Food Protein-derived Peptides.

Food protein-derived peptides are promising food ingredients for developing functional foods, since various bioactive peptides are released from food proteins. The Maillard reaction, which plays an important role in most processed foods, generates various chemical components during processing. Although changes of amino acids or proteins and reduced sugars by the Maillard reaction have been studied extensively, such changes of peptides by the Maillard reaction are still not resolved enough. Since food protein-derived peptides are widely utilized in many processed foods, it deserves concern and research on the changes of peptides by the Maillard reaction in foods during processing or storage. This chapter initially overviewed food protein-derived bioactive peptides. Then, Maillard reaction products generated from peptides are discussed. We focused particularly on their bioactivities.

The potential of food protein-derived anti-inflammatory peptides against various chronic inflammatory diseases.

Inflammation is considered as one of the major causes for the initiation of various chronic diseases such as asthma, cancer, cardiovascular disease, diabetes, obesity, inflammatory bowel disease, osteoporosis and neurological diseases like Parkinson's disease. Increasing scientific evidence has delineated that inflammatory markers such as TNF-α, IL-1, IL-6, IL-8 and CRP and different transcription factors such as NF-κB and STAT are the major key factors that regulate these inflammatory diseases. Food protein-derived bioactive peptides have been shown to exhibit anti-inflammatory activity by inhibiting or reducing the expression of these inflammatory biomarkers and/or by modulating the activity of these transcription factors. This review aims to discuss various molecular targets and underlying mechanisms of food protein-derived anti-inflammatory peptides and to explore their potential against various chronic inflammatory diseases. © 2015 Society of Chemical Industry.

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

QSAR studies may help to better understand structural requirements for peptide bioactivity and therefore to develop potent BAPs.

Food protein-derived bioactive peptides in management of type 2 diabetes

Type 2 diabetes (T2D), one of the major common human health problems, is growing at an alarming rate around the globe. Alpha-glucosidase and dipeptidyl peptidase IV (DPP-IV) enzymes play a significant role in development of T2D. Hence, reduction or inhibition of their activity can be one of the important strategies in management of T2D. Studies in the field of bioactive peptides have shown that dietary proteins could be natural source of alpha-glucosidase and DPP-IV inhibitory peptides. The purpose of this review is to provide an overview of food protein-derived peptides as potential inhibitors of alpha-glucosidase and DPP-IV with major focus on milk proteins. Efforts have been made to review the available information in literature on the relationship between food protein-derived peptides and T2D. This review summarizes the current data on alpha-glucosidase and dipeptidyl peptidase IV inhibitory bioactive peptides derived from proteins and examines the potential value of these peptides in the treatment and prevention of T2D. In addition, the proposed modes of inhibition of peptide inhibitors are also discussed. Studies revealed that milk and other food proteins-derived bioactive peptides play a vital role in controlling T2D through several mechanisms, such as the satiety response, regulation of incretin hormones, insulinemia levels, and reducing the activity of carbohydrate degrading digestive enzymes. The bioactive peptides could be used in prevention and management of T2D through functional foods or nutraceutical supplements. Further clinical trials are necessary to validate the findings of in vitro studies and to confirm the efficiency of these peptides for applications.

Novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of goby (Zosterisessor ophiocephalus) muscle proteins

In recent years, food protein-derived bioactive peptides have received considerable attention because of their numerous health benefits. Amongst bioactive peptides, those with antihypertensive activity are receiving special attention due to their role in cardiovascular diseases. Goby protein hydrolysates (GPHs) prepared by treatment with five different crude bacterial proteases were found to exhibit varying degrees of angiotensin I-converting enzyme (ACE) inhibitory activity. The hydrolysate generated by the crude protease from Bacillus mojavensis A21, which displayed the highest ACE inhibitory activity, was further fractionated by size exclusion chromatography on a Sephadex G-25 and reversed-phase high performance liquid chromatography (RP-HPLC). The molecular masses and amino acid sequences of five peptides, in sub-fraction F5-2, which exhibited the highest ACE inhibitory activity, were determined using ESI-MS and ESI-MS/MS, respectively. The structures of these peptides were identified as Ala-Arg-Ser, Val-Val-Ala-Pro-Phe-Ala-His-Gly-Thr, Arg-Ser-Thr-Ala, Phe-Tyr-Pro-Pro, Arg-Cys-Ser-Ala-Gly-Val. Further, the sequences of fifteen peptides in the F5-4 sub-fraction, which exhibited high activity, were determined. Therefore, GPHs have a potential as hypotensive nutraceutical ingredients. Peptides find many outlets of application in the biotechnological field, amongst which are pharmaceutical applications. Progression amongst new small molecules deposited like substance medicamentous blows itself. In this context, large pharmaceutical companies invest in peptide research to open therapeutic new prospects. Even if they are used as therapeutic agents for nearly one century in their natural form, the use of peptides remains parsimonious although we experienced a significant development since a few tens of years, in particular thanks to the clarification of the methods of production, chemical in solid or biological phase such as in phage display. Peptides present many advantages compared to traditional drugs that have small molecules, Generation of bioactive peptides by proteolysis of food proteins, using exogenous proteases, is a new and interesting approach for the production and identification of new and potent specific hypotensive agents. From another side, compared with natural peptides isolated from different sources, there is more diversity in structure and mode of action of the derived bioactive peptides. In fact, proteolysis of protein substrates, having different amino acid composition and sequences, by proteases having different specificities may generate numerous specific peptide inhibitors, with different lengths and amino acid sequences. These bioactive peptides have received considerable attention for their effectiveness in both the prevention and the treatment of hypertension.