JPH03280835A - Decomposition product of glair and food containing same decomposition product - Google Patents
Decomposition product of glair and food containing same decomposition productInfo
- Publication number
- JPH03280835A JPH03280835A JP2084580A JP8458090A JPH03280835A JP H03280835 A JPH03280835 A JP H03280835A JP 2084580 A JP2084580 A JP 2084580A JP 8458090 A JP8458090 A JP 8458090A JP H03280835 A JPH03280835 A JP H03280835A
- Authority
- JP
- Japan
- Prior art keywords
- egg white
- decomposition product
- hydrolyzate
- glair
- active fraction
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 238000000354 decomposition reaction Methods 0.000 title claims abstract description 9
- 235000013305 food Nutrition 0.000 title claims description 20
- 239000012588 trypsin Substances 0.000 claims abstract description 16
- 108091005804 Peptidases Proteins 0.000 claims abstract description 12
- 241001465754 Metazoa Species 0.000 claims abstract description 11
- 239000004365 Protease Substances 0.000 claims abstract description 11
- 108090000631 Trypsin Proteins 0.000 claims abstract description 10
- 102000004142 Trypsin Human genes 0.000 claims abstract description 10
- 108090000284 Pepsin A Proteins 0.000 claims abstract description 9
- 102000057297 Pepsin A Human genes 0.000 claims abstract description 9
- 229940111202 pepsin Drugs 0.000 claims abstract description 9
- 230000003301 hydrolyzing effect Effects 0.000 claims abstract description 7
- 108090000746 Chymosin Proteins 0.000 claims abstract description 4
- 102000004400 Aminopeptidases Human genes 0.000 claims abstract description 3
- 108090000915 Aminopeptidases Proteins 0.000 claims abstract description 3
- 102000005367 Carboxypeptidases Human genes 0.000 claims abstract description 3
- 108010006303 Carboxypeptidases Proteins 0.000 claims abstract description 3
- 102000004860 Dipeptidases Human genes 0.000 claims abstract description 3
- 108090001081 Dipeptidases Proteins 0.000 claims abstract description 3
- 108010067372 Pancreatic elastase Proteins 0.000 claims abstract description 3
- 102000016387 Pancreatic elastase Human genes 0.000 claims abstract description 3
- 108010019160 Pancreatin Proteins 0.000 claims abstract description 3
- 229940055695 pancreatin Drugs 0.000 claims abstract description 3
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 claims description 45
- 108010000912 Egg Proteins Proteins 0.000 claims description 45
- 102000002322 Egg Proteins Human genes 0.000 claims description 45
- 210000000969 egg white Anatomy 0.000 claims description 45
- 235000014103 egg white Nutrition 0.000 claims description 45
- 230000004531 blood pressure lowering effect Effects 0.000 claims description 14
- 102000035195 Peptidases Human genes 0.000 claims description 10
- UUUHXMGGBIUAPW-UHFFFAOYSA-N 1-[1-[2-[[5-amino-2-[[1-[5-(diaminomethylideneamino)-2-[[1-[3-(1h-indol-3-yl)-2-[(5-oxopyrrolidine-2-carbonyl)amino]propanoyl]pyrrolidine-2-carbonyl]amino]pentanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-methylpentanoyl]pyrrolidine-2-carbon Chemical compound C1CCC(C(=O)N2C(CCC2)C(O)=O)N1C(=O)C(C(C)CC)NC(=O)C(CCC(N)=O)NC(=O)C1CCCN1C(=O)C(CCCN=C(N)N)NC(=O)C1CCCN1C(=O)C(CC=1C2=CC=CC=C2NC=1)NC(=O)C1CCC(=O)N1 UUUHXMGGBIUAPW-UHFFFAOYSA-N 0.000 claims description 7
- 102000004270 Peptidyl-Dipeptidase A Human genes 0.000 claims description 7
- 108090000882 Peptidyl-Dipeptidase A Proteins 0.000 claims description 7
- 239000000463 material Substances 0.000 claims description 5
- 239000004615 ingredient Substances 0.000 claims description 3
- -1 chymotrypurine Proteins 0.000 claims description 2
- 230000005764 inhibitory process Effects 0.000 claims 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 claims 1
- 230000002401 inhibitory effect Effects 0.000 abstract description 13
- 102000004190 Enzymes Human genes 0.000 abstract description 12
- 108090000790 Enzymes Proteins 0.000 abstract description 12
- 229940088598 enzyme Drugs 0.000 abstract description 12
- 102000015427 Angiotensins Human genes 0.000 abstract description 2
- 108010064733 Angiotensins Proteins 0.000 abstract description 2
- 230000001077 hypotensive effect Effects 0.000 abstract description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 abstract 2
- 108090000317 Chymotrypsin Proteins 0.000 abstract 1
- 229960002376 chymotrypsin Drugs 0.000 abstract 1
- 229960001322 trypsin Drugs 0.000 abstract 1
- QIAFMBKCNZACKA-UHFFFAOYSA-N N-benzoylglycine Chemical compound OC(=O)CNC(=O)C1=CC=CC=C1 QIAFMBKCNZACKA-UHFFFAOYSA-N 0.000 description 8
- 230000006870 function Effects 0.000 description 8
- 239000002994 raw material Substances 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 7
- 238000011282 treatment Methods 0.000 description 7
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 5
- 230000007062 hydrolysis Effects 0.000 description 5
- 238000006460 hydrolysis reaction Methods 0.000 description 5
- 230000000694 effects Effects 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
- 206010020772 Hypertension Diseases 0.000 description 3
- 108010058846 Ovalbumin Proteins 0.000 description 3
- 239000005018 casein Substances 0.000 description 3
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 3
- 235000021240 caseins Nutrition 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 229940092253 ovalbumin Drugs 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 241000287828 Gallus gallus Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- HXOLFXRMWWHLMH-UHFFFAOYSA-L disodium boric acid carbonate Chemical compound [Na+].[Na+].OB(O)O.[O-]C([O-])=O HXOLFXRMWWHLMH-UHFFFAOYSA-L 0.000 description 2
- 235000013601 eggs Nutrition 0.000 description 2
- 235000013376 functional food Nutrition 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 239000005457 ice water Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 238000000034 method Methods 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 210000004080 milk Anatomy 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 108010076119 Caseins Proteins 0.000 description 1
- 239000004278 EU approved seasoning Substances 0.000 description 1
- 108010028690 Fish Proteins Proteins 0.000 description 1
- 108010058643 Fungal Proteins Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 244000294411 Mirabilis expansa Species 0.000 description 1
- 235000015429 Mirabilis expansa Nutrition 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108010009736 Protein Hydrolysates Proteins 0.000 description 1
- 108010073771 Soybean Proteins Proteins 0.000 description 1
- 229920002494 Zein Polymers 0.000 description 1
- 238000005377 adsorption chromatography Methods 0.000 description 1
- 210000001557 animal structure Anatomy 0.000 description 1
- 230000003712 anti-aging effect Effects 0.000 description 1
- 230000003276 anti-hypertensive effect Effects 0.000 description 1
- 235000015278 beef Nutrition 0.000 description 1
- 235000013361 beverage Nutrition 0.000 description 1
- 230000036772 blood pressure Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 235000008429 bread Nutrition 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 229940080701 chymosin Drugs 0.000 description 1
- 235000009508 confectionery Nutrition 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 238000004042 decolorization Methods 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 230000006806 disease prevention Effects 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 235000006694 eating habits Nutrition 0.000 description 1
- 210000002969 egg yolk Anatomy 0.000 description 1
- 239000012156 elution solvent Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 235000011194 food seasoning agent Nutrition 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 235000013536 miso Nutrition 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- GNOLWGAJQVLBSM-UHFFFAOYSA-N n,n,5,7-tetramethyl-1,2,3,4-tetrahydronaphthalen-1-amine Chemical compound C1=C(C)C=C2C(N(C)C)CCCC2=C1C GNOLWGAJQVLBSM-UHFFFAOYSA-N 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 235000020991 processed meat Nutrition 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009711 regulatory function Effects 0.000 description 1
- 230000033764 rhythmic process Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 230000001953 sensory effect Effects 0.000 description 1
- 230000037152 sensory function Effects 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 235000013555 soy sauce Nutrition 0.000 description 1
- 235000019710 soybean protein Nutrition 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 239000005019 zein Substances 0.000 description 1
- 229940093612 zein Drugs 0.000 description 1
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分野〕
本発明は、血圧降下作用を有する卵白加水分解物または
その活性画分、および該卵白加水分解物またはその活性
画分を含有してなる食品に関するものである。Detailed Description of the Invention [Industrial Field of Application] The present invention relates to an egg white hydrolyzate or an active fraction thereof having a blood pressure lowering effect, and a food product containing the egg white hydrolyzate or an active fraction thereof. It is related to.
食品には２つの機能があり、その１つは生命維持に必要
な栄養機能（−次機能）であり、他の１つは味覚、嗅覚
などの感覚応答に係わる感覚機能（二次機能）であると
されている。Food has two functions; one is a nutritional function (secondary function) necessary for sustaining life, and the other is a sensory function (secondary function) related to sensory responses such as taste and smell. It is said that there is.
最近、これらの機能のほかに、体調リズムの調整、生体
防御、疾病予防、疾病回復、老化抑制等々の高次の生命
活動にかかわる調整機能（三次機能）も食品に備わって
いると考えられるようになってきている。Recently, in addition to these functions, it has come to be believed that foods also have regulatory functions (tertiary functions) related to higher-order life activities, such as adjusting physical rhythms, biological defense, disease prevention, disease recovery, and anti-aging. It is becoming.
近年、これらの三次機能を生体内で発現する食品由来の
成分の解明が進み、これらの成分を配合強化した食品、
いわゆる機能性食品が市場に出まわるようになってきて
いる。In recent years, the elucidation of food-derived ingredients that express these tertiary functions in vivo has progressed, and foods with enhanced blends of these ingredients have been developed.
So-called functional foods are beginning to appear on the market.
高血圧症もそのような機能性食品のＲ発のための１つの
ターゲットとされ、血圧降下作用を示す食品由来の成分
の解明が精力的に行なわれている。Hypertension is also considered to be one of the targets for the R-induced effects of such functional foods, and efforts are being made to elucidate food-derived components that exhibit blood pressure-lowering effects.
たとえば、ゼラチン、カゼイン、魚類蛋白質、大豆蛋白
質、γ−ゼインなどを加水分解して得た加水分解物、ま
たは該加水分解物から抽出同定されたペプチドが血圧降
下作用を有することが既に報告サレテイル（特１ｊｉ［
５２−１４８６３１号、特開昭５８−１０９４２５号、
特開昭５９−４４３２３号、特開昭５９−４４３２４号
、特開昭６１−３６２２６号、特開昭６１−３６２２７
号、特開昭６２−１６９７３２号、特開昭６３−１４１
９９５号、特開昭６３−１４１９９６号、特開昭６４−
５４９７号、特開昭６４−９９３８号、特開平２−２０
２６３号、特開平２−２３８８５号、特開平２−３６１
２７号などの各公報参照）。For example, it has been reported that hydrolysates obtained by hydrolyzing gelatin, casein, fish protein, soybean protein, γ-zein, etc., or peptides extracted and identified from the hydrolysates, have antihypertensive effects. Special 1ji [
No. 52-148631, JP-A-58-109425,
JP-A-59-44323, JP-A-59-44324, JP-A-61-36226, JP-A-61-36227
No., JP-A-62-169732, JP-A-63-141
No. 995, JP-A-63-141996, JP-A-64-
No. 5497, JP-A-64-9938, JP-A-2-20
No. 263, JP-A No. 2-23885, JP-A No. 2-361
(Refer to each publication such as No. 27).
しかし、従来安価な蛋白源として供給可能な卵白を微生
物または植物起源の蛋白分解酵素により加水分解して得
られた加水分解物は微弱なアンジオテンシン転換酵素阻
害作用しか示さず（特開昭６２−１６９７３２号公報参
照）、血圧降下作用を有する医薬５食品等の原料とはな
りえなかった。However, the hydrolyzate obtained by hydrolyzing egg white, which has conventionally been available as a cheap protein source, with proteases of microbial or plant origin shows only a weak angiotensin converting enzyme inhibitory effect (Japanese Patent Application Laid-Open No. 169732-1982). (see Publication No. 1), it could not be used as a raw material for pharmaceuticals, foods, etc. that have a blood pressure lowering effect.
本発明者は、卵白を加水分解するのに使用されていた従
来の微生物または植物起源の蛋白分解酵素に代え、動物
起源の蛋白分解酵素を使用すれば、優れたアンジオテン
シン転換酵素阻害作用を有する卵白加水分解物を取得す
ることができることを知り、本発明を完成させた。The present inventors have demonstrated that egg white has excellent angiotensin converting enzyme inhibitory activity if an animal-derived protease is used instead of the conventional microbial or plant-derived protease used to hydrolyze egg white. The present invention was completed based on the knowledge that a hydrolyzate can be obtained.
すなわち、本発明は、卵白を動物起源の蛋白分解酵素に
より加水分解して得られる血圧降下作用を有する卵白分
解物またはその活性画分に関するものである。That is, the present invention relates to an egg white decomposition product or an active fraction thereof, which has a blood pressure lowering effect and is obtained by hydrolyzing egg white with an animal-derived protease.
また、本発明は、上記の血圧降下作用を有する卵白加水
分解物またはその活性画分（以下、「卵白加水分解物等
」と略称することもある）を含有してなる食品素材およ
び食品に関するものである。The present invention also relates to food materials and foods containing egg white hydrolyzate or its active fraction (hereinafter sometimes abbreviated as "egg white hydrolyzate, etc.") having the above-mentioned blood pressure lowering effect. It is.
以下、本発明の詳細な説明する。The present invention will be explained in detail below.
本発明の卵白加水分解物等を調製するための卵白原料は
特に制限されない。すなわち、鶏卵等を割卵し、卵黄を
分離して得られる未変性状のもの。The egg white raw material for preparing the egg white hydrolyzate and the like of the present invention is not particularly limited. In other words, it is an undenatured product obtained by breaking chicken eggs and separating the yolk.
該未変性卵白を変性させた変性卵白、冷凍状卵白を解凍
したもの、乾燥状卵白を水に溶解または懸濁したもの、
または上述の卵白から分画して得られるタンパク質画分
（たとえば卵白アルブミンなど）を水に溶解または懸濁
したものを使用することができる。Denatured egg white obtained by denaturing the undenatured egg white, frozen egg white thawed, dried egg white dissolved or suspended in water,
Alternatively, a protein fraction obtained by fractionating the above-mentioned egg white (e.g., ovalbumin) dissolved or suspended in water can be used.
上述の卵白原料を加水分解するのに使用する蛋白分解酵
素は動物起源のもので、卵白を加水分解した時に血圧降
下作用を有する成分を生成できるものであれば特に限定
されない。The protease used to hydrolyze the above-mentioned egg white raw material is of animal origin and is not particularly limited as long as it can produce a component having a blood pressure lowering effect when hydrolyzing egg white.
ここで、動物起源の蛋白分解酵素とは、動物の体内（臓
器など）に存在する酵素またはそれと実質的に同一の構
造と機能を有する蛋白分解酵素であって、その製法は問
わない。すなわち、たとえば動物の臓器、組織などから
抽出したもの、または遺伝子工学的手法を用いて微生物
で生産されたものであっても本発明の卵白加水分解等を
調製するために使用できる。Here, a protease of animal origin is an enzyme existing in the body (organ, etc.) of an animal, or a protease having substantially the same structure and function as that, and the production method thereof is not limited. That is, for example, even those extracted from animal organs, tissues, etc., or those produced with microorganisms using genetic engineering techniques can be used to prepare the egg white hydrolysis etc. of the present invention.
そのような動物起源の酵素としては、たとえばペプシン
、レンニン（キモシン）、トリプシン、キモドリブン、
パンクレアチン、エラスターゼ、カルボキシペプチダー
ゼ、アミノペプチダーゼ、ジペプチダーゼなどを例示す
ることができ、これらの酵素群から卵白を加水分解した
時に血圧降下作用を有する成分を生成させるのに好都合
なものを適宜選択して使用すればよい。Such enzymes of animal origin include, for example, pepsin, rennin (chymosin), trypsin, chymodriven,
Pancreatin, elastase, carboxypeptidase, aminopeptidase, dipeptidase, etc. can be exemplified, and from these enzyme groups, enzymes suitable for producing a component having a blood pressure lowering effect when egg white is hydrolyzed are selected as appropriate. Just use it.
酵素の使用量は対蛋白当り０．５〜１０％（Ｗ／Ｗ）の
範囲内より適宜選定すればよい。The amount of enzyme to be used may be appropriately selected within the range of 0.5 to 10% (W/W) per protein.
卵白原料の加水分解は、血圧降下作用を有する成分を効
率的に調製できる条件下で行う。Hydrolysis of the egg white raw material is carried out under conditions that allow efficient preparation of components having a blood pressure lowering effect.
たとえば、酵素としてペプシンを使用する場合にはＰＨ
０，５〜２．５の条件下、３５〜４０℃で１〜５０時間
反応させることにより卵白を加水分解することができる
。また、トリプシンを使用する場合にはＰＨ６，５〜７
．５の条件下、３５〜４０℃で１〜５０時間反応させる
ことにより卵白を加水分解することができる。For example, when using pepsin as the enzyme, the PH
Egg white can be hydrolyzed by reacting at 35 to 40°C for 1 to 50 hours under conditions of 0.5 to 2.5. In addition, when using trypsin, the pH should be 6.5-7.
．． Egg white can be hydrolyzed by reacting at 35 to 40°C for 1 to 50 hours under the conditions of 5.
加水分解の回数は１回に限定されず、複数同行ってもよ
い。The number of times of hydrolysis is not limited to one, but may be repeated multiple times.
加水分解を複数回行う場合、使用する酵素は同一のもの
であっても、異なったものであってもよい。When performing hydrolysis multiple times, the enzymes used may be the same or different.
加水分解終了後、必要により遠心分離、沈降分離、膜分
離、濾過等の通常の固液分離手段で固形分を除去したも
のを本発明の卵白加水分解物とする。After the hydrolysis is completed, if necessary, the solid content is removed by conventional solid-liquid separation means such as centrifugation, sedimentation, membrane separation, filtration, etc. to obtain the egg white hydrolyzate of the present invention.
このようにして得られた卵白加水分解物は、必要により
脱色、脱塩、濃縮、乾燥等の処理を施して最終製品とし
ての使用に好適な形態にまで加工処理することもできる
。The egg white hydrolyzate thus obtained can be processed into a form suitable for use as a final product by subjecting it to treatments such as decolorization, desalination, concentration, and drying, if necessary.
また、上述の卵白加水分解物を吸着クロマトグラフィー
処理、分子ふるいクロマトグラフィー処理、膜分離処理
（限外濾過など）等のペプチド混合物の分画処理に付し
て、血圧降下作用を有する活性画分のみを分画すること
もできる。In addition, the above-mentioned egg white hydrolyzate is subjected to a peptide mixture fractionation treatment such as adsorption chromatography treatment, molecular sieve chromatography treatment, membrane separation treatment (ultrafiltration, etc.) to obtain an active fraction that has a blood pressure lowering effect. It is also possible to fractionate only.
本発明の卵白加水分解物等は、血圧降下作用を有し、こ
れを各種食品に添加すれば、血圧降下作用を有する食品
を提供することができる。The egg white hydrolyzate of the present invention has a blood pressure lowering effect, and by adding it to various foods, it is possible to provide a food having a blood pressure lowering effect.
ユース等の飲料、菓子、パン、調味料、乳製品。Beverages for youth, sweets, bread, seasonings, dairy products.
食肉加工品など食品の種類、形態等は特に制限されない
が、たとえば、従来高血圧症の人々が摂取制限をしてい
る食品（たとえば醤油、味噌等の含塩食品）に添加すれ
ば、高血圧症の人でも血圧の上昇を心配することなく、
普通の人々と同様の食生活を楽しむことができる。There are no particular restrictions on the type or form of foods such as processed meat products, but for example, if added to foods that people with hypertension have traditionally restricted their intake (e.g., salt-containing foods such as soy sauce and miso), it may reduce the risk of hypertension. Even people do not have to worry about an increase in blood pressure,
You can enjoy the same eating habits as normal people.
以下、実施例を示し、本発明を具体的に説明する。EXAMPLES Hereinafter, the present invention will be specifically explained with reference to Examples.
実施例 １
乾燥卵白（キューピー■製）１０．をＯ，ＩＮ塩酸溶液
（ｐＨ１，０）２００−に溶解させ、これにペプシン６
００■（和光純薬工業■製）を加え、３７℃で１８時間
反応させた。Example 1 Dried egg white (manufactured by Kewpie ■) 10. was dissolved in O,IN hydrochloric acid solution (pH 1,0) 200-, and pepsin 6 was added to this.
00■ (manufactured by Wako Pure Chemical Industries, Ltd.) was added, and the mixture was reacted at 37°C for 18 hours.
反応後、水酸化ナトリウム溶液を用いて反応液をｐＨ７
，０に調整後１反応液全体を氷水で５分間冷却し、１５
０００Ｘｇで１５分間遠心分離して得た上清をペプシン
加水分解物とした。After the reaction, the reaction solution was adjusted to pH 7 using sodium hydroxide solution.
After adjusting to 0, the entire reaction solution was cooled with ice water for 5 minutes, and 15
The supernatant obtained by centrifugation at 000Xg for 15 minutes was used as a pepsin hydrolyzate.
このペプシン加水分解物にトリプシン溶液〔０，０５Ｍ
りん酸緩衝液（ｐＨ７，０）にトリプシン（和光純薬工
業■製）を溶解させたもの〕１０！（２５■のトリプシ
ン含有）を加え、３７℃で１５時間反応させた。Trypsin solution [0.05M] was added to this pepsin hydrolyzate.
Trypsin (manufactured by Wako Pure Chemical Industries, Ltd.) dissolved in phosphate buffer (pH 7.0)] 10! (containing 25 μl of trypsin) was added and reacted at 37° C. for 15 hours.
反応後、濃塩酸１０−を加え、反応液全体を氷水で５分
間冷却した。冷却後、水酸化ナトリウム溶液を加えて反
応液のｐＨを７．０に調整後、１５０００Ｘｇで１５分
間遠心分離して得た上滑をペプシン−トリプシン加水分
解物とした。After the reaction, 10-concentrated hydrochloric acid was added, and the entire reaction solution was cooled with ice water for 5 minutes. After cooling, the pH of the reaction solution was adjusted to 7.0 by adding a sodium hydroxide solution, and the supernatant obtained by centrifugation at 15,000×g for 15 minutes was used as a pepsin-trypsin hydrolyzate.
比較のために、マリンビーフ（新潟鉄工所■製）、酵母
蛋白（真人■製）を用いて上述と同様の方法によりペプ
シン加水分解物およびペプシン−トリプシン加水分解物
を得た。また乳カゼイン（和光純薬工業■製）に関して
は乳カゼインＬｏｇを水に溶解させたものに上述のトリ
プシン溶液１０ｔＱを用いて同様に処理してトリプシン
加水分解物を得た。For comparison, a pepsin hydrolyzate and a pepsin-trypsin hydrolyzate were obtained using marine beef (manufactured by Niigata Tekkosho ■) and yeast protein (manufactured by Masato ■) in the same manner as described above. Regarding milk casein (manufactured by Wako Pure Chemical Industries, Ltd.), a trypsin hydrolyzate was obtained by dissolving milk casein Log in water and treating it in the same manner using 10 tQ of the above-mentioned trypsin solution.
各加水分解物のアンジオテンシン転換酵素阻害活性の測
定はＣｕｓｈｍａｎとＣｈｅｕｎｇの方法（Ｂｉｏｃｈ
ｅ−。The angiotensin converting enzyme inhibitory activity of each hydrolyzate was measured using the method of Cushman and Cheung (Bioch
e-.
Ｐｈａｒｍａｃｏｌ、、 ２０． １６３７ （１
９７１） ） を改良して行った。Pharmacol, 20. 1637 (1
971)) was improved.
すなわち、１００ｍＭのホウ酸−炭酸ナトリウム緩衝液
（ｐＨ８，３，塩化ナトリウム３００ｍＭ。That is, 100mM boric acid-sodium carbonate buffer (pH 8.3, sodium chloride 300mM).
ヒプリルーヒスチジルーロイシン（Ｈｉｐｐ−Ｈｉｓ−
Ｌｅｕ ：ペプチド研究所製）５ｍＭを含有）０．５艷
に加水分解物５−を加え、３７℃で３分間保温した。Hipp-His-
Hydrolyzate 5- was added to 0.5 tubes (containing 5 mM of Leu (manufactured by Peptide Institute)) and kept at 37° C. for 3 minutes.
次に、これに酵素溶液〔ウサギ肺アセトン粉末（シグマ
社製）０．５ｇを５０＋Ｍホウ酸−炭酸ナトリウム緩衝
液（ｐＨ８，３）に懸濁させて得た上清液を酵素溶液（
０，０１ユニット１５０ｍ）とする）５０ｍを加えて３
７で３０分間反応させた。Next, an enzyme solution [a supernatant obtained by suspending 0.5 g of rabbit lung acetone powder (manufactured by Sigma) in a 50+M boric acid-sodium carbonate buffer (pH 8.3) was added to the enzyme solution (
0.01 unit 150m) Add 50m and 3
7 for 30 minutes.
反応後、ＩＮ−塩酸溶液０．５−加え、酢酸エチル３１
ＬＩ２を加えて１５分間撹拌後、酢酸エチル層から２−
を分取し、これを濃縮乾固した。得られた残渣を２ｄの
水に溶解させ、ＨＰＬＣ法で馬尿酸を定量する。After the reaction, add 0.5% of IN-hydrochloric acid solution and add 31% of ethyl acetate.
After adding LI2 and stirring for 15 minutes, 2-
was collected and concentrated to dryness. The obtained residue is dissolved in 2d water, and hippuric acid is quantified by HPLC method.
ＨＰＬＣの条件：
カラム：ＹＭＣＡＭ−３１２（ＩＩＩＹＭｃ製）溶出溶
媒：０．０５％トリフルオロ酢酸含有アセトニトリル
検 呂：２２８ｎ−の吸収
馬尿酸の量から相対的なアンジオテンシン転換酵素阻害
活性（相対阻害活性）を下記式により求めた。HPLC conditions: Column: YMCAM-312 (manufactured by IIIYMc) Elution solvent: Acetonitrile containing 0.05% trifluoroacetic acid Test: Relative angiotensin converting enzyme inhibitory activity (relative inhibitory activity) from the amount of absorbed hippuric acid of 228n- was calculated using the following formula.
Ａ、：加水分解物無添加時の馬尿酸の量Ａ ：加水分解
物添加時の馬尿酸の量
結果を第１表に示す。A: Amount of hippuric acid when no hydrolyzate is added A: Amount of hippuric acid when hydrolyzate is added The results are shown in Table 1.
第１表 第１表から明らかなように。Table 1 As is clear from Table 1.
ペプシン−トリゾ
シン処理後の相対阻害活性は卵白加水分解物のみが５０
％以上を維持し、他の蛋白原料を使用した場合にはいず
れも５０％以下の活性しか示さない。After pepsin-trizocine treatment, only egg white hydrolyzate had a relative inhibitory activity of 50%.
% or more, and when other protein raw materials are used, all of them show only 50% or less activity.
ゆえに、アンジオテンシン転換酵素阻害作用に基づく血
圧降下作用を有する加水分解物を調製する際の原料とし
て卵白が好適であることが示された。Therefore, it was shown that egg white is suitable as a raw material for preparing a hydrolyzate having a blood pressure lowering effect based on angiotensin converting enzyme inhibiting effect.
実施例 ２
卵白アルブミン（シグマ社製）および鶏卵から分離した
卵白を加熱して得られる加熱変性卵白を用いて、実施例
１と同様に処理して相対阻害活性を求めた。その結果を
第２表に示す。Example 2 Using ovalbumin (manufactured by Sigma) and heat-denatured egg white obtained by heating egg white separated from chicken eggs, the same treatment as in Example 1 was performed to determine the relative inhibitory activity. The results are shown in Table 2.
第２表
第２表から卵白原料としては卵白アルブミン、加熱変性
卵白を用いても乾燥卵白同様に相対阻害活性の高い加水
分解物を調製できることが確認された。Table 2 From Table 2, it was confirmed that a hydrolyzate with a high relative inhibitory activity can be prepared using ovalbumin or heat-denatured egg white as the raw material for egg white, similar to the case with dried egg white.
実施例 ３
実施例２と同様に加熱変性卵白を用いてペプシン−トリ
プシン加水分解物を調製後、該加水分解物１０１１１１
を試験管に分注した。Example 3 After preparing a pepsin-trypsin hydrolyzate using heat-denatured egg white in the same manner as in Example 2, the hydrolyzate 101111
was dispensed into test tubes.
この試験管を沸騰水浴上で１０分間加熱させた後、氷冷
水を用いて５分間冷却した。The test tube was heated on a boiling water bath for 10 minutes and then cooled using ice-cold water for 5 minutes.
加熱させたペプシン−トリプシン加水分解物と未加熱の
ペプシン−トリプシン分解物を実施例１と同様に処理し
て相対阻害活性を求めた。The heated pepsin-trypsin hydrolyzate and the unheated pepsin-trypsin hydrolyzate were treated in the same manner as in Example 1 to determine relative inhibitory activity.
その結果を第３表に示す。The results are shown in Table 3.
第３表
第３表から１本発明の卵白加水分解物は加熱処理によっ
てもアンジオテンシン酵素阻害活性の低下はほとんど認
められず、熱に対して安定であることが明らかとなった
。Table 3 Table 3 shows that the egg white hydrolyzate of the present invention showed almost no decrease in angiotensin enzyme inhibitory activity even after heat treatment, and was found to be stable against heat.
卵白原料を動物起源の蛋白分解酵素で加水分解して得た
本発明の卵白加水分解物は熱に対して安定であり、優れ
たアンジオテンシン転換酵素阻害活性を有し、血圧降下
作用を有する食品を調製するための食品素材として有用
である。The egg white hydrolyzate of the present invention obtained by hydrolyzing egg white raw material with an animal-derived protease is stable against heat, has excellent angiotensin converting enzyme inhibitory activity, and has a hypotensive effect. It is useful as a food material for preparation.
特に、実施例で行ったように卵白をまずペプシンで加水
分解し、次にトリプシンで加水分解したもの（ペプシン
−トリプシン加水分解物）は、これを摂取した場合であ
っても生体内の酵素で分解されて不活性化する危険性が
少なく、食品素材として好適である。In particular, when egg white is first hydrolyzed with pepsin and then with trypsin as in the example (pepsin-trypsin hydrolyzate), even when ingested, the enzymes in the body There is little risk of decomposition and inactivation, making it suitable as a food material.
Claims (1)
得られる血圧降下作用を有する卵白分解物またはその活
性画分。 ２）動物起源の蛋白分解酵素がペプシン、レンニン、ト
リプシン、キモトリプリン、パンクレアチン、エラスタ
ーゼ、カルボキシペプチダーゼ、アミノペプチダーゼ、
ジペプチダーゼから選ばれたものである請求項１記載の
卵白加水分解物またはその活性画分。 ３）血圧降下作用がアンジオテンシン転換酵素阻害に基
づくものである請求項１記載の卵白分解物またはその活
性画分。 ４）請求項１記載の卵白分解物またはその活性画分を成
分として含有する食品素材。 ５）請求項４記載の食品素材を含有する食品。[Scope of Claims] 1) An egg white decomposition product or an active fraction thereof having a blood pressure lowering effect obtained by hydrolyzing egg white with an animal-derived protease. 2) Proteolytic enzymes of animal origin include pepsin, rennin, trypsin, chymotrypurine, pancreatin, elastase, carboxypeptidase, aminopeptidase,
The egg white hydrolyzate or active fraction thereof according to claim 1, which is selected from dipeptidases. 3) The egg white decomposition product or active fraction thereof according to claim 1, wherein the blood pressure lowering effect is based on inhibition of angiotensin converting enzyme. 4) A food material containing the egg white decomposition product according to claim 1 or its active fraction as an ingredient. 5) A food containing the food material according to claim 4.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2084580A JPH03280835A (en) | 1990-03-29 | 1990-03-29 | Decomposition product of glair and food containing same decomposition product |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2084580A JPH03280835A (en) | 1990-03-29 | 1990-03-29 | Decomposition product of glair and food containing same decomposition product |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH03280835A true JPH03280835A (en) | 1991-12-11 |
Family
ID=13834616
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2084580A Pending JPH03280835A (en) | 1990-03-29 | 1990-03-29 | Decomposition product of glair and food containing same decomposition product |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH03280835A (en) |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1867237A1 (en) * | 2006-06-15 | 2007-12-19 | Nestec S.A. | Hypoallergenic Egg |
| JP2008507270A (en) * | 2004-07-22 | 2008-03-13 | グロバス・エッグ・サイエンスィス・ビー．ブイ． | Antihypertensive functional food |
| JP2009263308A (en) * | 2008-04-28 | 2009-11-12 | Taiyo Kagaku Co Ltd | Anti-inflammatory agent |
| JPWO2011126054A1 (en) * | 2010-04-07 | 2013-07-11 | 国立大学法人京都大学 | Bioactive peptide |
| CN107163130A (en) * | 2017-06-08 | 2017-09-15 | 广西大学 | A kind of inhibiting peptide of tonin and its preparation extracting method |
| EP4079315A4 (en) * | 2019-12-19 | 2024-01-24 | Nat Ct Child Health & Dev | Egg allergy preventing agent or the like, and food composition containing same |
-
1990
- 1990-03-29 JP JP2084580A patent/JPH03280835A/en active Pending
Cited By (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008507270A (en) * | 2004-07-22 | 2008-03-13 | グロバス・エッグ・サイエンスィス・ビー．ブイ． | Antihypertensive functional food |
| US8753698B2 (en) | 2004-07-22 | 2014-06-17 | Globus Egg Sciences B.V. | Anti-hypertensive functional food products |
| EP1867237A1 (en) * | 2006-06-15 | 2007-12-19 | Nestec S.A. | Hypoallergenic Egg |
| WO2007144398A1 (en) | 2006-06-15 | 2007-12-21 | Nestec S.A. | Hydrolysed egg proteins |
| US8062862B2 (en) | 2006-06-15 | 2011-11-22 | Nestec S.A. | Hydrolysed egg proteins |
| AU2007259232B2 (en) * | 2006-06-15 | 2012-12-13 | Nestec S.A. | Hydrolysed egg proteins |
| JP2009263308A (en) * | 2008-04-28 | 2009-11-12 | Taiyo Kagaku Co Ltd | Anti-inflammatory agent |
| JPWO2011126054A1 (en) * | 2010-04-07 | 2013-07-11 | 国立大学法人京都大学 | Bioactive peptide |
| CN107163130A (en) * | 2017-06-08 | 2017-09-15 | 广西大学 | A kind of inhibiting peptide of tonin and its preparation extracting method |
| EP4079315A4 (en) * | 2019-12-19 | 2024-01-24 | Nat Ct Child Health & Dev | Egg allergy preventing agent or the like, and food composition containing same |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Liu et al. | Bioactive peptides derived from egg proteins: A review | |
| Benjakul et al. | Fish protein hydrolysates: production, bioactivities, and applications | |
| JP5048487B2 (en) | Antihypertensive functional food | |
| US5356637A (en) | Method for preparing an enzymatic hydrolysate | |
| EP1568377A1 (en) | Cysteine protease inhibitor | |
| Grzonka et al. | Cysteine proteases | |
| JP2007523045A (en) | Bioactive peptide derived from egg white protein by enzymatic hydrolysis | |
| Bao et al. | Comparison of ACE inhibitory activity in skimmed goat and cow milk hydrolyzed by alcalase, flavourzyme, neutral protease and proteinase K | |
| US4853231A (en) | Method for preparation of tastable matters consisting primarily of low molecular weight peptides | |
| Itou et al. | Antihypertensive effect of heshiko, a fermented mackerel product, on spontaneously hypertensive rats | |
| US20060193930A1 (en) | Process for the preparation of protein hydrolysate from legumes | |
| JPH03280835A (en) | Decomposition product of glair and food containing same decomposition product | |
| JPH05276896A (en) | Peptide mixture having high fisher ratio, its production and nutrient-supplying composition for hepatic disease patient | |
| Hayes | Marine By‐Products as a Source of Proteins for Potential Food, Pharma, and Agricultural Feed Use | |
| JPS62169732A (en) | Hypotensor | |
| KR20130012688A (en) | Manufacture method of mineral binding peptides from barley bran proteins | |
| JP2006513716A (en) | Process for the preparation of angiotensin converting enzyme (ACE) inhibitors and uses thereof | |
| ZA200306957B (en) | Process for preparation of protein hydrolysate from soy flour. | |
| JP2007297324A (en) | Peptide, method for producing the same and angiotensin-converting enzyme inhibitor | |
| Permadi et al. | The potential of hydrolysate from rabbit meat protein as an angiotensin converting enzyme inhibitor | |
| BRPI0116968B1 (en) | Process for the preparation of a high protein hydrolyzate | |
| Chen et al. | Production of Angiotensin-I-Converting Enzyme inhibitory peptide from goat milk casein: optimization conditions of complex protease hydrolysate by response surface methodology and purification | |
| JP2022102874A (en) | Elastin peptide | |
| JPH0375144B2 (en) | ||
| Batista | Biological Activities of Fish‐protein Hydrolysates |