JPS63267298A - Polypeptide derived from corpuscular globin - Google Patents
Polypeptide derived from corpuscular globinInfo
- Publication number
- JPS63267298A JPS63267298A JP62099957A JP9995787A JPS63267298A JP S63267298 A JPS63267298 A JP S63267298A JP 62099957 A JP62099957 A JP 62099957A JP 9995787 A JP9995787 A JP 9995787A JP S63267298 A JPS63267298 A JP S63267298A
- Authority
- JP
- Japan
- Prior art keywords
- globin
- derived
- polypeptide
- proteolytic enzyme
- molecular weight
- 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
- 102000018146 globin Human genes 0.000 title claims abstract description 34
- 108060003196 globin Proteins 0.000 title claims abstract description 34
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 28
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 27
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 27
- 108091005804 Peptidases Proteins 0.000 claims abstract description 18
- 238000005187 foaming Methods 0.000 claims abstract description 18
- 102000035195 Peptidases Human genes 0.000 claims abstract description 17
- 241000193830 Bacillus <bacterium> Species 0.000 claims abstract description 6
- 210000004369 blood Anatomy 0.000 claims abstract description 6
- 239000008280 blood Substances 0.000 claims abstract description 6
- 230000007935 neutral effect Effects 0.000 claims abstract description 6
- 239000007864 aqueous solution Substances 0.000 claims abstract description 4
- 239000000203 mixture Substances 0.000 claims abstract description 3
- 150000001413 amino acids Chemical class 0.000 claims abstract 2
- 230000001804 emulsifying effect Effects 0.000 claims description 18
- 210000000601 blood cell Anatomy 0.000 claims description 14
- 238000004519 manufacturing process Methods 0.000 claims description 7
- 230000029087 digestion Effects 0.000 claims description 6
- 239000003995 emulsifying agent Substances 0.000 claims description 6
- 239000004088 foaming agent Substances 0.000 claims description 6
- 241000894006 Bacteria Species 0.000 claims description 3
- 239000007900 aqueous suspension Substances 0.000 claims 4
- 101100392772 Caenorhabditis elegans gln-2 gene Proteins 0.000 claims 1
- 101100228200 Caenorhabditis elegans gly-5 gene Proteins 0.000 claims 1
- 101100328158 Mus musculus Clmp gene Proteins 0.000 claims 1
- 101100170937 Mus musculus Dnmt1 gene Proteins 0.000 claims 1
- 239000006260 foam Substances 0.000 abstract description 13
- 238000006243 chemical reaction Methods 0.000 abstract description 10
- 102000004190 Enzymes Human genes 0.000 abstract description 8
- 108090000790 Enzymes Proteins 0.000 abstract description 8
- 239000000243 solution Substances 0.000 abstract description 7
- 239000000463 material Substances 0.000 abstract description 4
- 108090001109 Thermolysin Proteins 0.000 abstract description 2
- 239000002537 cosmetic Substances 0.000 abstract description 2
- 238000004108 freeze drying Methods 0.000 abstract description 2
- 235000021067 refined food Nutrition 0.000 abstract description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 238000000034 method Methods 0.000 description 8
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 229940088598 enzyme Drugs 0.000 description 6
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 5
- 239000002994 raw material Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 108010073771 Soybean Proteins Proteins 0.000 description 3
- 235000018102 proteins Nutrition 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 235000019710 soybean protein Nutrition 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 235000021120 animal protein Nutrition 0.000 description 2
- 239000005018 casein Substances 0.000 description 2
- 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 2
- 235000021240 caseins Nutrition 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 235000011121 sodium hydroxide Nutrition 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- LDMOEFOXLIZJOW-UHFFFAOYSA-N 1-dodecanesulfonic acid Chemical compound CCCCCCCCCCCCS(O)(=O)=O LDMOEFOXLIZJOW-UHFFFAOYSA-N 0.000 description 1
- 108090000145 Bacillolysin Proteins 0.000 description 1
- 101000973805 Bacillus caldolyticus Bacillolysin Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108010082495 Dietary Plant Proteins Proteins 0.000 description 1
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 108010054147 Hemoglobins Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102000035092 Neutral proteases Human genes 0.000 description 1
- 108091005507 Neutral proteases Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000003125 aqueous solvent Substances 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000002285 corn oil Substances 0.000 description 1
- 235000005687 corn oil Nutrition 0.000 description 1
- CBMPTFJVXNIWHP-UHFFFAOYSA-L disodium;hydrogen phosphate;2-hydroxypropane-1,2,3-tricarboxylic acid Chemical compound [Na+].[Na+].OP([O-])([O-])=O.OC(=O)CC(O)(C(O)=O)CC(O)=O CBMPTFJVXNIWHP-UHFFFAOYSA-L 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000002688 persistence Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 229940098458 powder spray Drugs 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/96—Cosmetics or similar toiletry preparations characterised by the composition containing materials, or derivatives thereof of undetermined constitution
- A61K8/98—Cosmetics or similar toiletry preparations characterised by the composition containing materials, or derivatives thereof of undetermined constitution of animal origin
- A61K8/981—Cosmetics or similar toiletry preparations characterised by the composition containing materials, or derivatives thereof of undetermined constitution of animal origin of mammals or bird
- A61K8/983—Blood, e.g. plasma
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Birds (AREA)
- Epidemiology (AREA)
- Zoology (AREA)
- Hematology (AREA)
- Dermatology (AREA)
- General Preparation And Processing Of Foods (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Cosmetics (AREA)
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分野〕
本発明は血球グロビン由来のポリペプチド及びその製造
法ならびにこのポリペプチドからなる乳化剤及び起泡剤
に関するものである。DETAILED DESCRIPTION OF THE INVENTION [Industrial Application Field] The present invention relates to a polypeptide derived from blood cell globin, a method for producing the same, and an emulsifier and foaming agent made of this polypeptide.
蛋白質やペプチド系の乳化性物質は、食品としての栄養
価が高いのみならず、保水性などの種々の機能特性を有
することから、合成低分子の界面活性剤に比べ特徴を有
し、また、その生体適合性ワ賢
から、種々の加工食 材として有用な物質である。Protein and peptide-based emulsifying substances not only have high nutritional value as food, but also have various functional properties such as water retention, so they have characteristics compared to synthetic low-molecular surfactants. Because of its biocompatibility, it is a useful substance as a variety of processed foods.
天然の原料としてよく用られているものに、動物性蛋白
質として乳カゼイン、植物性蛋白質として大豆蛋白質が
あげられる。いずれも、ある種度大量かつ安価に得るこ
とができるものであるが、それぞれに問題点を有する。Commonly used natural raw materials include milk casein as an animal protein and soybean protein as a vegetable protein. All of them can be obtained in large quantities and at low cost, but each has its own problems.
例えば、カゼインは乳臭、大豆蛋白質は大豆臭と呼ばれ
る特有の匂いを除去することが難しいこと、また大豆蛋
白質は数種の蛋白質を含み、不均一で巨大な分子量を有
するものであり、加工により均一なものを得るのが難し
いことなどがあげられる。これに対して、動物性蛋白質
源として大量かつ安価に得られ、しかも比較的均一組成
のものとして、血球から容易に得られるグロビンが注目
される。For example, casein has a milky odor, and soybean protein has a unique odor called soybean odor, which is difficult to remove.Also, soybean protein contains several types of proteins and has a heterogeneous and large molecular weight, so it is difficult to remove it through processing. Examples include difficulty in obtaining things. On the other hand, globin, which is easily obtained from blood cells, has attracted attention as a source of animal protein that can be obtained in large quantities at low cost and has a relatively uniform composition.
しかしながら血球ヘモグロビンから抽出・乾燥して得ら
れるグロビンは、中性付近忙等電点を有するため中性付
近では水にほとんど溶解しないため、食品や化粧品の素
材として用いるには難があり、また酸性、アルカリ性で
溶解しているグロビンも乳化力、起泡性等については満
足できるものではなかった。However, globin obtained by extracting and drying blood cell hemoglobin has an isoelectric point near neutrality, so it is hardly soluble in water near neutrality, making it difficult to use as a material for food or cosmetics. Even globin dissolved in alkaline conditions was not satisfactory in terms of emulsifying power, foaming ability, etc.
これを改善する目的で、血球蛋白質を水溶液中蛋白質分
解酵素で加水分解することにより、中性付近での溶解性
を向上させる試みがなされてきた。In order to improve this problem, attempts have been made to improve the solubility near neutrality by hydrolyzing blood cell proteins with proteolytic enzymes in an aqueous solution.
しかしながら従来の方法では溶解性は向上するものの、
加水分解が進みすぎ蛋白質としての機能が失われ、乳化
力等は著しく低下してしまうのが実状である。However, although conventional methods improve solubility,
The reality is that hydrolysis progresses too much, the protein function is lost, and emulsifying power etc. are significantly reduced.
本発明は、血液由来のグロビンを中性付近で水に懸濁状
態で仕込み、これに蛋白質分解酵素を作用させることに
より中性で水に良くとけ乳化力及び起泡力に優れた素材
である血球グロビン由来のポリペプチドを得ることがで
きることに基くものである。The present invention creates a material that is neutral, dissolves well in water, and has excellent emulsifying and foaming power by preparing blood-derived globin in a suspended state in water near neutrality and allowing proteolytic enzymes to act on it. This is based on the fact that polypeptides derived from blood cell globin can be obtained.
本発明のポリペプチドの原料とすることのできるグロビ
ンは、牛あるいは豚等のと畜の血球より種々の方法で調
製されたものを用いることができる。Globin that can be used as a raw material for the polypeptide of the present invention can be prepared from blood cells of slaughtered animals such as cows and pigs by various methods.
本発明のポリペプチドは上記グロビンまたは同含有物を
水性溶媒中に懸濁して蛋白質分解酵素で部分消化するこ
とによって製造することができる。The polypeptide of the present invention can be produced by suspending the above-mentioned globin or its contents in an aqueous solvent and partially digesting the suspension with a proteolytic enzyme.
その際のグロビンの濃度については懸濁状態となる濃度
であれば格別の限定はないが通常１ないし１５チ、好ま
しくは３ないし７チ（り／ ｄｔ）程度である。The concentration of globin at this time is not particularly limited as long as it is in a suspended state, but it is usually about 1 to 15 t, preferably about 3 to 7 dt.
使用する酵素については、種々の蛋白質分解酵素を用い
ることができるが、バチルス属（Ｂａｃｉｎｕｓ属）細
菌の耐熱性中性蛋白質分解酵素、例えばサーモライシン
などが特に望ましい。蛋白質分解酵素による部分消化の
際の酵素反応条件は、上述した様に基質であるグロビン
を懸濁状態として反応を開始させる以外％に従来と変わ
るところはない。As for the enzyme used, various proteolytic enzymes can be used, but heat-stable neutral proteolytic enzymes of bacteria belonging to the genus Bacillus, such as thermolysin, are particularly preferred. The enzyme reaction conditions for partial digestion with proteolytic enzymes are the same as before, except that the reaction is initiated with the substrate globin in a suspended state as described above.
蛋白質分解酵素の使用量は限定的ではないが、通常基質
であるグロビン１９に対して５０ないし２．００．０ユ
ニツト（酵素単位）程度、好ましくは２００ないし８０
０ユニット程度である。The amount of protease used is not limited, but it is usually about 50 to 2.00.0 units (enzyme units), preferably 200 to 80 units, relative to globin 19, which is the substrate.
It is about 0 units.
酵素反応の際の液性に関しては、使用酵素の作千幹素会
讃用領域であれば良いが、好ましくはグロビンが水に溶
けにくい領域すなわちｐＨ５〜１０、更に好ましくは６
〜９が選択される。反応温度については、酵素の作用に
適した領域と原料の調製条件や腐敗を考慮にいれて決定
すれば良いが、通常５℃〜８０℃（但し反応温度が６０
℃を越える場合は使用する酵素は耐熱性のものに限られ
る）。Regarding the liquid properties during the enzymatic reaction, it may be in the range where the enzyme used is used, but preferably it is in the range where globin is difficult to dissolve in water, that is, pH 5 to 10, more preferably pH 6.
~9 is selected. The reaction temperature can be determined by taking into account the region suitable for the action of the enzyme, the preparation conditions of the raw materials, and spoilage, but it is usually 5℃ to 80℃ (however, the reaction temperature is 60℃).
If the temperature exceeds ℃, use only heat-resistant enzymes).
好ましくは３０℃〜７０℃が選択される。反応時間は、
使用量及び反応温度によって変り得るが３０分〜２４時
間程度が望ましい。この反応によって懸濁状態にあった
グロビンは部分消化され、分子量約へ０００ないし４０
００程度となり、水溶液となる。Preferably, 30°C to 70°C is selected. The reaction time is
Although it may vary depending on the amount used and the reaction temperature, it is preferably about 30 minutes to 24 hours. Through this reaction, the globin in suspension is partially digested, and its molecular weight is reduced to approximately 40,000 to 40,000.
00 and becomes an aqueous solution.
侠雑物等に由来する不溶性物がある場合は、反応液から
濾過、遠心分離等の通常の固液分離手段を用いて除去し
てよい。If there are insoluble substances originating from foreign substances, they may be removed from the reaction solution using ordinary solid-liquid separation means such as filtration and centrifugation.
本発明のポリペプチドは必要に応じて蛋白質分解酵素を
除去または失活させたのち反応液から分離しないでその
まま用いることができる。The polypeptide of the present invention can be used as it is without being separated from the reaction solution after removing or inactivating the proteolytic enzyme if necessary.
得られた反応液を凍結乾燥、粉霧乾燥等の手段で乾燥す
ることにより、本発明のポリペプチドな得ることかでき
る。The polypeptide of the present invention can be obtained by drying the obtained reaction solution by freeze drying, powder spray drying, or the like.
この様な方法によって得られる本発明のポリペプチドは
平均分子量約へ００口ないし約４０００で、下記の様な
測定法で測定した乳化性及び起泡性がそれぞれ約１００
ないし約２００及び約（Ｌ５ないし約１を示す。The polypeptide of the present invention obtained by such a method has an average molecular weight of about 1,000 to about 4,000, and emulsifying and foaming properties of about 100 and 100, respectively, as measured by the following measuring method.
from about 200 and from about (L5 to about 1).
乳化性：２チ蛋白質溶液３０ｍにコーンオイル１０ゴを
加え、２５℃２分間ホモジカイズする。Emulsifying property: Add 10 g of corn oil to 30 m of the 2T protein solution and homogenize at 25°C for 2 minutes.
ここで得られたエマルジョンを純水とＳＤＳ （ドデシ
ルスルホン酸す十すウム）により１０００倍から５００
０倍に希釈する。その際ＳＤＳは、終濃度ｃＬ１％とな
るようにする。得られた希釈液について５００ ｎｍの
吸光度を測定する。The emulsion obtained here was mixed with pure water and SDS (sulfonate dodecyl sulfonate) to a concentration of 1000 to 500 times.
Dilute to 0x. At this time, SDS is adjusted to a final concentration of cL1%. The absorbance of the obtained diluted solution at 500 nm is measured.
起泡性：１５ｒｎ９窒素相当の試料を共栓付メスシリン
ダー（容量５０−）にとり、測定すべきｐＨの（ＬＯ２
Ｍクエン酸リン酸二ナトリウム緩衝液で２５−とする。Foaming property: Take a sample equivalent to 15rn9 nitrogen into a measuring cylinder with a stopper (capacity 50-), and adjust the pH (LO2) to be measured.
Make 25- with M citrate disodium phosphate buffer.
栓をし、垂直方向に毎秒２回の速度で１分振とうした後
、メスシリンダーを垂直に立て３分間静置後、泡の体積
を測定する。この体積（Ａ）とはじめの溶液の液量（２
５ｄ）との比を起泡性とする。After capping and shaking vertically for 1 minute at a speed of 2 times per second, the measuring cylinder was stood vertically and allowed to stand for 3 minutes, after which the volume of foam was measured. This volume (A) and the volume of the initial solution (2
5d) is defined as foaming property.
また、実施例中気泡安定性は以下の様にして測定した。In addition, bubble stability in the examples was measured as follows.
気泡安定性：前述の方法で起泡性を測定した後、そのま
ま２時間放置しふたたび泡の体積（Ｂ）を測定する。こ
の体積Ｂと起泡性測定時の泡の体積Ａとから求めた泡の
減少率（１００ＸＩ：Ａ−Ｂ）／Ａ）をもって気泡安定
性とする。Foam stability: After measuring the foamability using the method described above, the product is left to stand for 2 hours and the foam volume (B) is measured again. The foam stability is defined as the foam reduction rate (100XI:A-B)/A) determined from this volume B and the foam volume A at the time of foamability measurement.
本発明のポリペプチドは優れた乳化性、起泡性及び気泡
安定性を示し、乳化剤及び起泡剤として使用することが
できる。乳化剤又は起泡剤としての使用法及びその調製
法は慣用技術によることができる。The polypeptide of the present invention exhibits excellent emulsifying properties, foaming properties and foam stability, and can be used as an emulsifying agent and a foaming agent. Its use as an emulsifier or foaming agent and its preparation can be according to conventional techniques.
実施例１
豚の血球より抽出したグロビン（含水率７０％）１６１
．５９を純水に分散させ、１規定の苛性ソーダでｐＨ７
，５に調製し終−！１ｉ５０（１１）！Ｌｔとする。こ
れに、／＜？ルスステアロサーモフィラス（Ｂａ−・ａ
ｉ１１ｕ８−ｓｔｅａｒｏｔｈｅｒｍｏｐｈｉｌｕｓ
）由来の耐熱性中性プロテアーゼ１２．５＃を加え、５
０℃、２４時間反応させた後、これを噴霧乾燥し製品４
７グを得た。Example 1 Globin extracted from pig blood cells (water content 70%) 161
．． Disperse 59 in pure water and adjust the pH to 7 with 1N caustic soda.
, prepared in 5 and finished! 1i50 (11)! Let it be Lt. To this, /<? Rus stearothermophilus (Ba-・a
i11u8-stearothermophilus
), add 12.5 # of heat-stable neutral protease derived from
After reacting at 0°C for 24 hours, this was spray dried to obtain product 4.
I got 7g.
この試料について、上述の方法で乳化性を測定し、未処
理のグロビンと比較した。The emulsifying properties of this sample were measured by the method described above and compared with untreated globin.
実験結果は以下の通りである。The experimental results are as follows.
酵素未処理グロビンを１０（１１）とする。Let enzyme-untreated globin be 10 (11).
酵素処理グロビンは３０９チでありた。Enzyme-treated globin was 309 chi.
酵素処理をすることＫよって顕著な乳化性の向上がみら
れることがわかった。It was found that emulsifying properties were significantly improved by enzymatic treatment.
実施例２
豚の血球より抽出したグロビン（含水率７０％）１５０
ｇを純水に分散させ、１規定の苛性ソーダでｐＨ７，５
に調製し終量５００ｄとする。これに、バチルスステア
ロサーモフィラス（Ｂａｃｉｌｌｕθｓｔｅａｒｏｔｈ
ｅｒｍｏｐｈｉｌｕｓ ）由来の耐熱性中性プロテアー
ゼ１０ｑ（１ダ当たり５０００単位）を加え、５０’Ｃ
，２４時間反応させた後、これを噴霧乾燥し製品４５り
を得た。Example 2 Globin extracted from pig blood cells (water content 70%) 150
Disperse g in pure water and adjust the pH to 7.5 with 1N caustic soda.
The final amount is 500 d. In addition to this, Bacillus stearothermophilus (Bacillus θstearoth)
ermophilus) was added to the thermostable neutral protease 10q (5000 units per da) and incubated at 50'C.
After reacting for 24 hours, this was spray-dried to obtain 45 pieces of product.
この試料の起泡性、気泡安定性を前述の方法でＩ））！
７．５にて測定したところ第１表の通りであり、本発明
による改質グロビンの発泡性の向上が確認された。The foaming properties and foam stability of this sample were evaluated using the method described above.I))!
The results measured at 7.5 are as shown in Table 1, and it was confirmed that the foamability of the modified globin according to the present invention was improved.
第１表
傘数字は、測定された泡の減少率から安定性に換算した
ものを用いた。（つまり、減少率０で安定性１００チと
なる。）
〔発明の効果〕
本発明のポリペプチドは原料のグロビン粉末及び公知技
術によるその酵素消化物に比べ、中性で水圧法は乳化力
に優れ、しかも起泡力、気泡安定性とも優れており、特
に気泡安定性に著しく優れた素材である。The numbers in Table 1 are calculated by converting the measured foam reduction rate into stability. (In other words, the stability is 100% at a reduction rate of 0.) [Effects of the Invention] The polypeptide of the present invention is more neutral than the raw material globin powder and its enzymatic digest obtained by known techniques, and the hydraulic method has a lower emulsifying power. Moreover, it has excellent foaming power and foam stability, and is a material with particularly excellent foam stability.
本発明のポリペプチドからなる乳化剤は乳化性に侵れて
いる。また本発明のポリペプチドからなる起泡剤は起泡
性及び気泡持続性に優れている。The emulsifier comprising the polypeptide of the present invention has poor emulsifying properties. Further, the foaming agent comprising the polypeptide of the present invention has excellent foaming properties and foam persistence.
Claims (16)
００ないし２００、起泡性０．５ないし１の、水溶液中
で乳化力及び起泡性に優れた血球グロビン由来のポリペ
プチド。(1) Average molecular weight 8,000 to 3,000 emulsifying property 1
A polypeptide derived from blood cell globin having an excellent emulsifying power and foaming property in an aqueous solution, with a foaming property of 0.00 to 200 and a foaming property of 0.5 to 1.
％、Ａｓｎ３％、Ａｓｐ５％、Ｃｙｓ１％、Ｇｌｙ５％
、Ｇｌｎ２％、Ｇｌｕ７％、Ｈｉｓ８％、Ｌｅｕ１３％
、Ｌｙｓ９％、Ｍｅｔ１％、Ｐｈｅ７％、Ｐｒｏ４％、
Ｓｅｒ３％、Ｔｈｒ５％、Ｔｒｐ２％、Ｔｙｒ３％及び
Ｖａｌ１１％である特許請求の範囲第１項記載のポリペ
プチド。 蛋白質分解酵素(2) Its amino acid composition is approximately 7% Ala, 3% Arg.
%, Asn3%, Asp5%, Cys1%, Gly5%
, Gln2%, Glu7%, His8%, Leu13%
, Lys9%, Met1%, Phe7%, Pro4%,
The polypeptide according to claim 1, which has 3% Ser, 5% Thr, 2% Trp, 3% Tyr and 11% Val. proteolytic enzyme
解酵素で部分消化して得たものである特許請求の範囲第
１項または第２項記載のポリペプチド。(3) The polypeptide according to claim 1 or 2, which is obtained by partially digesting blood-derived globin with a proteolytic enzyme in an aqueous suspension thereof.
ｕｓ属）細菌由来の耐熱性中性蛋白質分解酵素を用いて
得たものである特許請求の範囲第（３）項記載のポリペ
プチド。(4) As a proteolytic enzyme, Bacillus spp.
The polypeptide according to claim (3), which is obtained using a heat-stable neutral proteolytic enzyme derived from a bacterium (genus U.S.).
る特許請求の範囲第３項または第４項記載のポリペプチ
ド。(5) The polypeptide according to claim 3 or 4, which is obtained by performing partial digestion at pH 6 to 9.
約３，０００となるまで行って得たものである特許請求
の範囲第３項ないし第５項のいずれかの項記載のポリペ
プチド。(6) The polypeptide according to any one of claims 3 to 5, which is obtained by performing partial digestion until the molecular weight of the product is about 8,000 to about 3,000. .
解酵素で部分消化することを特徴とする乳化力及び起泡
性に優れた血球由来のポリペプチドの製造法。(7) A method for producing a blood cell-derived polypeptide with excellent emulsifying power and foaming ability, which comprises partially digesting blood-derived globin with a proteolytic enzyme in its aqueous suspension.
ｌｕｓ属）細菌由来の耐熱性中性蛋白質分解酵素である
特許請求の範囲第７項記載の製造法。(8) The proteolytic enzyme used is Bacillus (Bacillus).
8. The production method according to claim 7, which is a heat-stable neutral proteolytic enzyme derived from a bacterium (of the genus Lus).
第７または第８項記載の製造法。(9) The manufacturing method according to claim 7 or 8, wherein the partial digestion is carried out at a pH of 6 to 9.
う特許請求の範囲第７項ないし第９項のいずれかの項記
載の製造法。(10) The production method according to any one of claims 7 to 9, in which partial digestion is carried out until the suspended state substantially disappears.
し３，０００となるまで行う特許請求の範囲第７項ない
し第１０項のいずれかの項記載の製造法。(11) The production method according to any one of claims 7 to 10, in which partial digestion is performed until the molecular weight of the product is approximately 8,000 to 3,000.
ないし３，０００、乳化性１００ないし２００、起泡性
０．５ないし１である特許請求の範囲第７項ないし第１
１項記載の製造法。(12) The resulting polypeptide has an average molecular weight of 8,000
Claims 7 to 1 have an emulsifying property of 100 to 3,000, an emulsifying property of 100 to 200, and a foaming property of 0.5 to 1.
The manufacturing method described in item 1.
性１００ないし２００、起泡性０．５ないし１の血球グ
ロビン由来のポリペプチドからなる乳化剤。(13) An emulsifier comprising a polypeptide derived from blood cell globin having an average molecular weight of 8,000 to 3,000, an emulsifying property of 100 to 200, and a foaming property of 0.5 to 1.
のグロビンをその水性懸濁液中蛋白質分解酵素で部分消
化して得たものである特許請求の範囲第１３項記載の乳
化剤。(14) The emulsifier according to claim 13, wherein the polypeptide derived from blood cell globin is obtained by partially digesting blood-derived globin with a proteolytic enzyme in an aqueous suspension thereof.
性１００ないし２００、起泡性０．５ないし１の血球グ
ロビン由来のポリペプチドからなる起泡剤。(15) A foaming agent comprising a polypeptide derived from blood cell globin having an average molecular weight of 8,000 to 3,000, emulsifying property of 100 to 200, and foaming property of 0.5 to 1.
のグロビンをその水性懸濁液中蛋白分解酵素で部分消化
して得たものである特許請求の範囲第１６項記載の起泡
剤。(16) The foaming agent according to claim 16, wherein the polypeptide derived from blood cell globin is obtained by partially digesting blood-derived globin with a proteolytic enzyme in an aqueous suspension thereof.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP62099957A JPS63267298A (en) | 1987-04-24 | 1987-04-24 | Polypeptide derived from corpuscular globin |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP62099957A JPS63267298A (en) | 1987-04-24 | 1987-04-24 | Polypeptide derived from corpuscular globin |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPS63267298A true JPS63267298A (en) | 1988-11-04 |
Family
ID=14261170
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP62099957A Pending JPS63267298A (en) | 1987-04-24 | 1987-04-24 | Polypeptide derived from corpuscular globin |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS63267298A (en) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008053767A1 (en) * | 2006-10-31 | 2008-05-08 | The Nisshin Oillio Group, Ltd. | PROCESS FOR PRODUCING γ-AMINOBUTYRIC ACID-CONTAINING COMPOSITION AND FOOD COMPRISING THE γ-AMINOBUTYRIC ACID-CONTAINING COMPOSITION |
| WO2008053766A1 (en) * | 2006-10-31 | 2008-05-08 | The Nisshin Oillio Group, Ltd. | Method for producing soymilk |
| CN108998492A (en) * | 2018-08-31 | 2018-12-14 | 南京钦润生物科技有限公司 | A kind of preparation method of globin |
-
1987
- 1987-04-24 JP JP62099957A patent/JPS63267298A/en active Pending
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008053767A1 (en) * | 2006-10-31 | 2008-05-08 | The Nisshin Oillio Group, Ltd. | PROCESS FOR PRODUCING γ-AMINOBUTYRIC ACID-CONTAINING COMPOSITION AND FOOD COMPRISING THE γ-AMINOBUTYRIC ACID-CONTAINING COMPOSITION |
| WO2008053766A1 (en) * | 2006-10-31 | 2008-05-08 | The Nisshin Oillio Group, Ltd. | Method for producing soymilk |
| JPWO2008053766A1 (en) * | 2006-10-31 | 2010-02-25 | 日清オイリオグループ株式会社 | Method for producing soymilk |
| JPWO2008053767A1 (en) * | 2006-10-31 | 2010-02-25 | 日清オイリオグループ株式会社 | Method for producing γ-aminobutyric acid-containing composition, food containing γ-aminobutyric acid-containing composition |
| CN108998492A (en) * | 2018-08-31 | 2018-12-14 | 南京钦润生物科技有限公司 | A kind of preparation method of globin |
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