JPH05209000A - Peptide composition having decreased allergenicity - Google Patents
Peptide composition having decreased allergenicityInfo
- Publication number
- JPH05209000A JPH05209000A JP3358445A JP35844591A JPH05209000A JP H05209000 A JPH05209000 A JP H05209000A JP 3358445 A JP3358445 A JP 3358445A JP 35844591 A JP35844591 A JP 35844591A JP H05209000 A JPH05209000 A JP H05209000A
- Authority
- JP
- Japan
- Prior art keywords
- whey protein
- molecular weight
- lactoglobulin
- composition
- peptide composition
- 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
- 239000000203 mixture Substances 0.000 title claims abstract description 59
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 42
- 230000003247 decreasing effect Effects 0.000 title abstract 2
- 108010046377 Whey Proteins Proteins 0.000 claims abstract description 50
- 102000007544 Whey Proteins Human genes 0.000 claims abstract description 49
- 235000021119 whey protein Nutrition 0.000 claims abstract description 47
- 102000008192 Lactoglobulins Human genes 0.000 claims abstract description 23
- 108010060630 Lactoglobulins Proteins 0.000 claims abstract description 23
- 150000001413 amino acids Chemical class 0.000 claims abstract description 20
- 235000019658 bitter taste Nutrition 0.000 claims abstract description 18
- 239000002994 raw material Substances 0.000 claims abstract description 12
- 239000007864 aqueous solution Substances 0.000 claims abstract description 7
- 239000001096 (4-ethenyl-1-azabicyclo[2.2.2]octan-7-yl)-(6-methoxyquinolin-4-yl)methanol hydrochloride Substances 0.000 claims abstract description 6
- NNKXWRRDHYTHFP-HZQSTTLBSA-N (r)-[(2s,4s,5r)-5-ethenyl-1-azabicyclo[2.2.2]octan-2-yl]-(6-methoxyquinolin-4-yl)methanol;hydron;dichloride Chemical compound Cl.Cl.C([C@H]([C@H](C1)C=C)C2)CN1[C@@H]2[C@H](O)C1=CC=NC2=CC=C(OC)C=C21 NNKXWRRDHYTHFP-HZQSTTLBSA-N 0.000 claims abstract description 6
- 108091005804 Peptidases Proteins 0.000 claims abstract description 6
- 102000035195 Peptidases Human genes 0.000 claims abstract description 6
- 229960001811 quinine hydrochloride Drugs 0.000 claims abstract description 6
- 238000002965 ELISA Methods 0.000 claims abstract description 5
- 230000005764 inhibitory process Effects 0.000 claims abstract description 5
- 102000004190 Enzymes Human genes 0.000 claims description 20
- 108090000790 Enzymes Proteins 0.000 claims description 20
- 230000000774 hypoallergenic effect Effects 0.000 claims description 6
- 241000196324 Embryophyta Species 0.000 claims description 3
- 241001465754 Metazoa Species 0.000 claims description 3
- 244000005700 microbiome Species 0.000 claims description 3
- 102000004157 Hydrolases Human genes 0.000 claims 1
- 108090000604 Hydrolases Proteins 0.000 claims 1
- 235000013305 food Nutrition 0.000 abstract description 5
- 239000003814 drug Substances 0.000 abstract description 3
- 230000002255 enzymatic effect Effects 0.000 abstract description 3
- 235000020247 cow milk Nutrition 0.000 abstract description 2
- 238000000354 decomposition reaction Methods 0.000 abstract description 2
- 230000000050 nutritive effect Effects 0.000 abstract 1
- 235000019833 protease Nutrition 0.000 abstract 1
- 239000000243 solution Substances 0.000 abstract 1
- 229940088598 enzyme Drugs 0.000 description 19
- 235000018102 proteins Nutrition 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 14
- 108090000623 proteins and genes Proteins 0.000 description 14
- 235000016709 nutrition Nutrition 0.000 description 10
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- 239000006228 supernatant Substances 0.000 description 8
- 239000004365 Protease Substances 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 238000010438 heat treatment Methods 0.000 description 7
- 238000004128 high performance liquid chromatography Methods 0.000 description 7
- 238000000034 method Methods 0.000 description 6
- 239000000843 powder Substances 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 108090000526 Papain Proteins 0.000 description 5
- 229940055729 papain Drugs 0.000 description 5
- 235000019834 papain Nutrition 0.000 description 5
- 108090000631 Trypsin Proteins 0.000 description 4
- 102000004142 Trypsin Human genes 0.000 description 4
- 239000013566 allergen Substances 0.000 description 4
- 239000005018 casein Substances 0.000 description 4
- 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 4
- 235000021240 caseins Nutrition 0.000 description 4
- 230000007071 enzymatic hydrolysis Effects 0.000 description 4
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 239000012588 trypsin Substances 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 102000004407 Lactalbumin Human genes 0.000 description 3
- 108090000942 Lactalbumin Proteins 0.000 description 3
- 102000014171 Milk Proteins Human genes 0.000 description 3
- 108010011756 Milk Proteins Proteins 0.000 description 3
- 239000005862 Whey Substances 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000000052 comparative effect Effects 0.000 description 3
- 230000003301 hydrolyzing effect Effects 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 235000021241 α-lactalbumin Nutrition 0.000 description 3
- 238000003556 assay Methods 0.000 description 2
- 208000010668 atopic eczema Diseases 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 235000013350 formula milk Nutrition 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 239000010985 leather Substances 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 235000021239 milk protein Nutrition 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 230000009469 supplementation Effects 0.000 description 2
- 208000004998 Abdominal Pain Diseases 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 108010004032 Bromelains Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 201000004624 Dermatitis Diseases 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 108010019160 Pancreatin Proteins 0.000 description 1
- 108010056079 Subtilisins Proteins 0.000 description 1
- 102000005158 Subtilisins Human genes 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 108090001109 Thermolysin Proteins 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 206010047700 Vomiting Diseases 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000000172 allergic effect Effects 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 235000020244 animal milk Nutrition 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- -1 aromatic amino acid Chemical class 0.000 description 1
- 235000019835 bromelain Nutrition 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 230000006837 decompression Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 230000001804 emulsifying effect Effects 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000003505 heat denaturation Methods 0.000 description 1
- 235000020256 human milk Nutrition 0.000 description 1
- 210000004251 human milk Anatomy 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 108010009355 microbial metalloproteinases Proteins 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
- 230000035764 nutrition Effects 0.000 description 1
- 229940055695 pancreatin Drugs 0.000 description 1
- 108010043535 protease S Proteins 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 229940108461 rennet Drugs 0.000 description 1
- 108010058314 rennet Proteins 0.000 description 1
- 230000001953 sensory effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000003068 static effect Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 230000008673 vomiting Effects 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2250/00—Food ingredients
- A23V2250/54—Proteins
- A23V2250/542—Animal Protein
- A23V2250/5424—Dairy protein
- A23V2250/54244—Beta lactoglobulin
Landscapes
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
Description
【０００１】[0001]
【産業上の利用分野】本発明は低アレルゲン性ペプチド
組成物に関する。本発明の組成物は、牛乳由来の蛋白質
のアレルゲン性がなく、苦味がなく、高い栄養価を有す
るため、栄養補給に有用であり、食品原料、医薬品原料
として使用することができる。FIELD OF THE INVENTION The present invention relates to a hypoallergenic peptide composition. INDUSTRIAL APPLICABILITY The composition of the present invention has no allergenicity of milk-derived protein, has no bitterness, and has a high nutritional value, and thus is useful for nutritional supplementation and can be used as a food material or a drug material.
【０００２】[0002]
【従来の技術】乳蛋白質は重要な蛋白供給源であり、食
品として広く利用されている。乳蛋白質は主にレンネッ
トにより凝固するカゼイン画分と凝固しないホエー蛋白
質に分類される。チーズ製造時に生産されるホエーに
は、このホエー蛋白質が大量に含有されており、かって
は廃棄されていたが、ホエー蛋白質の栄養上の効果が認
識され現在はホエー蛋白質として回収され、ホエー蛋白
質濃縮物(WPC) などとして広く利用されている。またホ
エー蛋白質はカゼインと比較した場合、アミノ酸組成が
優れており、カゼインで不足気味の含硫アミノ酸やトリ
プトファンなども多く、その栄養学上の効果も確認され
ている。このため、近年では、ホエー蛋白質を添加し栄
養効果を高めた育児用調製粉乳が開発され、広く普及し
ている。BACKGROUND OF THE INVENTION Milk protein is an important protein source and is widely used as a food. Milk proteins are classified into a casein fraction that coagulates mainly by rennet and a whey protein that does not coagulate. The whey produced during cheese production contained a large amount of this whey protein, which was once discarded, but since the nutritional effect of whey protein was recognized, it is now recovered as whey protein and concentrated in whey protein. Widely used as things (WPC). In addition, whey protein has an excellent amino acid composition as compared with casein, and there are many sulfur-containing amino acids and tryptophan, which are deficient in casein, and their nutritional effects have been confirmed. For this reason, in recent years, infant formula has been developed in which whey protein has been added to enhance the nutritional effect, and it has become widespread.
【０００３】ホエー蛋白質は種々の蛋白質から構成され
ているが、その主要なものとしてα- ラクトアルブミン
とβ- ラクトグロブリンが挙げられる。ヒト乳のホエー
がβ- ラクトグロブリンを含まないのに対し、牛乳ホエ
ーはその蛋白質の約半分がβ- ラクトグロブリンである
ため、育児用調製粉乳にホエー蛋白質を添加した場合こ
の組成の違いが原因となり、しばしば乳児に対しアレル
ギー性の症状を引き起こす。このため、消化の際の下
痢、腹痛、嘔吐などの症状が発生する。また湿疹などの
症状が発生することもある。このためβ- ラクトグロブ
リンに由来するアレルギーを低減するため、加熱による
蛋白質の変性を行ったり、β- ラクトグロブリンのみを
除去したりする方法が提案されている。また最近はホエ
ー蛋白質を酵素により分解しアレルゲン性を低下させる
方法が提案されている。The whey protein is composed of various proteins, of which α-lactalbumin and β-lactoglobulin are major ones. Human milk whey does not contain β-lactoglobulin, whereas cow milk whey contains β-lactoglobulin in about half of its protein, and this difference in composition is caused when whey protein is added to infant formula. , Often causing allergic symptoms in infants. Therefore, symptoms such as diarrhea, abdominal pain, and vomiting during digestion occur. In addition, symptoms such as eczema may occur. For this reason, in order to reduce allergies derived from β-lactoglobulin, methods of denaturing proteins by heating or removing only β-lactoglobulin have been proposed. Recently, a method of degrading whey protein by an enzyme to reduce allergenicity has been proposed.
【０００４】例えば特開平2-2319号公報ではホエー蛋白
質をトリプシン処理し、次いで熱処理、トリプシン再処
理し、残存する酵素を失活させることによりアレルゲン
を実質的に含まない動物乳蛋白加水分解物の製造方法が
開示されている。また特開平2-138991号公報では、カゼ
インやホエー蛋白質をパンクレアチンなどで処理し、ゲ
ル濾過により分子量が1000以下で抗原性を示さず、遊離
アミノ酸含量が20％以下で芳香族アミノ酸含量が全アミ
ノ酸の1.0 ％である低分子ペプチドの製造方法が開示さ
れている。さらに特開平2-182155号公報にはキモトリプ
シンとトリプシンで処理し、その後分画分子量5000のUF
膜で分離することによる遊離アミノ酸含量が10％以下、
分子量5000以上のペプチド含量が0 〜5 ％の組成物が開
示されている。しかしこれらの組成物のアレルゲン性が
どれくらい低下するか確認されておらず、また遊離のア
ミノ酸が多いため風味で劣ると考えられる。[0004] For example, in Japanese Patent Laid-Open No. 2-2319, a whey protein is treated with trypsin, then heat-treated and re-treated with trypsin to deactivate the remaining enzyme, thereby hydrolyzing an animal milk protein hydrolyzate containing substantially no allergen. A manufacturing method is disclosed. Further, in JP-A-2-138991, casein and whey proteins are treated with pancreatin, etc., and molecular weight is 1000 or less by gel filtration and no antigenicity is shown, and free amino acid content is 20% or less and aromatic amino acid content is total. A method for producing a low molecular weight peptide having 1.0% of amino acids is disclosed. Further, JP-A-2-182155 discloses that UF with a cutoff molecular weight of 5000 is treated with chymotrypsin and trypsin.
Free amino acid content of less than 10% by separation with a membrane,
Disclosed are compositions having a peptide content of 0 to 5% with a molecular weight of 5000 or more. However, it has not been confirmed how much the allergenicity of these compositions is reduced, and it is considered that the flavor is inferior due to the large amount of free amino acids.
【０００５】本発明者らはこれらの先行文献に記載され
た方法では、β- ラクトグロブリンに由来するアレルゲ
ンがそれほど低下しないことを確認している。また蛋白
質が分解されて生成する苦味のあるペプチドにより、得
られる組成物に強い苦味が発生することも問題として指
摘されている。さらに膜処理等により、アミノ酸組成が
変化する可能性がありこの場合は栄養上好ましくない。The present inventors have confirmed that the methods described in these prior documents do not significantly reduce the allergen derived from β-lactoglobulin. It has also been pointed out that a strong bitterness is generated in the obtained composition due to a bittering peptide produced by protein decomposition. Furthermore, the amino acid composition may change due to membrane treatment or the like, and this is not preferable in nutrition.
【０００６】また、Hayashi らはホエー蛋白質の水溶液
に蛋白分解酵素であるサーモリシンを蛋白質5mg 当たり
5 μg 添加し、2000気圧、30℃、3 時間処理することに
よりβ- ラクトグロブリン画分の一部が電気泳動で消失
することを報告している(R.Hayashi et.al., Journal o
f Food Science, vol.52,1107-1108,1987) 。しかしこ
の方法で得られた組成物ではアルブミン画分は変化して
おらず、高分子の状態を維持している。またアレルゲン
として問題なβ- ラクトグロブリンも一部分解されてい
ない。[0006] Hayashi et al. Also added an aqueous solution of whey protein with thermolysin, a proteolytic enzyme, per 5 mg of protein.
It has been reported that a part of the β-lactoglobulin fraction disappears by electrophoresis after addition of 5 μg and treatment at 2000 atm and 30 ° C for 3 hours (R. Hayashi et.al., Journal o.
f Food Science, vol.52,1107-1108,1987). However, in the composition obtained by this method, the albumin fraction does not change, and the polymer state is maintained. Also, β-lactoglobulin, which is a problem as an allergen, is not partially decomposed.
【０００７】[0007]
【発明が解決しようとする課題】本発明者らはホエー蛋
白質の抗原性除去低下させた蛋白質素材について検討を
進めてきた。特に、ホエー蛋白質の栄養効果を維持さ
せ、かつ、消化吸収の優れたホエー蛋白質としての乳化
性をもった、低アレルゲン化ペプチドについて検討を進
めた結果、ホエー蛋白質を高圧に付した後、蛋白分解酵
素処理を行い、遠心分離により不溶解物を分離除去する
ことにより、目的とする低アレルゲン性のペプチド組成
物を得ることができることが判明した。したがって、本
発明はホエータンパク質より得られる苦味がなく低アレ
ルゲン性のペプチド組成物の提供を課題とする。DISCLOSURE OF INVENTION Problems to be Solved by the Invention The inventors of the present invention have proceeded with studies on a protein material having reduced antigenic elimination of whey protein. In particular, as a result of proceeding with studies on a hypoallergenic peptide that maintains the nutritional effect of whey protein and has an emulsifying property as a whey protein excellent in digestion and absorption, as a result of subjecting the whey protein to high pressure, proteolysis was performed. It was found that the target peptide composition having a low allergenicity can be obtained by performing enzyme treatment and separating and removing insoluble matter by centrifugation. Therefore, an object of the present invention is to provide a peptide composition obtained from whey protein, which has no bitterness and is hypoallergenic.
【０００８】[0008]
【課題を解決するための手段】本発明に得られるホエー
蛋白質より得られる低アレルゲン性ペプチド組成物は下
記の特徴を有している。 分子量 :分子量5000以上が10％以下、500 以下が20％
以下であり分子量500 乃至5000が70％以上のペプチド組
成を示す、 β- ラクトグロブリンに対するインヒビションELISA
試験がβ- ラクトグロブリンの1000分の１以下の値を示
す、 塩酸キニーネを基準とした苦味試験値が2 以下を示
す、 アミノ酸組成を分析した場合、原料であるホエー蛋白
質のアミノ酸組成に同じか又は近似している。The hypoallergenic peptide composition obtained from the whey protein according to the present invention has the following characteristics. Molecular weight: molecular weight 5000 or more is 10% or less, 500 or less is 20%
Inhibition ELISA against β-lactoglobulin, which has a peptide composition with a molecular weight of 500 to 5000 of 70% or more
The test shows a value less than 1/1000 that of β-lactoglobulin, the bitterness test value based on quinine hydrochloride is 2 or less, and when the amino acid composition is analyzed, it is the same as the amino acid composition of the whey protein as a raw material. Or it is close.
【０００９】本発明組成物は、ホエー蛋白質をアミノ酸
までは分解しておらず、また苦味ペプチドの発生し易い
ジ、トリペプチドに相当する分子量の画分が少ないた
め、苦味や異味が少ないことが特徴である。またアレル
ゲンであるβ- ラクトグロブリンは完全に消失してお
り、アレルゲン性は天然のβ- ラクトグロブリンの１/1
000 に低下している。Since the composition of the present invention does not decompose whey protein into amino acids and has a small fraction of the molecular weight corresponding to di- and tri-peptides in which bitter peptides are easily generated, bitterness and off-taste may be small. It is a feature. In addition, the allergen β-lactoglobulin has completely disappeared, and the allergenicity is 1/1 that of natural β-lactoglobulin.
It has dropped to 000.
【００１０】本発明のペプチド組成物を得るためには、
ホエー蛋白質水溶液を200MPa以上の高圧に付した後、蛋
白分解酵素により加水分解し、次いで残渣を遠心分離し
た上清より得ることができる。本発明に使用する高圧装
置としては、市販の装置の一例として三菱重工（株）製
高圧試験装置MCT-150 などを例示できる。またこれ以外
の装置であってもよい。To obtain the peptide composition of the present invention,
It can be obtained from the supernatant obtained by subjecting the whey protein aqueous solution to a high pressure of 200 MPa or more, hydrolyzing it with a proteolytic enzyme, and then centrifuging the residue. Examples of the high-pressure device used in the present invention include a high-pressure test device MCT-150 manufactured by Mitsubishi Heavy Industries, Ltd. as an example of a commercially available device. Further, other devices may be used.
【００１１】ホエー蛋白質は水で5 〜30％、特に好まし
くは10〜20％濃度に溶解し、次いでpHを5 〜9 、特に好
ましくは6 〜8 に調整し、高圧に付する。高圧に付する
場合は上記のホエー蛋白質水溶液を静止圧200MPa以上、
特に好ましくは200 〜600MPaとし、温度20〜60℃、の条
件下で30分以内の処理時間とする。The whey protein is dissolved in water to a concentration of 5 to 30%, particularly preferably 10 to 20%, and then the pH is adjusted to 5 to 9, particularly preferably 6 to 8 and subjected to high pressure. When applying high pressure, the above whey protein aqueous solution should be applied at a static pressure of 200 MPa or more,
Particularly preferably, the treatment time is within 30 minutes under the conditions of 200 to 600 MPa and temperature of 20 to 60 ° C.
【００１２】次いで蛋白分解酵素を添加し酵素加水分解
を行う。蛋白分解酵素としては動物由来、植物由来、微
生物由来の酵素1 種または2 種以上の混合酵素が使用で
きる。本発明のペプチド組成物を得るためには動物由来
のトリプシン、植物由来のパパイン、ブロメライン、微
生物由来のプロレザー（天野製薬製) 、プロテアーゼS
(天野製薬製) 、アルカラーゼ2.4L（NOVO社製) 、ニュ
ートラーゼ1.5MG(NOVO社製) などが例示できる。これら
酵素の内、1 または2 種以上を選択して使用することが
好ましい。特にパパインとプロレザーの組み合わせは、
未分解の高分子ペプチドの残存がなく、本発明ペプチド
の収率が高く、特に好ましい。Next, a protease is added to carry out enzymatic hydrolysis. As the proteolytic enzyme, one kind of enzyme derived from animal, plant, or microorganism or a mixed enzyme of two or more kinds can be used. In order to obtain the peptide composition of the present invention, animal-derived trypsin, plant-derived papain, bromelain, microorganism-derived professional leather (manufactured by Amano Pharmaceutical Co., Ltd.), protease S
(Amano Pharmaceutical Co., Ltd.), Alcalase 2.4L (manufactured by NOVO), Neutrase 1.5MG (manufactured by NOVO), and the like. It is preferable to select and use one or more of these enzymes. Especially the combination of papain and professional leather,
It is particularly preferable because there is no undegraded polymer peptide remaining and the yield of the peptide of the present invention is high.
【００１３】酵素は、ホエー蛋白質1g当たり、酵素単位
50〜200unitsを添加し、0.5 〜10時間、40〜55℃で保持
し、酵素加水分解を行わせる。その後、蒸気により10〜
20分間加熱し、酵素を失活させた後、遠心分離を行い、
沈殿物を除去する。上清は凍結乾燥、噴霧乾燥を行い粉
末とすることができる。また液状のままあるいは濃縮液
としても得ることができる。また酵素反応に使用する酵
素は上述した酵素以外であっても使用可能であるが、使
用する酵素の比活性、至適反応条件下で加水分解を行わ
せれば良い。The enzyme is an enzyme unit per 1 g of whey protein.
Add 50-200units and hold at 40-55 ℃ for 0.5-10 hours to perform enzymatic hydrolysis. After that, 10 ~ by steam
After heating for 20 minutes to inactivate the enzyme, centrifuge,
Remove the precipitate. The supernatant can be freeze-dried and spray-dried to give a powder. It can also be obtained as a liquid or as a concentrated liquid. The enzyme used in the enzyme reaction may be other than the above-mentioned enzymes, but the specific activity of the enzyme used and the hydrolysis may be performed under optimum reaction conditions.
【００１４】得られた本発明ペプチド組成物はゲル濾過
や限外濾過などで分子量を測定する。本発明においては
TSKgel G3000PWXL 300×φ7.8 mm (東ソー製) を装着し
たHPLCクロマトグラフィーを用い、0.1 ％トリフルオロ
酢酸(TFA) を含む55％アセトニトリル(CH3CN) を溶媒と
して、0.3ml/分の流速で溶出し、210nm の吸光度を測定
してクロマトグラフィーを作成する。また、同様な操作
で分子量の判明している標準の蛋白質、ペプチドを溶出
しその溶出時間を測定する。図１及び表１にしめす分子
量と溶出時間の関係から、本発明のペプチド組成物の分
子量を測定できる。The molecular weight of the obtained peptide composition of the present invention is measured by gel filtration, ultrafiltration or the like. In the present invention
Using HPLC chromatography equipped with TSKgel G3000PW XL 300 × φ7.8 mm (Tosoh Corporation), using 55% acetonitrile (CH 3 CN) containing 0.1% trifluoroacetic acid (TFA) as a solvent, a flow rate of 0.3 ml / min. Elute with and measure the absorbance at 210 nm for chromatography. In the same manner, standard proteins and peptides of known molecular weight are eluted and the elution time is measured. From the relationship between the molecular weight shown in FIG. 1 and Table 1 and the elution time, the molecular weight of the peptide composition of the present invention can be measured.
【００１５】[0015]
【表１】 [Table 1]
【００１６】本発明ペプチドの抗原性は、酵素免疫測定
法（Enzyme-linked immunosolbentassay : ELISA)の抑
制試験（川瀬興三他、東邦医会誌、35巻 506頁、1989
年) に従ってβ- ラクトグロブリンを対照として行い、
β- ラクトグロブリンに対する抗原性として表記する。
本発明ペプチド組成物はβ- ラクトグロブリンの1000分
の1 の抗原性しか有しておらず、これは通常の酵素加水
分解法で製造したペプチド組成物よりさらに低い抗原性
である。The antigenicity of the peptide of the present invention is determined by an enzyme immunoassay assay (ELISA) inhibition test (Kawase Kozo et al., Toho Medical Journal, Vol. 35, p. 506, 1989).
Β-lactoglobulin as a control according to
Expressed as antigenicity against β-lactoglobulin.
The peptide composition of the present invention has only 1000 times less antigenicity than β-lactoglobulin, which is even lower in antigenicity than the peptide composition produced by the conventional enzymatic hydrolysis method.
【００１７】さらに、本発明ペプチド組成物は苦味の点
でも優れている。一般に蛋白質を酵素加水分解したペプ
チドは強い苦味をもつ。これは苦味物質である塩酸キニ
ーネを対照とする官能試験で評価できる。本発明ペプチ
ド組成物に対する苦味は、原料であるホエー蛋白質10％
水溶液に対し、塩酸キニーネを表２の割合で添加したも
のと比較して苦味点数で表記する。Furthermore, the peptide composition of the present invention is also excellent in bitterness. Generally, a peptide obtained by enzymatically hydrolyzing a protein has a strong bitterness. This can be evaluated by a sensory test using quinine hydrochloride, which is a bitter substance, as a control. The bitterness of the peptide composition of the present invention is 10% of whey protein as a raw material.
The quinine hydrochloride is added to the aqueous solution at the ratio shown in Table 2, and the bitterness score is shown.
【００１８】[0018]
【表２】 [Table 2]
【００１９】本発明ペプチドはおおむね1 〜2 の間で評
価されるが、通常の酵素加水分解法で製造したペプチド
組成物は2 〜3 またはそれ以上の評価をされる。The peptides of the present invention are generally evaluated between 1 and 2, while the peptide composition produced by the usual enzymatic hydrolysis method is evaluated for 2-3 or more.
【００２０】また本発明ペプチドは従来技術で開示され
ているような膜処理や分画操作を行わずに製造しうるた
めホエー蛋白質の持つアミノ酸組成をそのまま維持でき
る。これは、栄養上非常に重要な特徴である。Further, since the peptide of the present invention can be produced without performing membrane treatment or fractionation operation as disclosed in the prior art, the amino acid composition of whey protein can be maintained as it is. This is a very important nutritional feature.
【００２１】以下に実施例を示しさらに本発明を詳細に
説明する。The present invention will be described in more detail with reference to the following examples.
【実施例１】ホエー蛋白質100gを水750gで溶解し、水酸
化ナトリウムでpH8 に調整し、次いで28℃の温度で、20
0MPaの圧力下で10分間保持した。同様に400MPaの圧力下
で10分間、また600MPaに到達後即減圧の条件で加圧処理
を行った。加圧装置は三菱重工製MCT-150 を使用した。Example 1 100 g of whey protein was dissolved in 750 g of water, adjusted to pH 8 with sodium hydroxide, and then dissolved at a temperature of 28 ° C.
It was kept under a pressure of 0 MPa for 10 minutes. Similarly, pressure treatment was performed under a pressure of 400 MPa for 10 minutes, and immediately after reaching 600 MPa under the condition of decompression. The pressure device used was MCT-150 manufactured by Mitsubishi Heavy Industries.
【００２２】加圧終了後、パパイン（天野製薬製) 、プ
ロレザー（天野製薬製) をそれぞれホエー蛋白質1g当た
り、50units 、150unitsを添加混合し、蛋白質濃度を10
％になるように調整し、50℃で 6時間処理をした。その
後コッホ釜で20分間蒸気加熱し、酵素を失活させた。次
いで 7000rpm、または約5000G で遠心分離し、沈殿を除
去し、上清を回収した。さらにこの上清を凍結乾燥し乾
燥粉末として、200MPa加圧で68.4g 、400MPa加圧で64.5
g 、600MPa加圧で65.6g を得た。After completion of the pressurization, papain (manufactured by Amano Pharmaceutical Co., Ltd.) and Proleather (manufactured by Amano Pharmaceutical Co., Ltd.) were added and mixed at 50 units and 150 units per 1 g of whey protein, respectively, to give a protein concentration of 10
%, And treated at 50 ° C. for 6 hours. After that, steam heating was performed for 20 minutes in a Koch kettle to inactivate the enzyme. Then, the mixture was centrifuged at 7,000 rpm or about 5000 G to remove the precipitate and collect the supernatant. The supernatant was freeze-dried to give a dry powder, which was 68.4 g at 200 MPa pressure and 64.5 g at 400 MPa pressure.
65.6 g was obtained under pressure of 600 MPa.
【００２３】この粉末を0.05％の濃度で水に溶解し、20
μl を上述したHPLCに注入し分子量を測定した。また基
質として使用したホエー蛋白質を同濃度に調整しHPLCに
注入しそのクロマトグラムを得た。図2 に示すように本
発明ペプチド組成物は抗原性の原因となるβ- ラクトグ
ロブリンとα- ラクトアルブミンに相当するピークが完
全に消失していた。またこの組成物の70％以上の分子量
分布は 500〜5000の範囲に分布していた。クロマトグラ
ムから求めた分子量分布は下記表3 の結果であった。This powder was dissolved in water at a concentration of 0.05%,
The μl was injected into the above-mentioned HPLC to measure the molecular weight. The whey protein used as a substrate was adjusted to the same concentration and injected into HPLC to obtain its chromatogram. As shown in FIG. 2, the peptide composition of the present invention completely disappeared the peaks corresponding to β-lactoglobulin and α-lactalbumin, which cause antigenicity. The molecular weight distribution of 70% or more of this composition was in the range of 500 to 5000. The molecular weight distribution obtained from the chromatogram is the result shown in Table 3 below.
【００２４】[0024]
【表３】 [Table 3]
【００２５】[0025]
【実施例２】ホエー蛋白質100gを水750gで溶解し、水酸
化ナトリウムでpH8 に調整し、次いで50℃の温度で、20
0MPaの圧力下で10分間保持した。同様に400MPaの圧力下
で 5分間、また600MPaに到達後即減圧の条件で加圧処理
を行った。加圧装置は三菱重工製MCT-150 を使用した。Example 2 100 g of whey protein was dissolved in 750 g of water, adjusted to pH 8 with sodium hydroxide, and then heated at 50 ° C. for 20
It was kept under a pressure of 0 MPa for 10 minutes. Similarly, pressure treatment was performed under a pressure of 400 MPa for 5 minutes, and immediately after reaching 600 MPa under the condition of pressure reduction. The pressure device used was MCT-150 manufactured by Mitsubishi Heavy Industries.
【００２６】加圧終了後、パパイン（天野製薬製) 、プ
ロレザー（天野製薬製) をそれぞれホエー蛋白質1g当た
り、50units 、150unitsを添加混合し、蛋白質濃度を10
％になるように調整し、50℃で6 時間保持をした。その
後コッホ釜で20分間蒸気加熱し、酵素を失活させた。次
いで7000rpm で遠心分離し、沈殿を除去し、上清を回収
した。さらにこの上清を凍結乾燥し乾燥粉末として、20
0MPa加圧で70.0g 、400MPa加圧で73.7g 、600MPa加圧で
75.7g を得た。After completion of the pressurization, papain (manufactured by Amano Pharmaceutical Co., Ltd.) and proleather (manufactured by Amano Pharmaceutical Co., Ltd.) were added and mixed at 50 units and 150 units per 1 g of whey protein, respectively, to give a protein concentration of 10
% So that it was kept at 50 ° C. for 6 hours. After that, steam heating was performed for 20 minutes in a Koch kettle to inactivate the enzyme. Then, the mixture was centrifuged at 7,000 rpm to remove the precipitate, and the supernatant was recovered. The supernatant was freeze-dried to obtain a dry powder,
70.0g at 0MPa pressure, 73.7g at 400MPa pressure, 600MPa pressure
75.7g was obtained.
【００２７】この粉末を0.05％の濃度で水に溶解し、20
μl を上述したHPLCに注入し分子量を測定した。また基
質として使用したホエー蛋白質を同濃度に調整しHPLCに
注入しそのクロマトグラムを得た。図 3に示すように本
発明ペプチド組成物は抗原性の原因となるβ- ラクトグ
ロブリンとα- ラクトアルブミンに相当するピークが完
全に消失していた。またこの組成物の分子量分布は1000
〜3000の範囲に分布しており、分子量500以下の画分は
約15〜16％、5000以上の高分子は約 7〜9 ％であった。This powder was dissolved in water at a concentration of 0.05%,
The μl was injected into the above-mentioned HPLC to measure the molecular weight. The whey protein used as a substrate was adjusted to the same concentration and injected into HPLC to obtain its chromatogram. As shown in FIG. 3, the peptide composition of the present invention completely disappeared the peaks corresponding to β-lactoglobulin and α-lactalbumin, which are the causes of antigenicity. The molecular weight distribution of this composition is 1000
It was distributed in the range of ~ 3000, and the fraction with a molecular weight of 500 or less was about 15-16%, and the polymer with a molecular weight of 5000 or more was about 7-9%.
【００２８】[0028]
【比較例】本比較例においては、加熱変性を加えて酵素
処理を行って製造した例および、従来法の酵素処理のみ
で製造したペプチド組成物の製造例を示す。実施例1 、
2 と同様にホエー蛋白質100gを水750gで溶解し、水酸化
ナトリウムでpH8 に調整し、次いで60℃の温度で30分、
または75℃の温度で20分間あるいは90℃ 10 分間の加熱
条件で保持した。加熱処理終了後、パパイン（天野製薬
製)、プロレザー（天野製薬製) をそれぞれホエー蛋白
質1g当たり、50units 、 150units を添加混合し、蛋白
質濃度を10％になるように調整し、50℃で6 時間保持を
した。同様にホエー蛋白質を溶解、pH調整後直接酵素を
添加し酵素反応を行った。その後コッホ釜で20分間蒸気
加熱し、酵素を失活させた。次いで7000rpm で遠心分離
し、沈殿を除去し、上清を回収した。さらにこの上清を
凍結乾燥し乾燥粉末とした。[Comparative Example] In this comparative example, an example of producing by enzymatic treatment with heat denaturation and an example of producing a peptide composition produced only by conventional enzymatic treatment are shown. Example 1,
Similarly to 2, dissolve 100 g of whey protein with 750 g of water, adjust to pH 8 with sodium hydroxide, and then for 30 minutes at a temperature of 60 ° C.
Alternatively, it was kept at a temperature of 75 ° C for 20 minutes or at 90 ° C for 10 minutes. After the heat treatment, papain (manufactured by Amano Pharmaceutical Co., Ltd.) and Proleather (manufactured by Amano Pharmaceutical Co., Ltd.) were added and mixed with 50 units and 150 units per 1 g of whey protein, and the mixture was adjusted to a protein concentration of 10%. I kept time. Similarly, the whey protein was dissolved, the pH was adjusted, and then the enzyme was added directly to carry out the enzymatic reaction. After that, steam heating was performed for 20 minutes in a Koch kettle to inactivate the enzyme. Then, the mixture was centrifuged at 7,000 rpm to remove the precipitate, and the supernatant was recovered. Further, this supernatant was freeze-dried to obtain a dry powder.
【００２９】[0029]
【実施例３】本実施例においては、実施例1 、2 、比較
例において得られたペプチド組成物の抗原性試験および
苦味試験結果を示す。各ペプチド組成物の抗原性は、酵
素免疫測定法（Enzyme-linked immunosolbent assay :
ELISA)の抑制試験（川瀬興三他、東邦医会誌、35巻 506
頁、1989年)に従ってβ- ラクトグロブリンを対照とし
て行い、β- ラクトグロブリンに対する抗原性として測
定した。Example 3 In this example, the results of the antigenicity test and the bitterness test of the peptide compositions obtained in Examples 1 and 2 and Comparative Example are shown. The antigenicity of each peptide composition is determined by the enzyme-linked immunosolbent assay:
ELISA) inhibition test (Kouze Kozo et al., Toho Medical Association, Vol. 35, 506
Pg., 1989), β-lactoglobulin was used as a control, and the antigenicity to β-lactoglobulin was measured.
【００３０】また各ペプチド組成物の苦味試験結果とし
て、原料であるホエー蛋白質10％水溶液に対し、塩酸キ
ニーネを表1 の割合で添加したものと比較して苦味点数
で測定した。As a bitterness test result of each peptide composition, a bitterness score was measured in comparison with quinine hydrochloride added in a ratio of Table 1 to a 10% aqueous solution of whey protein as a raw material.
【００３１】結果を下記表４に示した。The results are shown in Table 4 below.
【表４】 [Table 4]
【００３２】本発明組成物は、苦味点数において従来の
方法に勝っており、また抗原性においても優れていた。
また加熱処理後の酵素処理によって製造したペプチド組
成物と比較しても苦味が少なく優れていることが明らか
であった。The composition of the present invention was superior to the conventional method in bitterness and was excellent in antigenicity.
It was also clear that the peptide composition had less bitterness and was superior to the peptide composition produced by the enzyme treatment after the heat treatment.
【００３３】[0033]
【実施例４】本実施例においては、本発明組成物のアミ
ノ酸組成の分析例を示す。実施例１によって得られた組
成物を試料として、常法により加水分解を行いアミノ酸
分析用試料とした。また同様に原料であるホエー蛋白質
をアミノ酸分析用試料とした。両試料とも高速アミノ酸
分析計を用いて分析を行った。結果を表５に示した。Example 4 In this example, an analysis example of the amino acid composition of the composition of the present invention will be shown. The composition obtained in Example 1 was used as a sample and hydrolyzed by a conventional method to give a sample for amino acid analysis. Similarly, whey protein as a raw material was used as a sample for amino acid analysis. Both samples were analyzed using a fast amino acid analyzer. The results are shown in Table 5.
【００３４】[0034]
【表５】 [Table 5]
【００３５】本発明組成物は原料であるホエー蛋白質の
アミノ酸組成と一致していた。The composition of the present invention was in agreement with the amino acid composition of the whey protein as a raw material.
【００３６】[0036]
【発明の効果】本発明のペプチド組成物はホエータンパ
ク質より得られ、苦味がなく低アレルゲン性であり、ま
たホエー蛋白質のアミノ酸組成を維持しており栄養効果
が高い。従って、栄養補給に有用であり、食品原料、医
薬品原料として使用することができる。EFFECTS OF THE INVENTION The peptide composition of the present invention is obtained from whey protein, has no bitterness and has a low allergenicity, maintains the amino acid composition of whey protein, and has a high nutritional effect. Therefore, it is useful for nutritional supplementation and can be used as a raw material for foods and a raw material for pharmaceuticals.
【図１】分子量の判明している標準蛋白質の分子量とHP
LCによる流出時間との関係を示す。[Fig. 1] Molecular weight and HP of standard protein of known molecular weight
The relation with the outflow time by LC is shown.
【図２】実施例１のペプチド組成物及び、原料であるホ
エー蛋白質のHPLCパターンを示す。FIG. 2 shows an HPLC pattern of the peptide composition of Example 1 and whey protein as a raw material.
【図３】実施例２のペプチド組成物及び、原料であるホ
エー蛋白質のHPLCパターンを示す。FIG. 3 shows an HPLC pattern of the peptide composition of Example 2 and whey protein as a raw material.
───────────────────────────────────────────────────── フロントページの続き (51)Int.Cl.5 識別記号 庁内整理番号 ＦＩ 技術表示箇所 Ｃ１２Ｐ 21/06 8214−4Ｂ ─────────────────────────────────────────────────── ─── Continuation of the front page (51) Int.Cl. 5 Identification code Office reference number FI technical display location C12P 21/06 8214-4B
Claims (2)
に付した後、蛋白分解酵素により酵素分解処理を行って
得ることのできる、次の性質を有する低アレルゲン化ペ
プチド組成物。 分子量5000以上が10％以下、500 以下が20％以下であ
り分子量500 乃至5000が70％以上のペプチド組成を示
す、 β- ラクトグロブリンに対するインヒビションELISA
試験がβ- ラクトグロブリンの1000分の１以下の値を示
す、 塩酸キニーネを基準とした苦味試験値が2 以下を示
す、 アミノ酸組成が原料のホエー蛋白質のアミノ酸組成に
同じか又は近似している。1. A hypoallergenic peptide composition having the following properties, which can be obtained by subjecting a whey protein aqueous solution to a pressure of 200 MPa or more and then enzymatically decomposing it with a proteolytic enzyme. Inhibition ELISA against β-lactoglobulin, showing a peptide composition in which a molecular weight of 5000 or more is 10% or less, 500 or less is 20% or less, and a molecular weight of 500 to 5000 is 70% or more.
The test shows a value of 1/1000 or less of β-lactoglobulin, the bitterness test value based on quinine hydrochloride is 2 or less, and the amino acid composition is the same as or close to the amino acid composition of the whey protein as a raw material. ..
由来の酵素を2 種類以上使用するものである請求項1 記
載の低アレルゲン化ペプチド組成物。2. The hypoallergenic peptide composition according to claim 1, wherein the protein hydrolase uses two or more kinds of enzymes derived from animals, plants and microorganisms.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP3358445A JPH05209000A (en) | 1991-12-27 | 1991-12-27 | Peptide composition having decreased allergenicity |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP3358445A JPH05209000A (en) | 1991-12-27 | 1991-12-27 | Peptide composition having decreased allergenicity |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH05209000A true JPH05209000A (en) | 1993-08-20 |
Family
ID=18459344
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP3358445A Pending JPH05209000A (en) | 1991-12-27 | 1991-12-27 | Peptide composition having decreased allergenicity |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH05209000A (en) |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0947229A (en) * | 1995-06-01 | 1997-02-18 | Oomu Nyugyo Kk | Low-bitter and low-allergenic lactic composition and its production |
| WO2008111562A1 (en) * | 2007-03-13 | 2008-09-18 | Snow Brand Milk Products Co., Ltd. | Whitening agent |
| JP2011015633A (en) * | 2009-07-08 | 2011-01-27 | Kao Corp | Bitter taste inhibitor |
| CN106290893A (en) * | 2016-07-18 | 2017-01-04 | 南昌大学 | A kind of based on Platinum Nanoparticles probe in detecting Lac Bovis seu Bubali beta lactoglobulin and the method for sensitization residue thereof |
| CN115530283A (en) * | 2022-09-29 | 2022-12-30 | 黑龙江飞鹤乳业有限公司 | Protein compositions |
| CN115697069A (en) * | 2020-02-19 | 2023-02-03 | 完美日股份有限公司 | Hypoallergenic recombinant milk proteins and compositions comprising the same |
-
1991
- 1991-12-27 JP JP3358445A patent/JPH05209000A/en active Pending
Cited By (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0947229A (en) * | 1995-06-01 | 1997-02-18 | Oomu Nyugyo Kk | Low-bitter and low-allergenic lactic composition and its production |
| WO2008111562A1 (en) * | 2007-03-13 | 2008-09-18 | Snow Brand Milk Products Co., Ltd. | Whitening agent |
| JP2008255090A (en) * | 2007-03-13 | 2008-10-23 | Snow Brand Milk Prod Co Ltd | Skin-bleaching agent |
| AU2008225531B2 (en) * | 2007-03-13 | 2013-06-20 | Megmilk Snow Brand Co., Ltd | Whitening agent |
| US9173902B2 (en) | 2007-03-13 | 2015-11-03 | Megmilk Snow Brand Co., Ltd. | Skin-whitening agent |
| JP2011015633A (en) * | 2009-07-08 | 2011-01-27 | Kao Corp | Bitter taste inhibitor |
| CN106290893A (en) * | 2016-07-18 | 2017-01-04 | 南昌大学 | A kind of based on Platinum Nanoparticles probe in detecting Lac Bovis seu Bubali beta lactoglobulin and the method for sensitization residue thereof |
| CN115697069A (en) * | 2020-02-19 | 2023-02-03 | 完美日股份有限公司 | Hypoallergenic recombinant milk proteins and compositions comprising the same |
| CN115530283A (en) * | 2022-09-29 | 2022-12-30 | 黑龙江飞鹤乳业有限公司 | Protein compositions |
| CN115530283B (en) * | 2022-09-29 | 2024-01-26 | 黑龙江飞鹤乳业有限公司 | Protein composition |
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