Application Of Bioactive Peptides Research Articles

Applications of Bioactive Peptides in Dermatology.

Applications of Bioactive Peptides in Dermatology.

Research Progress in The Application of Bioactive Peptides in Cosmeceutical Products

Consumer demand for natural source cosmeceutical products with protective and therapeutic functions has prompted the cosmeceutical industry to look for alternative active ingredients. Natural bioactive peptides have single or multifunctional biological properties, such as anti-aging, anti-inflammatory, antibacterial, antioxidant activities, etc., which can promote the improvement of skin health by providing specific physiological functions, and are ideal raw materials for the development of medicinal cosmetics. In this paper, the preparation and characterization methods of bioactive peptides were reviewed, and the bioactivities of peptides related to their potential cosmeceutical applications were introduced in detail, and the challenges and opportunities of developing bioactive peptide-based cosmeceutical formulations were expounded, so as to provide references for the application and commercial development of natural bioactive peptides in the field of medicinal cosmetics.

Exploration of Compost Soil for the Production of Thermo-Stable Bacillus Protease to Synthesize Bioactive Compounds through Soy Protein Hydrolysis

Application of bioactive peptides (BAPs) is promising due to their potential antimicrobial, antioxidant, agonistic, and ACE inhibition properties. To achieve a stable and active peptide at relatively high pH and temperatures by microbial fermentation, a wide variety of microorganisms need to be explored from diverse habitats, and compost is the excellent source. In an attempt to isolate potent protease-producing bacteria, gelatin-supplemented DM agar medium was used. Out of 140 pure cultures, initial protease production selects isolate D3L/1 (26 U/mL), and 16S rDNA sequencing confirmed it as Bacillus subtilis. Protease production was increased to 55.55 U/mL, with pH 7.5, 1% glucose, 1% casein, 1% ammonium sulfate, for 96 h of fermentation, at 37 °C under 140 rpm of shaking. Ion-exchange, and size-exclusion chromatography, 30 KDa protease was purified up to 4.1-fold (specific activity 3448.62 U/mL; 67.66% yield). The enzyme was active under broad temperatures (60 °C optimum), organic solvents, and pH variations. A total of 5% H2O2 can only reduce 40% of enzyme activity. However, 1 mM, Fe2+, and Cu2+ increased enzyme activity by five times. Soy hydrolysis (SPI) byD3L/1 protease produces bioactive compound (<3 KDa), which confirmed the peptide bond in the far UV region (205 nm, 215 nm, 225 nm, and 280 nm). The compound was ineffective towards Serratia marcescens but active against Escherechia coli (47%), Staphylococcus aureus (28%), and Pseudomonas aeruginosa (12%).

Bioactive peptides derived from fermented foods: Preparation and biological activities

Bioactive peptides (BAPs) with potential health benefits are gaining popularity as people become more health-conscious. Fermented foods are produced through the vigorous metabolic activities of numerous microorganisms, which convert macromolecules in the food matrix into bioactive components, including BAPs. Access to endogenous BAPs in fermented foods reduces costs while simplifying isolation steps and provides a high-quality direct source of BAPs. Fermented foods-derived BAPs have been shown to have antihypertensive, antioxidant, and antibacterial activities; however, there is a lack of information on the production of BAPs through fermented foods, and a large number of BAPs resources in fermented foods have not been effectively explored. Therefore, this review introduces the current research status, preparation methods, biological functions, and digestive stability of BAPs in fermented foods, followed by a discussion of the shortcomings in current research and future directions to provide a foundation for applications of BAPs in fermented foods in the food and pharmaceutical fields.

A review on the application of bioactive peptides as preservatives and functional ingredients in food model systems

The rising demand for health-promoting foods has led to the search for alternative, sustainable, and multifunctional peptide sources. Unconventional though promising sources such as agro-industrial wastes and by-products, insects, marine, and plant RuBisCo could be the future sources of bioactive peptides. Bioactive peptides derived from various proteins are biologically active regulators that can be used as food additives to prevent oxidation and microbial spoilage. Therefore, bioactive peptides have been applied to maintain the quality and microbial safety of food products. Besides, peptides can be used as functional ingredients to treat or prevent chronic and lifestyle diseases. The present review highlights the recent findings of alternative sources of bioactive peptides, technological improvements in bioactive peptides identification and isolation, and some obstacles to the widespread application and uses of bioactive peptides. Especially, the present review discusses the application of bioactive peptides in food model systems as food additives and functional ingredients. Novelty impact statement Recent research shows that high-quality unconventional proteins could be the future alternatives to animal proteins to derive bioactive peptides. Bioactive peptides not only play a significant role in human health but also prevent lipid oxidation and microbial growth in foods. Hence, protein hydrolysates and peptides can replace synthetic preservatives to extend the shelf life of food products. Innovative research dedicated to the purification, isolation, and application of bioactive peptides to foods could bring multiple benefits to consumers, food processors, nutraceutical industries, and other stakeholders.

Regulation of Feeding and Therapeutic Application of Bioactive Peptides

Regulation of Feeding and Therapeutic Application of Bioactive Peptides

A Review on Extraction, Characterization, and Applications of Bioactive Peptides From Pressed Black Cumin Seed Cake.

Plenty of black cumin cake was generated as a natural waste material after pressing the oil. Nigella sativa (black cumin) seeds and cakes are of precious nutritional value as they contain proteins, phenolics, essential amino acids, and bioactive compounds. Owing to their antioxidant properties, scientists and food manufacturers have extensively developed them. Notably, global awareness among consumers about the benefits of innovative food ingredients has been increased. Meanwhile, it has to be noted that vast amounts of cake by-products are not effectively utilized, which might cause economic loss and environmental consequences. This review aimed to highlight the antioxidant abilities, extraction, characterization, functional characteristics, and utilization of active peptides acquired from black seed oil cake. This overview would critically evaluate black seed cake proteins, plentiful in bioactive peptides that might be utilized as valuable additives in feed, food, pharmaceutical, and cosmetic industries. The addition of bioactive peptides to restrain the oxidation of fat-based products and preserve food safety is also addressed.

Chemistry and Biofunctional Significance of Bioactive Peptide Interactions with Food and Gut Components.

Food-derived bioactive peptides (BAPs) have gained significant interest as functional agents for developing food products with health benefits. To elucidate the underlying bioactivity mechanisms, current research investigates mostly the structure-activity relationship of native peptides. However, peptide structures are highly susceptible to chemical modifications, which can subsequently influence their physiological behaviors and bioactivities. This paper highlights the peptide structure modifications occurring with major food components during processing and the digestive environment of the gut as well as associated changes in peptide properties and biofunctions. Given the modification propensity of peptides, focus should be shifted toward characterizing the nature, biofunctions, gut activity, bioavailability, and safety of the modified peptides toward achieving pragmatic food applications of BAPs.

Structure-informed separation of bioactive peptides.

The application of proteomic and peptidomic technologies for food-derived bioactive peptides is an emerging field in food sciences. These technologies include the use of separation tools coupled to a high-resolution spectrometric and bioinformatic tools for prediction, identification, sequencing, and characterization of peptides. To a large extent, one-dimensional separation technologies have been extensively used as a continuous tool under different optimized conditions for the identification and analysis of food peptides. However, most one-dimensional separation technologies are fraught with significant bottlenecks such as insufficient sensitivity and specificity limits for complex samples. To address this limitation, separation systems based on orthogonal, multidimensional principles, which allow for the coupling of more than one analytical separation tool with different operational principles, provide a higher separation power than one-dimensional separation tools. This review describes the structure-informed separation and purification of protein hydrolyzates to obtain peptides with desirable bioactivities. PRACTICAL APPLICATIONS: Application of bioactive peptides in the formulation of functional foods, nutraceuticals, and therapeutic agents have increasingly gained scholarly and industrial attention. The bioactive peptides exist originally in protein sources and are only active after hydrolysis of the parent protein. Currently, several tools can be configured in one-dimensional or multidimensional systems for the separation and purification of protein hydrolyzates. The separations are informed by the structural properties such as the molecular weight, charge, hydrophobicity or hydrophilicity, and the solubility of peptides. This review provides a concise discussion on the commonly used analytical tools, their configurations, advantages and challenges in peptide separation. Emphasis is placed on how the structural properties of peptides assist in the separation and purification processes and the concomitant effect of the separation on peptide bioactivity.

Functions and Applications of Bioactive Peptides From Corn Gluten Meal.

Corn protein has been identified as an important source of bioactive peptides. Such peptides can be released during hydrolysis induced by proteolytic enzymes or microbial fermentation. Corn peptides have been found to exhibit different functions in vitro and in vivo such as antihypertensive, hepatoprotective, anti-obesity, antimicrobial, antioxidative, mineral-binding and accelerating alcohol metabolism. To date, 22 sequences of bioactive corn peptides have already been identified. There is an increasing commercial interest in the production of corn peptides with the purpose of using them as active ingredients, which may find use in the treatment of liver injury, hypertension, dental carries, oxidative stress, mineral malabsorption and obesity. These bioactive peptides may be used in formulation of functional foods, nutraceuticals, and natural drugs because of their health benefit effects.

Influence of peptide characteristics on their stability, intestinal transport, and in vitro bioavailability: A review.

In recent years, large amounts of peptides have been purified and characterized from food protein hydrolysates. Many of these peptides have been demonstrated to be of potential application as health-improving ingredients against plenty of disease conditions, such as cancer, inflammation, and cardiovascular disease. The real efficacy of functional application of these peptides depends on their stability, transport, and bioavailability in target tissues, which in turn depends on the peptides characteristics. Therefore, the characteristic-function parameters are crucial for peptides using as functional agents. This review article intends to summarize the effects of peptide characteristics, including molecular weight, charge and hydrophobicity, on their stability, intestinal transport, and in vitro bioavailability. PRACTICAL APPLICATIONS: In the near future, bioactive peptides will play important roles in the area of functional foods and pharmacy. However, the gastrointestinal digestion and transport usually restrict their bioavailability in vivo. Understanding the relationships between peptide characteristics and their digestion stability, bioavailability may provide guidance and theoretical basis for the further application of bioactive peptides.

Milk Protein Peptides With Angiotensin I-Converting Enzyme Inhibitory (ACEI) Activity

Bioactive peptides derived from milk proteins are currently of great scientific interest due to their beneficial health properties. The group of bioactive peptides most studied up until now are the angiotensin-I converting enzyme inhibitory (ACEI) peptides, which, when administered orally, seem to possess the capacity to lower blood pressure in hypertensive subjects. The various techniques of separation, identification, and classification of bioactive peptides obtained from milk and milk products, permit the selection of molecules with the highest level of health benefits to be used as a functional ingredient in the production of milk products with blood pressure-lowering effects such as Evolus® or Calpis®. This review focuses on the major research in the areas of isolation, identification, and application of bioactive peptides with ACEI activity in milk proteins, paying special attention to in vitro, in animal model systems, and in clinical studies of hypertensive patients.