Consumers’ awareness of the health promoting effects of functional food and nutritional health products is the driving force of the functional food and nutritional health products market.Bioactive peptides are known to have high tissue affinity, specificity and health-promoting efficiency.Therefore, the research on bioactive peptides derived from food is increasing exponentially.Over the years, many potential bioactive peptides from food have been documented;However, obstacles such as the need to establish optimal conditions for industrial-scale production and the lack of well-designed clinical trials to provide strong evidence of health claims remain.Other important factors such as the likelihood of allergens, cytotoxicity and the stability of peptides during gastrointestinal digestion need to be addressed.This review discusses our current understanding of the health effects, processing methods, and development challenges of bioactive peptides derived from foodstuffs.
The protein in food can serve as nutrient not only, still can rise to promote healthy physiology chemistry action.Most of the physiological activity of proteins is carried out by peptide sequences encoded in the parental proteins, which become active when cut completely.Bioactive peptides are released during enzymatic proteolysis of proteins (gastrointestinal digestion, in vitro hydrolysis using proteolytic enzymes) and during food processing (cooking, fermentation, ripening).Bioactive peptides are known to inhibit protein-protein interactions due to their small size and specificity.Nature remains the largest source of bioactive peptides because plants, animals, fungi, microorganisms and their products contain a variety of proteins.Over the years, bioactive peptides in food have been discovered by classical or bioinformatics methods.The classical method involves the hydrolysis of proteins by food-grade proteolytic enzymes to release many peptides from the hydrolysate.Alternatively, proteins can be fermented by bacteria.Bacterial proteolytic enzymes hydrolyze proteins to release peptides into the hydrolysate.The bioactivity of the hydrolysate was then tested in vitro.If the hydrolysates show good biological activity, they are confirmed by in vivo tests.Bioactive hydrolysates can then be developed into functional foods.Bioactive peptides from hydrolysis products can also be isolated and purified into nutritional health products for non-drug therapy.
Bioinformatics (computer modeling) methods, on the other hand, rely on information available in databases to determine the frequency of bioactive peptides identified in proteins of interest.Specific enzymes can be selected to hydrolyze peptides from segments identified by cleavage of parental proteins.This strategy enhances the identification of known peptides from unknown proteins.However, the key challenge in the development of bioactive peptides for therapeutic purposes is the difficulty in establishing a causal relationship between bioactive peptide consumption and its expected health effects on humans.However, as the therapeutic efficacy of bioactive peptides continues to be demonstrated, it is necessary to review the latest advances in bioactive peptides.In this review, we discuss recent advances in the production of bioactive peptides from food, including antidiabetic peptides, cholesterol-lowering peptides, antihypertensive peptides, anticancer peptides, antimicrobial peptides, and multifunctional peptides.We also discussed the impact of processing methods on the bioactivity of peptides and the challenges associated with the development of bioactive peptides.
- Challenges in Bioactive Peptide Development
Because bioactive peptides are encrypted in food, the degree of proteolysis during production is an indispensable factor to be considered.However, peptides released during fermentation and enzymatic proteolysis are still susceptible to further hydrolysis as long as the enzymatic reaction or fermentation process continues.This may result in a decrease or loss of biological activity due to the continuous degradation of the peptide.This makes it challenging to design dynamic models for proteolysis.
Moreover, peptides produced by microbial fermentation using wild microorganisms are not reproducible.This is because microorganisms are living cells and their metabolic activities, and the type and level of enzymes cannot be controlled.Therefore, the amount of specific bioactive peptides released after fermentation cannot be guaranteed.Therefore, modified strains or genetically recombinant strains or pure enzymes can help alleviate this challenge.At the same time, enzymes are more expensive for proteolysis than for microbial fermentation.In addition, bioactive peptides in food hydrolysates sometimes have improved activity due to their synergistic effects with other components in the hydrolysates.Therefore, when tested as a nutritional supplement alone, some isolated peptides may show reduced biological activity.
Another important challenge in the production of bioactive peptides is the stability of the resulting peptides.Most food-derived peptides are easily degraded in the gut and therefore do not show any activity in vivo when tested in vivo.In this case, by inserting the structure at the end of the inducing probe and also by splicing the peptide sequence, the purified peptide with good activity can be stabilized to prevent digestion.This stabilization strategy will improve bioavailability of the consumed peptides.
- Conclusions and Future Perspectives
Bioactive peptides in food are valuable functional drugs in healthy diet, which can prevent and cure diseases.Consumer awareness of the health effects of functional foods is a powerful driver of the search for and production of bioactive peptides in foods.Milk-derived tripeptide IPP and VPP are the most studied food-derived antihypertensive peptides and have shown positive effects in human studies.This ensures confirmation of bioactive peptides from other food sources in human studies.Many food hydrolysates also show multifunctional bioactivity effects, however, their composition is unknown.The identification of peptides in these hydrolysates is important for studying the mechanisms by which they exert their health effects.
The search for bioactive peptides by microbial fermentation will remain a promising and inexpensive strategy for the production of bioactive peptides in foods, as many peptides with different potentials are produced during fermentation in microbial proteolytic systems that are generally considered safe.In the near future, the development and use of genetically modified strains will become important because they release large amounts of proteolytic enzymes that hydrolyze food proteins.In addition, bioactive peptides derived from pure food will soon be sold in large quantities on the market and sold as nutritional health products.These peptides can be regulated as drugs because they are well characterized and their properties and mechanisms of action can be determined.
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