Porcine placenta enzymatic hydrolysate comprising novel peptide and composition for relieving hangovers comprising same

Abstract

The present invention relates to a porcine placenta enzymatic hydrolysate comprising a novel peptide and a composition for relieving hangovers comprising same. In addition, the porcine placenta enzyme hydrolysate prepared according to the present invention can exhibit excellent hangover-relieving efficacy even at a low dose. It can reduce blood alcohol and acetaldehyde concentrations, increase the activities of ADH and ALDH, and exhibit lipid peroxidation inhibitory and antioxidant effects. In addition, the composition according to the present invention can achieve an excellent hangover relief effect by using the porcine placenta enzymatic hydrolysate, betaine, and curcumin in combination.

Description

Porcine placenta enzyme hydrolysate containing a novel peptide and a hangover relief composition containing the same The present application claims priority to Korean Patent Application No. 10-2025-0015403 filed on February 6, 2025, and the entire specification is a reference to the present application. The present invention relates to a porcine placenta enzyme hydrolysate containing a novel peptide and a composition for relieving hangovers containing the same. The placenta is composed of blood chorionic membranes and maintains contact between the fetus and maternal tissues to supply the fetus with necessary oxygen and nutrients. It also plays a crucial role in removing waste products generated by the fetus. The placenta contains various nutrients and hormones essential for fetal growth, and porcine placenta is widely used in adults, particularly for alleviating menopausal symptoms and for cosmetic purposes. The placenta contains essential amino acids, melatonin, nucleic acid components such as RNA and DNA, and the antioxidant enzyme SOD (Superoxide Dismutase).

[0003] It is known to be useful for fatigue recovery and immune enhancement due to the presence of growth factors and cytokines such as oxide dismutase, hyaluronic acid, antioxidants, cytokines, placental peptides, insulin-like growth factor, epidermal growth factor (EGF), and senescent cell activating factor (SCAF). Furthermore, porcine placenta possesses high homology to the protein structure of the human placenta among mammalian placentas, and it has been reported to be a source of bio-active cytokines that govern cell differentiation and fetal development, serving as important components of proteins, various nutrients, DNA, and RNA. Due to these characteristics, porcine placenta is being applied in food and pharmaceuticals. However, despite these various benefits, there are limitations to the commercialization of porcine placenta hydrolysate. Porcine placenta hydrolysate faces difficulties in product development because a large amount must be consumed to demonstrate its efficacy (Korean Registered Patent No. 10-2252955). In addition, the salty taste and salinity are limitations as food compositions, and the salinity and color are also limitations as cosmetic products. Accordingly, since it is necessary to develop a manufacturing process that exhibits efficacy when the intake of porcine placenta hydrolysate is reduced, the present invention aimed to develop a manufacturing process that reduces the intake of porcine placenta hydrolysate while exhibiting excellent efficacy. The improved production process of the porcine placenta enzyme hydrolysate of the present invention maintains the quality of the porcine placenta enzyme hydrolysate compared to the existing patent (Korean Registered Patent No. 10-2252955), improves the saltiness and taste of the powder, and reduces the process cost by shortening the process time through the elimination of unnecessary processes during the manufacturing process. Meanwhile, a hangover refers to the physical and mental discomfort that occurs after excessive drinking. Hangovers develop the day after drinking or after a certain period of time has passed. Major symptoms known to include headaches, nausea, fatigue, thirst, dry mouth, and decreased concentration. Acetaldehyde produced by hangovers is highly toxic, and NAD+ (nicotinamide adenine dinucleotide) plays a crucial role in the metabolic process for its breakdown. NAD+ is involved in the action of enzymes essential for alcohol metabolism, such as alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH). NAD+ plays a vital role in cellular energy production (ATP synthesis) and DNA repair; as NAD+ and NADH are mutually convertible substances, their balance significantly influences cellular energy metabolism and redox reactions. When NAD+ is relatively higher or in balance, alcohol metabolism proceeds smoothly, acetaldehyde decreases rapidly, and hangover symptoms eventually resolve. Furthermore, hangovers are primarily attributed to acetaldehyde produced during the metabolism of alcohol (ethanol) and cell damage caused by oxidative stress. In this process, lipid peroxidation can act as an important physiological mechanism. Inhibiting lipid peroxidation is crucial for improving hangovers, and regulating it can alleviate hangover symptoms. Amino acids known to have hangover-relieving effects include L-cysteine, glutathione, arginine, methionine, alanine, glutamate, aspartic acid, glycine, histidine, serine, isoleucine, leucine, and valine. These amino acids play important roles in alcohol metabolism and are being studied for their potential to aid in the breakdown of acetaldehyde. (S. Choi, H. Kang. Alcoholism, (2015)) In particular, there are claims that specific amino acids, such as glycine, serine, and histidine, may be effective in relieving hangovers. (T. Nakamura, Journal of Nutrition, (2018)) Furthermore, there are numerous studies on how vitamins contribute to the alleviation of hangover symptoms. In particular, B vitamins (B1, B6, B12) are known to play an effective role in relieving alcohol-induced hangovers and have been reported to contribute to reducing symptoms such as fatigue, headache, and muscle pain (Jay DBB Voigt, a review of the literature (2015)). Additionally, it has been reported that vitamin C supplementation was effective in alleviating headache, nausea, and fatigue after a hangover (Kimberly SJ H, a randomized controlled trial (2014)). Curcumin, as the main component of turmeric and curcuma, is known for its various benefits, such as relieving hangovers, improving liver function, reducing muscle fatigue, increasing skin moisture, and acting as an antioxidant. It has been reported that beverages containing curcuma extract, when consumed with alcohol, reduce the "intoxication" inherent to alcohol to an appropriate level and have an effect of preventing the "be sick from drinking" (Takuya Hamano, Applied Pharmacology (2007)). The hackberry tree is also known as Jiguja, Hokkaenamu, and Horikkenamu. It is described in the Compendium of Materia Medica and the Dictionary of Chinese Medicine as being highly effective for alcohol-related symptoms such as hangover relief, alcohol poisoning, and bad breath, and it has been reported that hackberry fruit extract plays a role in helping to relieve hangovers (Park Eun-mi, Journal of the Korean Society of Food Culture (2006)). Puerariae radix is ​​known to have effects such as relieving hangovers, recovering from fatigue, quenching thirst, lowering blood pressure, preventing diarrhea, and protecting the stomach and intestines. As a result of conducting research on ingredients with excellent hangover relief effects, the inventors confirmed that porcine placenta enzyme hydrolysate is effective in relieving hangovers, and that the hangover relief effect is significantly superior when used in combination with betaine and curcumin, thereby completing the present invention. The present invention provides a porcine placenta enzyme hydrolysate containing a novel peptide. In addition, the present invention provides a food composition for relieving hangovers or a health functional food composition comprising a porcine placenta enzyme hydrolysate containing a novel peptide as an active ingredient. In addition, the present invention provides a pharmaceutical composition for relieving hangovers comprising a porcine placenta enzyme hydrolysate containing a novel peptide as an active ingredient. In addition, the present invention provides a food composition for relieving hangovers or a health functional food composition comprising porcine placenta enzyme hydrolysate, betaine, and curcumin as active ingredients. However, the technical problems that the present invention aims to solve are not limited to those mentioned above, and other unmentioned problems will be clearly understood by those skilled in the art from the description below. The present invention provides a porcine placenta enzyme hydrolysate containing the peptide of SEQ ID NO. 1. In addition, the present invention provides a food composition for relieving hangovers or a health functional food composition comprising a porcine placenta enzyme hydrolysate containing the peptide of SEQ ID NO. 1 as an active ingredient. In addition, the present invention provides a pharmaceutical composition for relieving hangovers comprising a porcine placenta enzyme hydrolysate containing the peptide of SEQ ID NO. 1 as an active ingredient. The above porcine placenta enzyme hydrolysate may include the peptide of SEQ ID NO. 1. The above peptide may be derived from porcine placenta enzyme hydrolysate. The above porcine placenta enzyme hydrolysate can lower blood alcohol and acetaldehyde. The above porcine placenta enzyme hydrolysate can increase the activity of ALD (alcohol dehydrogenase) and acetaldehyde dehydrogenase. The above porcine placenta enzyme hydrolysate may have an antioxidant effect that inhibits lipid peroxidation. The above porcine placenta enzyme hydrolysate can increase the NAD+ / NADH ratio. The above porcine placenta enzyme hydrolysate can suppress exhaled alcohol concentration after alcohol intake. The above porcine placenta enzyme hydrolysate can inhibit LDH. The above porcine placenta enzyme hydrolysate can inhibit apoptosis. The above porcine placenta enzyme hydrolysate can inhibit CYP2E1 gene expression. In addition, the present invention provides a food composition for relieving hangovers comprising porcine placenta enzyme hydrolysate, betaine, and curcumin as active ingredients. The above composition may further include one or more selected from the group consisting of vitamins, amino acids, and plant extracts. The above vitamins may include one or more selected from the group consisting of vitamin B1, niacin, pantothenic acid, vitamin B6, vitamin B12, and folic acid. The above amino acids may include one or more selected from the group consisting of taurine, arginine, aspartic acid, asparagine, methionine, glutamic acid, and alanine. The above plant extract may include one or more selected from the group consisting of red ginseng extract, Hovenia dulcis extract, Pueraria root extract, Pueraria flower extract, milk thistle extract, noni extract, acerola extract, and yeast extract. The above composition may be formulated into a formulation selected from the group consisting of tablets, capsules, powders, granules, jellies, liquids, and pills. In addition, the present invention may provide a food composition for relieving hangovers or a health functional food composition composed of a dual formulation (liquid and tablet). The liquid may include porcine placenta enzyme hydrolysate, betaine, and curcumin, and the tablet may include milk thistle extract, Hovenia dulcis fruit extract, kudzu root extract, and yeast extract. The above liquid may further include citric acid, taurine, L-asparagine, L-arginine, and vitamins, and the above tablet may further include L-asparagine, taurine, and vitamins. The vitamins contained in the above liquid may include vitamin B1, niacin, pantothenic acid, vitamin B6, vitamin B12, and folic acid, and the vitamins contained in the above tablet may include vitamin B2 and vitamin B1. The above liquid may further include one or more selected from the group consisting of citric acid, vitamins, amino acids, plant extracts, and sweeteners. The above vitamins may include one or more selected from the group consisting of vitamin B1, vitamin B2, niacin, pantothenic acid, vitamin B6, vitamin B12, and folic acid. The above sweetener may include one or more selected from the group consisting of fructose, glucose, honey, fructooligosaccharide, sucrose, aspartame, acesulfame potassium, sucralose, enzyme-treated stevia, pear concentrate, pineapple concentrate, apple concentrate, and grape concentrate. In addition, the present invention provides a use for relieving hangovers of a porcine placenta enzyme hydrolysate containing the peptide of SEQ ID NO. 1 or a composition containing the same as an active ingredient. In addition, the present invention provides a method for relieving a hangover comprising the step of administering to an individual a porcine placenta enzyme hydrolysate containing the peptide of SEQ ID NO. 1 or a composition containing the same as an active ingredient. In addition, the present invention provides a hangover relief use of a composition comprising porcine placenta enzyme hydrolysate, betaine, and curcumin as active ingredients. In addition, the present invention provides a method for relieving a hangover comprising the step of administering to an individual a composition containing porcine placenta enzyme hydrolysate, betaine, and curcumin as active ingredients. The porcine placenta enzyme hydrolysate prepared according to the present invention may include a novel peptide (Sequence No. 1). Furthermore, the porcine placenta enzyme hydrolysate prepared according to the present invention may exhibit excellent hangover relief efficacy even at low doses. Upon alcohol consumption, it may reduce blood alcohol and acetaldehyde concentrations, increase the activity of ADH and ALDH, and exhibit lipid peroxidation inhibition and antioxidant effects. It may also increase the NDA+ / NADH ratio and inhibit apoptosis genes. Additionally, the composition according to the present invention can achieve excellent hangover relief effects by using porcine placenta enzyme hydrolysate, betaine, and curcumin in combination. Figure 1 shows the LC-MS pattern of a porcine placenta enzyme hydrolysate according to one embodiment of the present invention. Figure 2 shows the LC / MS chromatograms of porcine placenta enzyme hydrolysate and synthetic peptide (GPOG) according to one embodiment of the present invention. Figure 3 shows the MS / MS chromatogram of porcine placenta enzyme hydrolysate and synthetic peptide (GPOG) according to one embodiment of the present invention. Figure 4 shows an LC / MS chromatogram of porcine placenta enzyme hydrolysate according to one embodiment of the present invention. Figure 5 shows the results of measuring changes in blood ethanol and acetaldehyde concentrations through the intake of porcine placenta enzyme hydrolysate (EPPH) according to one embodiment of the present invention (*p<0.05; **p<0.01; ***p<0.001). FIG. 6 shows the results of DPP and liver tissue H&E staining analysis following the ingestion of porcine placental enzyme hydrolysate (EPPH) according to one embodiment of the present invention: (A) DPPH Scavenging activity (*p<0.05; **p<0.01; ***p<0.001). (B) Liver tissue H&E staining (HDFE: Hovenia dulcis Fruit extract 67.2 mg / kg; EPPH: Porcine placenta enzymatic hydrolysate 22.70 mg / kg BW). FIG. 7 shows the results of confirming the lipid peroxidation inhibitory effect by porcine placenta enzyme hydrolysate (EPPH) according to one embodiment of the present invention (*p<0.05; **p<0.01; ***p<0.001). Figure 8 shows the results of analyzing the change in the NAD+ / NADH ratio in liver tissue by porcine placental enzyme hydrolysate (EPPH) according to one embodiment of the present invention (*p<0.05; **p<0.01; ***p<0.001). Figure 9 shows the action pathway of the phosphokinase array and EPPH (porn placental enzyme hydrolysate). Figure 10 is a graph showing the results of measuring blood alcohol concentration after consuming the compositions according to the examples and comparative examples. FIG. 11 is a photograph showing a dual-formulation hangover remedy according to one embodiment of the present invention. The present invention will be described in detail below. The present invention provides a porcine placenta enzyme hydrolysate containing a peptide composed of the amino acid sequence of SEQ ID NO. 1. The above peptide may be derived from porcine placenta enzyme hydrolysate. The above peptide may be included in the porcine placenta enzyme hydrolysate at a concentration of 1 to 15 mg / g. More preferably, it may be included at a concentration of 2.9 to 8.7 mg / g. If the peptide content is less than 1 mg / g, the peptide content is insufficient to produce an effect, and if the peptide content exceeds 15 mg / g, although the intake amount is high, it may not be a concentration that produces a greater effect. Accordingly, when the peptide content is in the range of 1 to 15 mg / g, it may be a concentration that produces the most optimal effect upon intake. The above porcine placenta enzyme hydrolysate may be hydrolyzed by one or more hydrolytic enzymes selected from the group consisting of papain, pronase, bromelain, and alkalase. More preferably, it may be hydrolyzed with papain. The above porcine placenta enzyme hydrolysate can reduce blood alcohol and acetaldehyde concentrations. The present invention can increase the activity of ADH and ALDH of porcine placenta enzyme hydrolysate. The above porcine placenta enzyme hydrolysate may have an antioxidant effect. The above porcine placenta enzyme hydrolysate can inhibit AST and ALT. The above porcine placenta enzyme hydrolysate can inhibit LDH. The above porcine placenta enzyme hydrolysate can suppress exhaled alcohol concentration. The above porcine placenta enzyme hydrolysate can increase the NAD+ / NADH ratio. The above porcine placenta enzyme hydrolysate can inhibit apoptosis. The above porcine placenta enzyme hydrolysate can exhibit lipid peroxidation inhibitory and antioxidant effects, and thereby provide hangover relief, improvement of alcohol-induced liver damage, improvement of fatigue, improvement of fatty liver, and / or anti-inflammatory effects. The above porcine placenta enzyme hydrolysate can increase the NDA+ / NADH ratio and thereby provide hangover relief, improvement of alcohol-induced liver damage, improvement of fatigue, improvement of fatty liver, recovery of muscle damage and improvement of exercise performance, and / or anti-inflammatory effects. The above porcine placenta enzyme hydrolysate can contribute to preventing or alleviating the progression of the disease by suppressing apoptosis gene expression. In addition, the present invention provides a method for preparing a porcine placenta enzyme hydrolysate comprising the peptide of SEQ ID NO. 1. The above porcine placenta enzyme hydrolysate (a) A step of crushing pig placenta from which foreign matter has been removed with a constant, adding 3% papain, and hydrolyzing for 20 hours; (b) a step of heating the hydrolysate to inactivate papain, then contacting it with a filtration aid and purifying it by filtration; (c) a step of adding ethanol to the filtrate of porcine placenta enzyme hydrolysate and using a filter to remove sugars, proteins, and impurities that are not sufficiently hydrolyzed; and (d) It can be manufactured by the step of concentrating the filtered liquid and then sterilizing it through a filter. The porcine placenta enzyme hydrolysate produced by the above manufacturing method improved the taste by reducing saltiness and salinity, thereby increasing the utility value of the powder, and lowered the production cost by reducing the production process time by eliminating unnecessary processes. More specifically, in the above manufacturing method, the deblowing solvent was changed to a constant, thereby reducing the saltiness and salinity of the porcine placenta enzyme hydrolysate powder and improving its taste, which increased the utility value of the powder. In addition, by eliminating the activated carbon process from the existing production process, the production process time was reduced and the production cost was lowered. By improving the quality of the porcine placenta enzyme hydrolysate through this process, the utility of the porcine placenta enzyme hydrolysate was increased. In addition, superior efficacy can be achieved with a lower dosage than that administered in existing patents. In addition, the porcine placenta enzyme hydrolysate produced by the above manufacturing method contains major components, and in particular, contains the novel peptide of SEQ ID NO. 1. In addition, the present invention provides a pharmaceutical composition for relieving hangovers comprising a porcine placenta enzyme hydrolysate containing a peptide composed of SEQ ID NO. 1 as an active ingredient. In addition, the present invention provides a food composition for relieving hangovers or a health functional food composition comprising a porcine placenta enzyme hydrolysate containing a peptide composed of SEQ ID NO. 1 as an active ingredient. In addition, the present invention provides a food composition for relieving hangovers or a health functional food composition comprising porcine placenta enzyme hydrolysate, betaine, and curcumin as active ingredients. The above composition may include 0.04 to 22 weight% of porcine placenta enzyme hydrolysate, 0.1 to 10 weight% of betaine, and 0.002 to 0.5 weight% of curcumin based on 100 weight% of the total composition. The above composition may further include one or more selected from the group consisting of vitamins, amino acids, and plant extracts. In the above composition, vitamins may be included in an amount of 0.01 to 20 weight%, amino acids in an amount of 0.01 to 30 weight%, and plant extracts in an amount of 0.01 to 50 weight%. The above vitamins may include one or more selected from the group consisting of vitamin B1, vitamin B2, niacin, pantothenic acid, vitamin B6, vitamin B12, and folic acid. The above composition may contain 0.01 to 10 wt% of vitamin B1, 0.01 to 10 wt% of vitamin B2, 0.01 to 10 wt% of niacin, 0.01 to 10 wt% of pantothenic acid, 0.01 to 10 wt% of vitamin B6, 0.0001 to 0.01 wt% of vitamin B12, and 0.001 to 0.2 wt% of folic acid. The above amino acids may include one or more selected from the group consisting of taurine, arginine, aspartic acid, asparagine, methionine, glutamic acid, and alanine. In the above composition, taurine may be included in an amount of 0.01 to 10 wt%, arginine in an amount of 0.01 to 20 wt%, aspartic acid in an amount of 0.01 to 20 wt%, asparagine in an amount of 0.01 to 15 wt%, methionine in an amount of 0.01 to 10 wt%, glutamic acid in an amount of 0.01 to 10 wt%, and alanine in an amount of 0.01 to 10 wt%. The above plant extract may include one or more selected from the group consisting of red ginseng extract, Hovenia dulcis extract, Pueraria root extract, Pueraria flower extract, milk thistle extract, noni extract, acerola extract, and yeast extract. In the above composition, red ginseng extract may be included in an amount of 0.01 to 5 wt%, Hovenia dulcis extract in an amount of 0.01 to 5 wt%, Pueraria root extract in an amount of 0.01 to 5 wt%, Pueraria flower extract in an amount of 0.01 to 5 wt%, milk thistle extract in an amount of 0.01 to 40 wt%, noni extract in an amount of 0.01 to 5 wt%, acerola extract in an amount of 0.01 to 5 wt%, and yeast extract in an amount of 0.01 to 10 wt%. The above composition may be formulated into a formulation selected from the group consisting of tablets, capsules, powders, granules, jellies, liquids, pills, and dual formulations (liquid and tablets). In addition, the present invention provides a food composition for relieving hangovers (a dual-formulation food composition) composed of a liquid (or liquid composition) and a tablet (or tablet composition), wherein the liquid comprises porcine placenta enzyme hydrolysate, betaine, and curcumin, and the tablet comprises milk thistle extract, Hovenia dulcis fruit extract, kudzu root extract, and yeast extract. Liquid (or liquid composition) in a dual formulation The above liquid composition may contain 0.04 to 3 weight% of porcine placenta enzyme hydrolysate, 0.1 to 10 weight% of betaine, and 0.002 to 0.5 weight% of curcumin, based on 100 weight% of the total liquid composition. The above liquid composition may further include one or more selected from the group consisting of citric acid, vitamins, amino acids, plant extracts, and sweeteners, or may further include one or more selected from the group consisting of citric acid, taurine, L-asparagine, L-arginine, and vitamins. In the above liquid composition, citric acid may be included in an amount of 0.1 to 7.5 wt%, taurine in an amount of 0.04 to 10 wt%, L-asparagine in an amount of 0.02 to 10 wt%, L-arginine in an amount of 0.2 to 20 wt%, and vitamins in an amount of 0.1 to 5 wt%. The vitamins included in the above liquid may include one or more selected from the group consisting of vitamin B1, vitamin B2, niacin, pantothenic acid, vitamin B6, vitamin B12, and folic acid. The above liquid composition may contain 0.01 to 1 wt% of vitamin B1, 0.01 to 1 wt% of vitamin B2, 0.01 to 1 wt% of niacin, 0.01 to 1 wt% of pantothenic acid, 0.01 to 1 wt% of vitamin B6, 0.0001 to 0.001 wt% of vitamin B12, and 0.001 to 0.2 wt% of folic acid. The above sweetener may include one or more selected from the group consisting of fructose, glucose, honey, fructooligosaccharide, sucrose, aspartame, acesulfame potassium, sucralose, enzyme-treated stevia, pear concentrate, pineapple concentrate, apple concentrate, and grape concentrate. Tablet (or tablet composition) in a dual formulation In the above tablet, based on 100% by weight of the total tablet, milk thistle extract may be included in an amount of 1 to 40% by weight, Hovenia dulcis fruit extract in an amount of 0.1 to 2% by weight, kudzu root extract in an amount of 0.1 to 1% by weight, and yeast extract in an amount of 0.1 to 10% by weight. The above tablet may further include one or more selected from the group consisting of L-asparagine, taurine, and vitamins. In the above tablet, L-asparagine may be included in an amount of 0.1 to 15 weight%, taurine in an amount of 0.1 to 5 weight%, and vitamins in an amount of 0.1 to 20 weight%. The above vitamin may include one or more selected from vitamin B2 or vitamin B1. In the above tablet, vitamin B2 may be included in an amount of 0.1 to 10 weight% and vitamin B1 in an amount of 0.1 to 10 weight%. In the present invention, the term "health functional food" refers to a food manufactured and processed in the form of tablets, capsules, powders, granules, liquids, pills, etc., using raw materials or ingredients that possess functional properties useful to the human body. Here, "functional properties" means obtaining effects useful for health purposes, such as regulating nutrients or physiological actions regarding the structure and function of the human body. The food or health functional food of the present invention may be manufactured by methods commonly used in the industry, and may be manufactured by adding raw materials and ingredients commonly added in the industry. Furthermore, the formulation of the food or health functional food may be manufactured without restriction as long as it is a formulation recognized as a food or health functional food. Unlike general pharmaceuticals, the food or health functional food composition of the present invention uses food as a raw material, which has the advantage of not causing side effects that may occur with long-term use of pharmaceuticals, and is highly portable, allowing it to be consumed as an adjuvant to enhance the effects of preventing or improving hangovers. The formulation of a food or health functional food can be in the form of powder, granule, pill, tablet, or capsule, as well as any form of general food or beverage. There are no specific restrictions on the types of food mentioned above, and examples of food to which the substance may be added include meat, sausage, bread, chocolate, candy, snacks, confectionery, pizza, ramen, other noodles, chewing gum, dairy products including ice cream, various soups, beverages, tea, drinks, alcoholic beverages, and vitamin complexes, and may include all food in the conventional sense. Generally, when manufacturing food or beverages, the above active ingredient may be added in an amount of 15 parts by weight or less, preferably 10 parts by weight or less, per 100 parts by weight of raw material. However, in the case of long-term consumption for the purpose of health and hygiene or health control, the above amount may be less than the above range, and furthermore, since the present invention uses fractions from natural products, there is no problem in terms of safety, so it may be used in an amount greater than the above range. Among the functional foods according to the present invention, the beverage may contain various flavoring agents or natural carbohydrates as additional ingredients, as in conventional beverages. The natural carbohydrates described above may be monosaccharides such as glucose and fructose, disaccharides such as maltose and sucrose, polysaccharides such as dextrin and cyclodextrin, and sugar alcohols such as xylitol, sorbitol, and erythritol. As sweeteners, natural sweeteners such as taumatin and stevia extract, or synthetic sweeteners such as saccharin and aspartame may be used. The proportion of the natural carbohydrates may be about 1 to 15 g, preferably about 3 to 8 g, per 100 mL of the beverage according to the present invention. In addition to the above, the food or health functional food composition according to the present invention may contain various nutritional agents, vitamins, electrolytes, flavoring agents, coloring agents, pectic acid and its salts, alginic acid and its salts, organic acids, protective colloidal thickeners, pH adjusters, stabilizers, preservatives, glycerin, alcohol, and carbonating agents used in carbonated beverages. Furthermore, the health functional food composition of the present invention may contain fruit pulp for the production of natural fruit juices, fruit juice beverages, and vegetable beverages. These ingredients may be used independently or in combination. The proportion of these additives is not limited, but is generally selected in the range of 0.01 to 0.1 parts by weight per 100 parts by weight of the functional food composition of the present invention. The pharmaceutical composition according to the present invention does not have a particularly limited content of the active ingredient as long as it contains the active ingredient, but preferably, the active ingredient may be included in an amount of 5 to 30 weight % with respect to the total weight of the composition. However, it is not limited thereto. In this case, if the active ingredient is below the concentration range, there is a problem in that it is difficult to exert a desirable preventive or therapeutic effect, and if it exceeds the concentration range, the change in the expected effect may be negligible. The pharmaceutical composition according to the present invention may be formulated and used in the form of oral formulations such as powders, granules, tablets, capsules, suspensions, emulsions, syrups, and aerosols, external formulations, suppositories, and sterile injectable solutions according to conventional methods, and may include a suitable carrier, excipient, or diluent that is conventionally used in the manufacture of pharmaceutical compositions for formulation. The above-mentioned carrier, excipient, or diluent may include various compounds or mixtures including lactose, dextrose, sucrose, sorbitol, mannitol, xylitol, erythritol, maltitol, starch, acacia gum, alginate, gelatin, calcium phosphate, calcium silicate, cellulose, methyl cellulose, microcrystalline cellulose, polyvinylpyrrolidone, water, methylhydroxybenzoate, propylhydroxybenzoate, talc, magnesium stearate, and mineral oil. When formulating, it can be manufactured using diluents or excipients such as commonly used fillers, weights, binders, wetting agents, disintegrants, and surfactants. A solid dosage form for oral administration can be prepared by mixing at least one excipient, such as starch, calcium bonate, sucrose or lactose, gelatin, etc., with the above-mentioned jasmon. In addition to simple excipients, lubricants such as magnesium stearate and talc may also be used. Liquid formulations for oral administration include suspensions, liquid formulations, emulsions, syrups, etc., and may contain various excipients, such as humectants, sweeteners, flavorings, and preservatives, in addition to commonly used simple diluents like water and liquid paraffin. The dosage of the active ingredient included in the pharmaceutical composition according to the present invention varies depending on the patient's condition, body weight, severity of the disease, drug form, route of administration, and duration, but can be appropriately selected by a person skilled in the art. The general dosage of the active ingredient included in the pharmaceutical composition of the present invention may be administered in the range of 0.0001 to 2,000 mg / kg / day for adults, preferably within the range of 0.001 to 1,000 mg / kg / day. The administration may be performed once a day or divided into several doses. However, the scope of the present invention is not limited by the above dosage. The present invention will be explained in more detail below through examples. The purpose, features, and advantages of the present invention will be easily understood through the following examples. The present invention is not limited to the examples described herein and may be embodied in other forms. The examples introduced herein are provided to ensure that the concept of the present invention is sufficiently conveyed to those skilled in the art to which the present invention pertains. Therefore, the present invention should not be limited by the following examples. Example 1. Preparation of porcine placenta enzymatic hydrolysate After thawing the pig placenta in a thawing machine and removing impurities with tap water, the placenta was placed in a meat tenderizer to tenderize it, facilitating blood removal. Subsequently, the pig placenta was washed several times with water to remove the blood, and then crushed to facilitate hydrolysis. 3% of a proteolytic enzyme (papain) was added to the pig placenta prepared as described above, and hydrolysis was carried out for 20 hours. After hydrolysis was complete, the proteolytic enzyme was inactivated by heating, and after cooling, the pig placenta enzyme hydrolysate was brought into contact with a filtration aid and filtered for purification. Subsequently, ethanol was added to the filtrate of the pig placenta enzyme hydrolysate and stirred, and then impurities were removed using a filter. The filtered liquid was concentrated, and the liquid was sterilized by sterilizing it through a 0.2㎛ filter. The sterilized liquid was freeze-dried to obtain the final freeze-dried pig placenta enzyme hydrolysate powder. Example 2. Preparation of a liquid composition for hangover relief A liquid hangover remedy was prepared by homogeneously mixing the compositions of Table 1 below and sterilizing them. Porcine placenta enzyme hydrolysate was prepared and used according to Example 1, and other ingredients were purchased from a domestic food ingredient supplier. Content (Weight%) Porcine placenta enzyme hydrolysate 1.1% Water-soluble curcumin (Curcumin content 12%) 0.5% Betaine 3.5% Crystalline fructose 5% Citric acid 3.7% Vitamin B1 nitrate 0.39% Niacinamide 0.19% Calcium pantothenate 0.34% L-arginine 5% L-asparagine 0.3% Milk thistle extract powder 1% Red ginseng extract 0.1% Yeast extract 0.1% Purified water Remaining amount Total (Weight%) 100% Example 3. Preparation of a dual-formulation hangover remedy A dual-formulation hangover remedy was prepared with the composition shown in Table 2 below. The liquid formulation was prepared by homogeneously mixing the composition and sterilizing it, and the tablets were prepared by mixing and then using a tablet press. Porcine placenta enzyme hydrolysate was prepared and used according to Example 1, and other ingredients were purchased from a domestic food ingredient supplier. Ingredient Content (Weight%) Liquid Porcine Placenta Hydrolyzed Powder 1,100 Betaine 3,500 Water-soluble Curcumin (Curcumin content 12%) 0.500 Citric Acid 3,700 Taurine 1,000 L-Asparagine 0.500 L-Arginine 5,000 Vitamin B6 Hydrochloride 0.5 Calcium Pantothenate 0.5 Niacinamide 0.1 Vitamin B1 Nitrate 0.1 Vitamin B12 (0.1%) 0.1 Folic Acid 0.00 1 Purified Water Remaining Total (Weight%) 100.00 Tablet 1 Milk Thistle Extract Powder 28,400 Vitamin B2 2 Vitamin B1 Nitrate 3 Hovenia dulcis fruit extract powder 1,000 Kudzu root extract powder 0.500 Yeast extract 1L - Asparagine 2 Taurine 0.500 Crystalline cellulose 12 Silicon dioxide 1,000 Magnesium stearate 1,000 HPMC 1,000 Glucose Remaining Total (Weight%) 100.00 HPMC: hydroxypropyl methylcellulose Experimental Example 1. Analysis of porcine placenta enzyme hydrolysate Experimental Example 1-1. Analysis of Indicator Amino Acids in Porcine Placenta Enzymatic Hydrolysate In order to confirm the characteristics of the porcine placenta enzyme hydrolysate prepared according to Example 1, the inventors conducted an experiment to analyze the amino acid content and HPLC pattern of the prepared porcine placenta enzyme hydrolysate. Table 3 shows the total amino acid content (mg / g) of porcine placenta enzyme hydrolysate confirmed by analysis, and the content of indicator amino acids leucine and isoleucine among them. Results of Amino Acid Analysis of Porcine Placenta Enzymatic Hydrolysate Batch 1 Batch 2 Batch 3 Average Total Amino Acids (mg / g) 195.3 188.9 213.3 199.2 L-Isoleucine (mg / g) 10.04 10.6 310.4 10.36 L-Leucine (mg / g) 22.7 323.4 22.2 22.79 Experimental Example 1-2. Confirmation of a Novel Peptide The porcine placenta enzyme hydrolysate obtained in Example 1 was mixed with 500 µl of purified water added to 500 µl of the sample, and the filtered liquid was centrifuged to transfer the supernatant (100 µl) to a vial and sequenced using a MicroQ-TOF III mass spectrometer (Bruker Daltonics, 255748 Germany). <Analysis Conditions> - Column: Poroshell 120 EC-C18 (2.1 - Flow rate: 200 µl / min - Lee Dong-sang: Mobile phase A: H2O / FA ​​= 100 / 0.1 (v / v), Mobile phase B: Acetonitrile / FA = 100 / 0.1 (v / v) StepTime(min)Flow Rate(μl / min)A(%)B(%)00200982152009822252007030327200595437200595539200982655200982 As a result of the above analysis, a total of six peptides were identified (Fig. 1, Table 5). Peptide and Amino Acid Sequences in Porcine Placenta Enzymatic Hydrolysate No. m / zRT (min) Charge Sequence Remarks 1343.161.71 GPOGG:glycine(Gly) P:proline(Pro) O:hydroxyproline(Hyp) G:glycine(Gly) PEP-1 (Sequence No. 1) 2357.214.21 Q*LKQ* : Pyroglutamic Acid from Glutamine 3440.219.61 GPOGPO : hydroxyproline (Hyp) 4380.1910.71 5399.23121 6445.2612.91 Experimental Example 1-3. Verification of Peptide To verify the above PEP-1 peptide, a peptide verification test was conducted to confirm that the peptide synthesized by Anigen matches the peptide present in porcine placenta enzyme hydrolysate. 1) Verification of PEP-1 (GPOG) in porcine placenta enzymatic hydrolysate In the case of PEP-1, the peptide within the porcine placenta enzyme hydrolysate was verified using two methods. As the first method, the chromatograms of the porcine placenta enzyme hydrolysate and the synthetic peptide (GPOG) were analyzed. The chromatograms were examined by spiking the porcine placenta enzyme hydrolysate (A), the peptide (GPOG) (B), and the synthetic peptide (C) onto the porcine placenta enzyme hydrolysate. As a result, the porcine placenta enzyme hydrolysate and the synthetic peptide were identified as having the same peak. Thus, it was confirmed that the porcine placenta enzyme hydrolysate contains the GPOG peptide (PEP-1) (Fig. 2). As a second method, the MS / MS patterns of porcine placenta enzyme hydrolysate and peptide (GPOG) were examined. As a result, the MS / MS pattern of the porcine placenta enzyme hydrolysate matched the MS / MS pattern of the peptide (GPOG), confirming that the porcine placenta enzyme hydrolysate contains GPOG peptide (PEP-1) (Fig. 3). Experimental Example 1-4. PEP-1 (GPOG) content in porcine placenta enzymatic hydrolysate In the present invention, among the six identified peptides, one peptide was selected as the indicator substance by confirming peak size and inter-batch reproducibility. The selected PEP-1 peptide has a GPOG sequence and a molecular weight of 342 Da, and the reproducibility of peptide content across three batches was confirmed (Tables 6 and 7). Peptide and amino acid sequences in porcine placenta enzymatic hydrolysate No. m / zRT (min)ChargeSequence PEP-1 (Sequence No. 1) 343.160.941 GPOGO: hydroxyproline (Hyp) It was confirmed that the content of the above-mentioned PEP-1 peptide in the porcine placental enzyme hydrolysate ranged from 2.9 mg / g to 8.7 mg / g. (Fig. 4 and Table 7) Reproducibility of Peptide GPOG (SEQ No. 1) Content in Porcine Placenta Enzymatic Hydrolysate (Content Unit: mg / g) Batch 1 Batch 2 Batch 3 Average Content in Hydrolysate (mg / g) PEP-1 (SEQ No. 1) 5.60 5.85 5.87 5.77 2.9 ~ 8.7 mg / g Experimental Example 2. Evaluation of in vivo efficacy of porcine placenta enzyme hydrolysate for hangover improvement 2.1 Animal husbandry The animals used in this study were 7-week-old male Sprague-Dawley (SD) rats (body weight ≤ 250–260 g) purchased from Daehan Biolink (Eumseong, Chungbuk, Korea). Upon introduction, the animals' health status was verified during a 2-week quarantine period, after which healthy individuals were used in the study. The rats were kept in an environment controlled by a 12-hour light-dark cycle, with 8 animals per group, and provided with standard feed and water on an open basis. During the experiment, the animals in the facility were maintained at a temperature of 23 ± 2°C and a relative humidity of 50 ± 10%, and all experimental procedures were approved by the Institutional Animal Care and Use Committee (IACUC) of Korea University (Approval No.: KUIACUC-2024-0001). Healthy animals underwent a quarantine and acclimatization process for two weeks, and rats were randomly divided into six groups for the test. 2.2 Test Group The test group is as follows. (1) Normal control group (2) Negative control group (3) Positive control: Hovenia dulcis fruit concentrate (67.2 mg / kg body weight, bw) (4) Porcine placenta enzyme hydrolysate low dose group (11.36 mg / kg body weight, bw) (5) Porcine placenta enzyme hydrolysate medium dose group (16.53 mg / kg body weight, bw) (6) Porcine placenta enzyme hydrolysate high dose group (22.70 mg / kg body weight, bw) After a single dose of EPPH at three concentrations of 11.36, 16.53, and 22.7 mg / kg bw, 30 minutes later, ethanol (3 g / kg bw) was administered orally to all rats except the normal control group. 2.3 Analysis of Acetaldehyde and Ethanol Content Blood samples for pharmacokinetic studies were collected via the retroorbital vein at 0, 1, 2, and 5 hours after ethanol administration. The blood samples were centrifuged at 3,000 rpm for 30 minutes at 4°C, and serum ethanol (EtOH) and acetaldehyde levels were measured by colorimetric analysis using an ethanol and acetaldehyde kit. Ethanol Content: Serum ethanol content was measured using the MAK076 kit (Merck Millipore, MA, USA). 50 μL of rat serum mixed with ethanol analysis buffer was added to each well, and after preparing the master reaction mix according to the kit instructions, 50 μL of the master reaction mix was added and incubated at room temperature for 60 minutes. After incubation, at 570 nm (A 570The absorbance was measured at ). The ethanol content was A provided in the kit. 570 It was evaluated using a standard. Acetaldehyde content: Serum acetaldehyde levels were measured using the KA6206 kit (Abnova, Taipei, Taiwan). 20 μL of rat serum was filled into each well, and after preparing the working reagent according to the manufacturer's instructions, 80 μL of working reagent was added. After mixing the plates, they were incubated at room temperature for 30 minutes, and at 565 nm (A 565 The absorbance was measured at ). The acetaldehyde concentration was A provided in the kit. 565 It was calculated using the standard. As a result, it was confirmed that blood ethanol and acetaldehyde concentrations tended to decrease depending on the concentration of EPPH administered; blood ethanol concentration reached a peak at 1 hour and acetaldehyde concentration at 2 hours, after which they gradually decreased over 5 hours. In particular, blood ethanol and acetaldehyde concentrations decreased statistically significantly in the group administered high concentrations of EPPH (Figure 2 (A) and (B)). This indicates that EPPH has the effect of reducing blood ethanol concentration after drinking. 2.4 AUC and C of alcohols and acetaldehyde max , T max analyze The results of the Area Unver Curve (AUC) analysis based on the experimental results of Figures 5 (A) and (B) are shown in Figures 5 (C) and (D), respectively. It was confirmed that the concentrations of ethanol and acetaldehyde were significantly reduced in the groups administered EPPH at intermediate (16.5 mg / kg bw) and high (22.7 mg / kg bw) concentrations compared to the control group that consumed ethanol. This confirms that EPPH significantly reduces blood ethanol and acetaldehyde concentrations. Serum Ethanol and Acetaldehyde Cmax and Tmax Levels EtOH Acetaldehyde C max1 (nmol)T max (h)C max (mM)T max (h)Alcohol 2 7.50 ± 0.68 3 1.75 ± 0.494.88 ± 0.682.13 ± 0.44HDFE5.00 ± 0.03 *,4 1.00 ± 0.00 2.90 ± 0.26 *,# 2.25 ± 0.41L-EPPH6.30 ± 0.59 # 1.13 ± 0.134.12 ± 0.352.13 ± 0.44M-EPPH5.91 ± 0.641.00 ± 0.004.01 ± 0.592.00 ± 0.46H-EPPH4.21 ± 0.09 **,# 1.00 ± 0.00 2.24 ± 0.14 **,# 2.13 ± 0.44 1 C max , maximum plasma concentration; T max , time to reach C max 2 Alcohol, single administration of 3 g / kg bw of alcohol after administration of physiological saline; HDFE, administration of 67.2 mg / kg bw of HDFE followed by a single dose of 3 g / kg bw of alcohol as a positive control; Single administration of 3 g / kg bw of alcohol following administration of L-EPPH, 11.36 mg / kg bw of EPPH; M-EPPH, single administration of 3 g / kg bw alcohol after administration of 16.53 mg / kg bw EPPH; Single administration of 3 g / kg bw alcohol following administration of H-EPPH and 22.70 mg / kg bw of EPPH 3 Results are expressed as means ± SEM (n = 8) 4*P< 0.05, **P< 0.01, significantly different from the Alcohol group; #,P< 0.05, significantly different from the HDFE group 2.4 Blood and Analysis For the mechanism study, blood was collected by cardiac blood sampling and centrifuged at 3,000 rpm for 30 minutes at 4°C to separate the plasma. Blood analysis was performed using a Cobas C111 analyzer (Roche, Basel, Switzerland), and fasting blood glucose, fasting triglycerides, total cholesterol, HDL cholesterol, LDL cholesterol, ALT, AST, LDH, total bilirubin, total protein, and albumin were analyzed in the plasma samples. Plasma insulin analysis was performed using the EZRMI (Rat / Mouse Insulin, Millipore, MA, USA) kit. 10 μL of serum was dispensed into each 96-well plate, 80 μL of detection antibody was added, and the plates were incubated at room temperature at 400 rpm for 2 hours. After incubation, the remaining solution was discarded, and the plates were washed three times with wash buffer and shaken to remove residual buffer. Subsequently, 100 μL of enzyme solution was added to each well and incubated on a plate shaker for 30 minutes. Afterward, the solution was removed and the plates were washed six times with wash buffer. 100 μL of substrate solution was added and incubated on a room temperature shaker for 20 minutes, after which 100 μL of stop solution was added to stop the reaction. Finally, absorbance was measured at 370 nm using a microplate reader (Multiskan Go, Thermo Fisher Scientific, CA, USA). The insulin concentration of the sample was calculated based on the A370 standard provided in the kit. Plasma arginine vasopressin analysis was performed using the RK06676 (Rat Arginine Vasopressin (AVP) ELISA kit, ABclonal, MA, USA). Briefly, 100 μL of serum was dispensed into each well and incubated at 37°C for 2 hours. Subsequently, the samples were washed three times with wash buffer, 100 μL of working biotin conjugate antibody was added, and the samples were incubated at 37°C for 1 hour. After incubation, the samples were washed three times, 100 μL of substrate solution was added, and the samples were incubated in the dark at 37°C for 15 minutes. Finally, 50 μL of stop solution was added to stop the reaction. Absorbance was measured at 450 nm using a microplate reader (Multiskan Go, Thermo Fisher Scientific, CA, USA), and the AVP concentration of the samples was A provided in the kit 450 Calculate based on the standard. As a result, AST and ALT levels in rats administered ethanol were significantly elevated compared to the normal group, and it was confirmed that AST and ALT levels decreased upon EPPH treatment. In addition, LDH levels were found to be reduced by the Hovenia dulcis extract (HDFE) and EPPH. These results suggest that EPPH may have a protective effect against liver damage caused by acute ethanol ingestion. Changes in serum biomarkers induced by EPPH Non-alcohol Alcohol HDFE EPPH Body weight (g) 259.1 ± 2.5 258.2 ± 2.0 258.7 ± 3.5 257.9 ± 3.2 Liver weight (g) 7.8 ± 0.2 8.1 ± 0.1 7.8 ± 0.2 8.0 ± 0.2 Plasma analysis Arginine vasopressin (ρg / mL) 38.2 ± 3.7 40.9 ± 4.1 36.2 ± 1.9 34.7 ± 1.8 Aspartate transaminase (U / L) 50.3 ± 1.0 * 56.5 ± 5.6 45.5 ± 3.5 43.3 ± 2.2 * Alanine transferase (U / L) 146.6 ± 8.7 166.2 ± 18.3 129.0 ± 8.5124.3 ± 5.9*Lactate dehydrogenase (U / L)282.1 ± 18.9421.6 ± 83.0229.1 ± 15.3*228.8 ± 28.6* 2.5 DPPH and Liver Tissue H&E Staining The DPPH radical test was performed according to the method described by Chung et al. (2008). Briefly, each sample was mixed with DPPH (Sigma-Aldrich, St. Louis, MO, USA) solution and incubated at 37°C for 30 minutes. Ascorbic acid (1 mg / mL, Sigma-Aldrich) was used as a reference substance. The absorbance of each solution was measured at 517 nm using a microplate reader (Thermo Fisher Scientific). EPPH was confirmed to exhibit strong radical scavenging activity in DPPH analysis. As shown in Figure 6 (A), it was confirmed that the DPPH radical scavenging ability was statistically significantly higher in the high concentration EPPH 22.70 mg / kg bw group. H&E staining results in liver tissue revealed no liver tissue damage or lipid droplets resulting from acute ethanol or EPPH administration. This experiment demonstrates that the single administration of ethanol did not lead to tissue damage (Fig. 6 (B)). 2.6 Histological Analysis (Inhibition of Lipid Peroxidation) 1) TBARS assay (Thiobarbituric acid reactive substance assay) measurement: The TBARS assay was performed using a TBARS assay kit (700870, Cayman, MI, USA) in accordance with the manufacturer's instructions. Approximately 25 mg of rapid-frozen liver tissue was homogenized over ice in RIPA buffer containing a protease inhibitor. The homogenized samples were centrifuged at 1,600 × g at 4°C for 10 minutes, after which 100 μL of each sample was added to a 1.5 mL microcentrifuge tube. 100 μL of TCA assay reagent (10%) was added to each vial, and 800 μL of the color reagent provided in the kit was added and mixed. After heating the vials in boiling water for 1 hour, the absorbance of 200 μL of the supernatant was measured at 535 nm using a microplate reader (Multiskan, USA). 535 It was measured at [location]. The TBARS concentration of the sample was calculated based on the A535 standard provided in the kit. 2) MDA Analysis: Hepatic lipid peroxidation was measured using a commercial malondialdehyde (MDA, ER1878, FineTest, Wuhan, China) kit, and the experiment was performed according to the manufacturer's instructions. Briefly, 1 g of rapid-frozen liver tissue was homogenized in 9 mL of PBS containing a protease inhibitor. The homogenized sample was centrifuged at 5,000 × g for 5 minutes, after which 50 μL of the supernatant was added to each well. Subsequently, 50 μL of biotin-labeled antibody was added and incubated at 37°C for 45 minutes. Afterward, the plate was thoroughly washed, 100 μL of SABC working solution was added, and the sample was incubated at 37°C for an additional 30 minutes. Afterward, 90 μL of TMB substrate solution was added and incubated at 37°C for 20 minutes, after which the absorbance was measured at 450 nm using a microplate reader (Multiskan, USA). The MDA concentration of the sample is A provided in the kit. 450 It was calculated based on the standard. As a result, quantification of hepatic lipid peroxidation levels through TBARS analysis revealed that ethanol intake significantly increased hepatic TBARS content, but administration of EPPH significantly decreased hepatic TBARS content (Fig. 7A). As a result of evaluating liver oxidative stress through MDA analysis, liver MDA levels increased with ethanol intake, but MDA concentrations significantly decreased upon administration of EPPH (Fig. 7B). In addition, Cyp2e1 gene expression related to the antioxidant system was also found to be statistically significantly reduced in the EPPH administration group compared to the alcohol intake group (Fig. 7C). The results of this study suggest that EPPH may exhibit an antioxidant effect that reduces lipid peroxidation products in rat liver. 2.7 Measurement of NAD+ / NADH and NADP+ / NADPH Levels NAD + / NADH and NADP+ / NADPH levels are NAD + / NADH Analysis Kit (ab65348, Abcam, Cambridge, UK) and NADP + Measurements were performed using the NAD+ / NADH and NADP+ / NADPH analysis kit (ab65349, Abcam, Cambridge, UK). Liver tissue samples, rapidly frozen in liquid nitrogen, were homogenized in respective NAD+ / NADH and NADP+ / NADPH extraction buffers, and then analyzed after enzyme removal using a 10 kDa spin column (ab93349, Abcam, Cambridge, UK). The analysis was performed according to the kit instructions, and NAD + / NADH and NADP + / NADPH levels were quantified based on protein content. As a result, ethanol intake decreased the NAD+ / NADH ratio, but EPPH showed a significant increase in the NAD+ / NADH ratio (Fig. 8). These results suggest that EPPH maintains NAD+ homeostasis and exhibits protective effects against ethanol-induced hepatic oxidative stress and liver damage. When ethanol is consumed through alcohol, NAD+ is converted to NADH during the ethanol breakdown process, leading to an increase in NADH in liver tissue. This inhibits fatty acid oxidation, which can cause fatty liver disease. The results of this experiment indicate that EPPH increases NAD+, which can provide hepatoprotective effects by preventing the development of fatty liver in the long term. Furthermore, NAD+ in tissues increases Sirtuin protein activity, which is essential for maintaining healthy tissue function. Therefore, an increase in the NAD+ / NADH ratio within liver tissue implies that it can bring about comprehensive positive effects on liver tissue protection. 2.9 Phospho kinase assay The Cell Signaling Phospho Antibody Array (Fullmoon Biosystems, CA, USA) was used to evaluate differential protein expression after EPPH treatment. Proteins were extracted from rapid-frozen liver tissue at 4°C using RIPA buffer containing Halt protease inhibitors. After centrifugation at 13,000 rpm for 20 minutes, the soluble protein fraction was collected. Protein concentration was measured using a protein analysis dye concentrate (Bio-Rad, Hercules, California, USA). The experiment was conducted according to the manufacturer's protocol. Briefly, slides were incubated in a shaking incubator for 45 minutes, treated with a blocking reagent, and thoroughly washed several times with distilled water. Bound biotinylated proteins were detected using 1:1000 diluted Cy3-labeled streptavidin (GE Healthcare, Little Chalfont, UK). After 20 minutes of incubation, slides were washed with distilled water, completely dried by centrifugation, and scanned using a GenePix 4100A scanner (E-Biogen, Seoul, Korea). Protein expression values ​​were analyzed and quantified using Excel-based DEG analysis software (ExDEGA; www.e-biogen.com, Seoul, Korea) and visualized as a heatmap. Expression levels were displayed as a distribution ranging from pink (high expression) to sky blue (low expression), with white indicating a one-fold change. Phosphorylation microarray analysis was performed to investigate the effects of EPPH on liver ethanol metabolism, and seven proteins were identified that changed by more than 20% compared to the alcohol control group. Consistent with RNA sequencing results, it was confirmed that EPPH administration alleviated apoptosis by inhibiting CASP9, BAX, the oncoprotein TP53, and cell cycle checkpoint kinase 2 (CHK2) (Fig. 9). EPPH administration downregulated MAPK8 / MAPK9 / MAPK10 compared to the alcohol administration group, which showed that EPPH protects against alcohol-induced liver damage by downregulating JNK, which regulates cellular processes such as cell proliferation, survival, apoptosis, and inflammation. In addition, through analysis of KEGG, a gene associated with AMPK (Prkaa) and Sirt1, and pathway mapping, it was confirmed that EPPH intake caused significant changes in the CHK2, TP53, and PRKAB1 (AMPK-SIRT1-PGC1α) signaling pathways (Fig. 9). Therefore, it was confirmed that the effect of EPPH intake upon alcohol consumption rapidly metabolizes ethanol and acetaldehyde in the blood, and demonstrated that it alleviates hangovers by suppressing liver damage such as AST, ALT, and lipid peroxides in the liver. This hangover alleviation effect was confirmed by improving the expression of Aldh2, a gene related to alcohol metabolism, and suppressing Cyp2e1 expression to inhibit ROS, TBARS, and MDA in the liver caused by alcohol intake, as well as by inhibiting apoptosis and increasing the phosphorylation of the AMPK-SIRT1-PGC1α-CPT1A pathway (Fig. 9). It is believed that the intake of EPPH exhibits antioxidant and anti-inflammatory effects by regulating important pathways related to ethanol metabolism, oxidative stress, and cell survival caused by alcohol consumption, and helps improve muscle damage, fatigue, and hangovers, as well as protect against ethanol-induced liver damage. In a study using experimental animals (SD rats), a single administration of 22.7 mg / kg / day to rats resulted in no particular toxicity and showed significant results. In accordance with the U.S. FDA guidelines for calculating effective drug concentrations based on the ratio to body surface area, the effective dose (22.7 mg / kg / day) effective in the animal study was converted to a human standard to calculate the effective dose, and based on this result, the daily intake dose for humans was set at 220 mg. Accordingly, in this study, the intake of porcine placenta enzyme hydrolysate was set at 220 mg / day based on the results of the animal study. Basis for calculating daily intake: 22.7 mg / kg / day × 0.162 × 60 kg = 220.644 mg / day Rat Dose / Conversion factor relative to body surface area / Adult body weight Experimental Example 3. Evaluation of the hangover relief efficacy of a composition containing porcine placenta enzyme hydrolysate, betaine, and curcumin as active ingredients A liquid hangover remedy was prepared with the composition shown in the table below, and a clinical trial was conducted. The liquid formulation was prepared by homogeneously mixing the said composition and then sterilizing it. Example 2 Comparative Example 1 Comparative Example 2 Comparative Example 3 Comparative Example 4 Comparative Example 5 Control Porcine Placenta Enzyme Hydrolysate 1.1% 1.1% 1.1% 1.1% Water-soluble curcumin (curcumin content 12%) 0.5% 0.5% 0.5% Betaine 3.5% 3.5% Crystalline fructose 5% 5% 5% 5% 5% 5% 5% Citric acid 3.7% 3.7% 3.7% 3.7% 3.7% 3.7% 3.7% Vitamin B1 Nitrate 0.39% 0.39% 0.39% 0.39% 0.39% 0.39% Niacinamide 0.19% 0.19% 0.19% 0.19% 0.19% 0.19% Calcium Pantothenate 0.34% 0.34% 0.34% 0.34% 0.34% 0.34% 0.34% L-Arginine 5% 5% 5% 5% 5% 5% L-Asparagine 0.30 0.30 0.30 0.30 0.30 30.3 Milk Thistle Extract Powder 1% 1% 1% 1% 1% 1% 1% Red Ginseng Extract 0.1% 0.1% 0.1% 0.1% 0.1% 0.1% 0.1% Yeast Extract 0.1% 0.1% 0.1% 0.1% 0.1% 0.1% 0.1% Purified Water Remaining Amount Remaining Amount Remaining Amount Remaining Amount Remaining Amount Remaining Amount Total (Weight%) 100 100 100 100 100 100 100 Method for evaluating hangover relief efficacy Twenty men weighing 65–85 kg were selected, and the experiment was conducted at 10-day intervals as follows (the subjects participating in the experiment were not allowed to experience alcohol consumption during the test period): 1) Deliver precautions regarding this human clinical trial for hangover relief to the test subjects, gather them on the day of the trial, and provide a standard meal. 2) Ingest the test food orally 1 hour and 30 minutes after a meal (20,000 mg of liquid composition). 3) Consume alcohol (90 g or 0.789 g / kg bw) within 30 minutes after consuming the test food (Example 2, Comparative Examples 1–5) or the control food (for this test, consume 1.5 bottles of Chamisul Fresh (16.0%) product). 4) Consumption of a minimal amount of snacks (e.g., 20 pieces of Shrimp Crackers) is permitted while consuming alcohol. 5) Fast for 4 hours after consuming alcohol. 6) Water may be consumed in the same amount 4 hours after alcohol consumption (e.g., 100 mL of water in a single serving). 7) Measure breath alcohol concentration over time and conduct a sensory evaluation. Experimental Example 3-1. Measurement of blood alcohol concentration Blood alcohol concentrations were measured using a breath alcohol analyzer (ALC-2 Alcoscan) before alcohol consumption and after 0.5 hr, 1 hr, 2 hr, 6 hr, and 15 hr after alcohol consumption, and the results are shown in Table 13 and Figure 10. As a result of the measurement, it was confirmed that the hangover relief effect was superior in the test in which the beverage made by mixing porcine placenta enzyme hydrolysate / betaine / curcumin of Example 2 was consumed, as it lowered the blood alcohol concentration more than in the test in which only porcine placenta enzyme hydrolysate, or betaine, or curcumin was consumed. 0hr 0.5hr 1hr 2hr 6hr 15hr Example 2 00.01 90.06 40.05 20.0280 Comparative Example 1 00.028 0.08 30.07 30.0380 Comparative Example 2 00.036 0.09 10.07 90.0350 Comparative Example 3 00.04 20.10 10.08 30.04 20 Comparative Example 4 00.04 80.10 90.09 10.04 80 Comparative Example 5 00.05 10.11 30.10 10.04 90 Control Group 00.05 90.12 20.10 10.05 70 Experimental Example 3-2. Sensory Evaluation of Hangover Symptom Relief It was evaluated based on a total of 12 items, including fatigue, apathy (lack of interest), concentration problems, clumsiness, confusion (distractedness), thirst, sweating, shivering (chills), gastrointestinal disturbances, nausea, dizziness, and heart palpitations, and the degree of hangover relief was rated on a 10-point scale (0 points = no symptoms, 10 points = extreme symptoms). The evaluation results are shown in the table below (Survey method: AHSS (Alcohol Hangover Severity Scale) questionnaire). As a result calculated using the Colby formula, the predicted hangover relief activity when three active ingredients are mixed is 59.33, and the actual measured hangover relief effect of the example containing three active ingredients is 35.33, so it can be seen that the example has a synergistic effect for hangover relief. Sample Name Control Group Example 2 Comparison Example 1 Comparison Example 2 Comparison Example 3 Comparison Example 4 Comparison Example 5 Questionnaire Score Average (Total 120 points) 4.3 points 42.4 points 57.2 points 65.6 points 71.6 points 80.3 87.6 Degree of Hangover Relief (%) 3.6 0 35.3 34 7.6 75 4.6 75 9.6 76 6.9 0 73.00 * Degree of Hangover Relief (%): The AHSS questionnaire assigns 10 points for the most severe hangover; therefore, a lower score indicates a less severe hangover. This value is calculated by dividing the average questionnaire score by the total score (120 points).

Claims

1. Porcine placenta enzyme hydrolysate containing a peptide composed of sequence number 1.

2. A pharmaceutical composition for relieving hangovers comprising a porcine placenta enzyme hydrolysate containing a peptide composed of SEQ ID NO. 1 as an active ingredient.

3. A food composition for relieving hangovers comprising porcine placenta enzyme hydrolysate containing a peptide composed of SEQ ID NO. 1 as an active ingredient.

4. In Claim 3, A food composition characterized in that the above-mentioned peptide is derived from porcine placenta enzyme hydrolysate.

5. In Claim 3 A food composition characterized by the above porcine placenta enzyme hydrolysate lowering blood alcohol and acetaldehyde.

6. In Claim 3, A food composition characterized by the above porcine placenta enzyme hydrolysate enhancing the activity of alcohol dehydrogenase and acetaldehyde dehydrogenase.

7. In Claim 3, A food composition characterized by the above porcine placenta enzyme hydrolysate having an antioxidant effect that inhibits lipid peroxidation.

8. In Claim 3, A food composition characterized by the above porcine placenta enzyme hydrolysate increasing the NAD+ / NADH ratio.

9. In Claim 3, A food composition characterized by the above porcine placenta enzyme hydrolysate inhibiting exhaled alcohol concentration after alcohol intake.

10. In Claim 3, A food composition characterized by the above porcine placenta enzyme hydrolysate inhibiting LDH.

11. In Claim 3, A food composition characterized by the above porcine placenta enzyme hydrolysate inhibiting apoptosis.

12. In Claim 3, A food composition characterized by the above porcine placenta enzyme hydrolysate inhibiting CYP2E1 gene expression.

13. A food composition for relieving hangovers comprising porcine placenta enzyme hydrolysate, betaine, and curcumin as active ingredients.

14. In Claim 13, A food composition characterized by the above porcine placenta enzyme hydrolysate comprising a peptide of SEQ ID NO.

1.

15. In Claim 13, A food composition characterized by further comprising one or more selected from the group of vitamins, amino acids, and plant extracts.

16. In Claim 15, A food composition characterized by comprising one or more vitamins selected from the group consisting of vitamin B1, niacin, pantothenic acid, vitamin B6, vitamin B12, and folic acid.

17. In Claim 15, A food composition characterized by comprising one or more amino acids selected from the group consisting of taurine, arginine, aspartic acid, asparagine, methionine, glutamic acid, and alanine.

18. In Claim 15, A food composition characterized by comprising one or more selected from the group consisting of red ginseng extract, Hovenia dulcis extract, Pueraria root extract, Pueraria flower extract, milk thistle extract, noni extract, acerola extract, and yeast extract.

19. In Claim 13, A food composition characterized by being formulated into a formulation selected from the group consisting of tablets, capsules, powders, granules, jellies, liquids, pills, and dual formulations.

20. A food composition for relieving hangovers consisting of a liquid and a tablet, The above liquid comprises porcine placenta enzyme hydrolysate, betaine, and curcumin, and The above-mentioned tablet is a food composition characterized by comprising milk thistle extract, Hovenia dulcis fruit extract, kudzu root extract, and yeast extract.

21. In claim 20, The above liquid further contains citric acid, taurine, L-asparagine, L-arginine, and vitamins, and The above-mentioned tablet is a food composition characterized by further including L-asparagine, taurine, and vitamins.

22. In Claim 21, The vitamins contained in the above liquid include vitamin B1, niacin, pantothenic acid, vitamin B6, vitamin B12, and folic acid, and A food composition characterized by the fact that the vitamins included in the above tablets include vitamin B2 and vitamin B1.

23. In claim 20, A food composition characterized by the above liquid further comprising one or more selected from the group consisting of citric acid, vitamins, amino acids, plant extracts, and sweeteners.

24. In Claim 23, A food composition characterized by comprising one or more vitamins selected from the group consisting of vitamin B1, vitamin B2, niacin, pantothenic acid, vitamin B6, vitamin B12, and folic acid.

25. In Claim 23, A food composition characterized by comprising one or more sweeteners selected from the group consisting of fructose, glucose, honey, fructooligosaccharide, sucrose, aspartame, acesulfame potassium, sucralose, enzyme-treated stevia, pear concentrate, pineapple concentrate, apple concentrate, and grape concentrate.

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