Active peptide is the general name of more than 1000 peptides (such as soybean peptide, deep-sea fish skin peptide, sea cucumber peptide, etc. are one of the active peptides).
Peptides are compounds of two or more amino acids linked by peptide bonds, which play an important physiological role in the human body and exert physiological functions.Active peptides are called active peptides, also called bioactive peptides or bioactive peptides.
Chinese name
Active peptide
Foreign name
Active Peptide
Overview
Peptides are two or more
Role
What does active peptide reduction do to human body
Active peptides play a key role in human growth and development, metabolism, disease, aging and death.Active peptides are the most important active substances in human body.It is precisely because of the increase or decrease of its secretion in the body that human beings have the cycle of infancy, childhood, adulthood, old age and death.The injection of active peptide breaks the cycle of life, thus achieving the magic effect of prolonging life and effectively slowing down aging.
Classification of active peptides
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Physiological peptide
Physiological active peptides are important chemical messengers to communicate information between cells and organs. Through endocrine and other ways of action, they enable the body to form a highly tight control system to regulate life processes such as growth, development, reproduction, metabolism and behavior.These peptides are generally called physiological active peptides.It mainly includes the following types:
Binding peptide
Most mineral element binding peptides contain phosphorylatedserineGroups and glutamyl residues, andMineral elementThe binding sites exist on the side of the negatively charged side chains of these amino acids, and the most obvious feature is that they contain phosphate groups.Phosphoric acid containing serine is required to combine with calciumGroupAnd the freedom of glutamic acidcarboxylGroup, this combination can enhance the solubility of mineral peptide complex.Casein phosphopeptide(CPP for short) is the most studied mineral element binding peptide at present. It can combine with a variety of mineral elements to form soluble organic phosphates, which act as many mineral elements such as Fe2+Mn2+、Cu2+、Se2+，In particular, the carrier of Ca2+transport in the body can promote the absorption of Ca2+and other mineral elements in the small intestine.
The casein phosphopeptides have serine phosphorylation structure in the molecule, and have significant absorption effect on calcium.It is the application of biotechnology fromMilk proteinNatural physiologically active peptide isolated from milkCaseinThere are two substances.The α - casein phosphopeptide made from α - casein is composed of 37 differentamino acidIt is composed of phosphopeptides, including 7 serines bound to phosphate groups,molecular weight46000.The β - casein phosphopeptide made from β - casein is a phosphopeptide composed of 25 different amino acids, including 5 serines bound to the phosphate group, with a molecular weight of 3100.Casein phosphopeptides are a group of 25-37Amino acid residueUnder the condition of pH 7 ～ 8, it can effectively form soluble complexes with calcium.
Phosphopeptide
Its physiological functions mainly include the following aspects:
(1) Promote the development of bones and teeth of growing children;
Japan, Australia, Germany, etc. have used it in functional foods, such as calcium and iron supplements added with casein phosphopeptides in Japan, including liquid drinks, fortified dairy products, biscuits, cakes, sweets, etc.In 1994, the large-scale industrial production of casein phosphopeptides was exclusively realized by Guangzhou Light Industry Research Institute in China. As the first mineral element binding peptide used in food, casein phosphopeptides are increasingly valued by people
Active peptide reagent
These peptides includeglutathione, incretin peptide, etc.Glutathione can be completely absorbed in the small intestine, and it can maintainErythrocyte membraneIt has the function of protecting and restoring the activity of enzymes that need sulfhydryl groups. It is a coenzyme orCofactor, can participate in the absorption and transport of amino acidsMethemoglobinOfReductionAnd promote the absorption of iron.
Glutathione (GSH) is produced byglutamate、CysteineandglycineadoptPeptide bondThe condensed tripeptide compounds are widely found in animal liver, blood, yeast, wheat germ, various vegetables, etcplant tissue It is also distributed in a small amount.Glutathione has unique physiological functions and is called longevity factor and anti-aging factor.Japan began to develop and apply to food in the 1950s, and has been widely used in the field of food processing.The research on glutathione in China is still in its infancy.The production methods of glutathione mainly includeSolvent extraction, chemical synthesis, microbial fermentation and enzyme synthesis, among which microbial cells or enzymes are usedbiosynthesisGlutathione has great development potential. At present, it is mainly produced by yeast fermentation.
(2) AsFree radical scavenger, which can protect the cell membrane from oxidative damage and preventred blood cellHemolysis and promote the reduction of methemoglobin.
(5) It can alleviate the discomfort caused by hypoxia, nausea and liver disease.
(6) PreventableSkin agingAnd pigmentation, reducingmelaninIt can improve the antioxidant capacity of the skin and make the skin shiny.
With the development of enzyme regulators andinhibitorWith the deepening of research, they play an increasingly important role in human health.
Antibacterial peptide
Also known as antibacterial peptides, it is usually associated with antibiotic peptides and antiviral peptides, including cyclic peptides, glycopeptides and lipopeptides, such asBacitracinBacitracinPolymyxin, lactic acid bactericide, subtilisin andNisinEtc.Antimicrobial peptides have good thermal stability and strong antibacterial effect.
Endogenous products can be produced by removing microorganisms, animals and plantsAntibacterial peptideIn addition, food protein can also be enzymatically hydrolyzed to obtain effective antimicrobial peptides, such aslactoferrinAntibacterial peptide obtained in.Lactoferrin is an iron binding glycoprotein. As a prototype protein, it is considered to be an important defense mechanism of host against bacterial infection.Researchers usePepsinSplit lactoferrin and purified three antibacterial peptides, which can act onEscherichia coli, both presentedcationForm.these ones hereBioactive peptideIt takes effect 30 minutes after contact with pathogenic bacteria, and is a good substitute for antibiotics.
neuropeptide
After enzymolysis, a variety of food proteins will produceNeuroactive peptide, such as the opioid active peptide derived from wheat glutenin, which is an in vitro pepsin andThermophilic proteaseHydrolysis products.
Neuroactive peptides include opioid active peptidesEndorphin、EnkephalinAnd other regulatory peptides.Neuroactive peptides play an important role in human beings. They can regulate human emotions, respiration, pulse, body temperature, etc. Unlike ordinary analgesics, they have no side effects.
Immune peptide
Immunoactive peptideCan stimulatemacrophageThis peptide is called immunoactive peptide.It can be divided into endogenous and exogenous immune active peptides.Endogenous immune active peptides includeinterferon、InterleukinAnd β - endorphin, which are the center of activating and regulating the immune response of the body.Exogenous immune active peptides mainly come from casein in human milk and cow milk.
Immunoactive peptides have many physiological functions. They can not only enhance the immune ability of the body, but also play an important role in immune regulation in animals;It can also stimulate the bodylymphocyteProliferation and enhancement ofMegaphilTo improve the body's resistance to external pathogens.
Flavoring peptide
Some active peptides can improve the palatability and flavor of food. We call these peptides flavoring peptides.
Sour peptide
Sour peptideIt is usually related to sour taste and Umami taste.Umami flavor hasSodium glutamateIt usually consists of dipeptide or tripeptide containing sodium glutamate and sodium aspartate.First time fromPapainThe octopeptide separated from the processed beef extract, called "delicious peptide", is the best example of Umami flavor.It is reported that delicious peptides have typical beef soup taste, which is mainly due to the synergistic effect of N-terminal dipeptide Lys Gly, central acidic tripeptide Asp Glu Glu and C-terminal tripeptide Ser Leu Ala.
Sweet peptide
Sweet peptideTypical representatives are dipeptide sweetener and alitame, which have the characteristics of good taste, high safety and low calorie.Among them, dipeptide sweetener has been approved by more than 70 countries for application in more than 500 kinds of food and drugs, which can be used to enhance theSweetness, adjust the flavor.In addition, lysine dipeptide has been proved to be an effective substitute for dipeptide sweetener. Its ester free functional characteristics make it more stable during food processing and storage.
Bitter peptide
Bitterness is that some foods, such as beer, coffeecheeseAnd other important taste components.Basic dipeptide such as ornithine-β - alanineGlutamic acid oligomers are often used as bitter ingredients in many foods.At present, researchers have isolated bitter peptides from fermented foods and enzymatic hydrolysates of casein.
Salty peptide
Some basic dipeptides, such as guanyltaurine hydrochloride and guanylyl - β - alanine hydrochloride, show strong salty taste, sometimes accompanied by Umami flavor.However, it was found that peptides are salt free in the absence of hydrogen chloride.It can be developed into a substitute for high sodium condiments.
Flavor enhancing peptides
somefood additivesAlthough the antibacterial effect is good, it will not produce residues in animals, so it is a safe and residue free antibiotic.However, its taste is too poor, and the palatability of food will be significantly reduced after adding food.Some dipeptides, such as Gly Leu, Pro Glu and Val Glu, can use their buffering effect to improve food palatability.The short chain glutamic acid polypeptide can effectively mask the bitterness.Curculin and Miraculin can mask sour taste and turn sour taste into sweet taste.In a word, some bioactive peptides can improve the palatability of food by simulating, masking and enhancing flavor.
Hormonal peptide
Hormone peptides includegrowth hormoneReleasing peptides, oxytocin, etc., produce a variety of physiological effects by acting as hormones or regulating hormone responses.Hormone peptide is a new synthetic peptide developed in the 1990sbiological activityPeptide, which has the biological activity of releasing growth hormone in animals.
Antioxidant peptide
Some food derived peptides have antioxidant effects, among which carnosine, a natural dipeptide, is the most familiar one.It is reported that antioxidant peptides can inhibithemoglobin, fatOxygenaseFatty rancidity catalyzed by singlet oxygen in vitro.In addition, several low molecular weight antioxidant peptides were identified from mushrooms, potatoes and honey, which can inhibitpolyphenol oxidaseIt can directly react with quinone products catalyzed by polyphenol oxidase to prevent the formation of polyoxide, thus preventing browning reaction of food.By removing heavy metal ions and promotingFree radicalOfperoxideAnd some antioxidant peptides andProteolytic enzymeIt can reduce the automatic oxidation rate and peroxide content of fat.
Nutritional peptide
For people or animalsGrowth and developmentPeptides with nutritional effects are called nutritional peptides.For example, free amino acids and peptides can be released by enzymolysis and digestion of proteins in the intestine.A large number of studies have shown that proteins and peptides have some special additional effects on animal growth in addition to supplying amino acids directly to animal body.The amount of free amino acid replacing complete protein is limited, and the production level of low protein diet cannot reach the production level of high protein diet in any case.The importance of protein in animal diets is partly reflected in the production of bioactive peptides in the small intestine.Peptidenutritive valueIt is higher than free amino acids and intact proteins for the following reasons:
1. Generally speaking, the antigenicity of small peptides is lower than that of large peptides or prototype proteins.
2. Compared with transporting free amino acids, the body transportsSmall peptideIt passes through the wall of the small intestine faster.
3. The osmotic pressure of peptides is lower than that of free amino acids, so it can improve the absorption efficiency of small peptides and reduce osmotic problems.
4. Small peptides also have good senses/Gustatory senseeffect.
At present, the research field of bioactive peptides has developed rapidly, and has been highly valued by scientists and governments all over the world. In just a few years, many bioactive peptides have been identified.Some active peptides have been industrialized as functional food.The research and development of bioactive peptides, as a new high-tech field in the world, has great market potential.
In addition, active peptides can also be used as drugs.At present, hundreds of peptide drugs have been produced, involving the clinical treatment of most diseases.for exampleinsulinIt has saved countless peoplediabetesPatient's life.In 2003, China broke outatypical pneumonia（SARS）。The Fourth Military Medical UniversityIn the research of anti SARS drugs, researchers found three polypeptides that have a clear inhibitory effect on SARS virus.This study on the inhibition of coronavirus has laid a solid foundation for the synthesis of a series of polypeptide drugs and the development of anti SARS drugs.These three peptides have been officially approved by the China Center for Disease Control and PreventionInstitute for Virus Disease Prevention and ControlIdentification of virus resource center.Researchers believe that SARS coronavirus is a single strandRiboseNucleic acid virus.In SARSpathogenAfter being identified, the researchers found that there was a "coronal" ring around SARS coronavirus, with four structural proteins inside, especiallyS proteinThe self replication and erosion of SARS virusHuman cellsThe polypeptide can prevent the coronavirus from invading the cells, thus inhibiting the coronavirus from invading the human cells.Experts said that there is no specific drug to treat SARS in the world, so this kind of polypeptide has a clear inhibitory effect on SARS coronavirus.On May 15, 2003,State Intellectual Property Office of ChinaThe patent application for this research achievement in China has been accepted.
Modern nutrition research has found that most of the proteins consumed by human beings are digested and absorbed in the form of low peptides after the action of enzymes in the digestive tract, and the proportion of absorption in the form of free amino acids is very small.Further experiments revealed that peptide digested faster and absorbed more than free amino acid, indicating that peptideBiological potencyAnd nutritional value is higher than free amino acids.This is also the infinite charm of active peptides.
Bioactive peptides are 20 proteinsNatural amino acidFromDipeptideA general term for different peptides with complex linear and circular structures, which are multifunctional compounds derived from proteins.Active peptides have a variety of human metabolism and physiological regulation functions, are easy to digest and absorb, have the functions of promoting immunity, hormone regulation, anti-bacterial, anti-virus, lowering blood pressure, lowering blood lipids, etc., and are extremely safe to eat. They are currently the most popular research topic and functional factors with great development prospects in the international food industry.[1]
Extraction method of active peptide
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There are two main methods of peptide extraction, one is chemical extraction, the other is physical extraction.Both have advantages and disadvantages. The "chemical extraction method" is mainly“Chemical enzymeReaction extraction method ".It has fast reaction and large production, but its disadvantage is that the extracted peptides have low activity. This method is the main source of peptide products on the market;The "physical extraction method" mainly refers to the "dielectric capacitance method active peptide extraction technology", which is characterized by slow reaction and small production, but the peptides produced have high activity.
Secretory cycle
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What are the secretion cycles of human bioactive peptides?
In different age periods, the secretion amount of various active peptides also varies greatly. According to the secretion amount, human life can generally be divided into:
① The period of sufficient secretion (youth before 25 years old): this period has balanced endocrine and strong immune function, and the human body is generally not prone to disease;
② Under secretion period (imbalance period) (30-50 years old adults and middle age). If the secretion of active peptides is insufficient or unbalanced, various related factors will appearSub health stateAnd mild disease symptoms (common among people over 40 years old);
③ Secretion deficiency period (severe deficiency period) (middle age and old age over 50 years old) This period is serious If the active peptide is seriously deficient and unbalanced, very prominent aging symptoms may appear, or various related diseases may occur (more obvious for people over 50 years old);
④ Secretion termination period (aging period): this period is very short, because the "commander" active peptide controlling human endocrine does not secrete or secretes less, which leads to cell function decline, organ function failure and loss, and finally leads to the end of life.
