JPS63215699A - Fractionation of egg yolk lipoprotein and egg yolk water-soluble protein - Google Patents
Fractionation of egg yolk lipoprotein and egg yolk water-soluble proteinInfo
- Publication number
- JPS63215699A JPS63215699A JP4590087A JP4590087A JPS63215699A JP S63215699 A JPS63215699 A JP S63215699A JP 4590087 A JP4590087 A JP 4590087A JP 4590087 A JP4590087 A JP 4590087A JP S63215699 A JPS63215699 A JP S63215699A
- Authority
- JP
- Japan
- Prior art keywords
- egg yolk
- water
- alginic acid
- protein
- livetin
- 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
- 108010000912 Egg Proteins Proteins 0.000 title claims abstract description 101
- 102000002322 Egg Proteins Human genes 0.000 title claims abstract description 101
- 235000013345 egg yolk Nutrition 0.000 title claims abstract description 98
- 210000002969 egg yolk Anatomy 0.000 title claims abstract description 97
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 49
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 49
- 238000005194 fractionation Methods 0.000 title claims 2
- 102000004895 Lipoproteins Human genes 0.000 title abstract 4
- 108090001030 Lipoproteins Proteins 0.000 title abstract 4
- 235000010443 alginic acid Nutrition 0.000 claims abstract description 45
- 229920000615 alginic acid Polymers 0.000 claims abstract description 45
- 239000000783 alginic acid Substances 0.000 claims abstract description 31
- 229960001126 alginic acid Drugs 0.000 claims abstract description 31
- 150000004781 alginic acids Chemical class 0.000 claims abstract description 28
- 239000007788 liquid Substances 0.000 claims abstract description 24
- 239000002244 precipitate Substances 0.000 claims abstract description 13
- 239000007787 solid Substances 0.000 claims abstract description 13
- 238000000034 method Methods 0.000 claims description 21
- 229940072056 alginate Drugs 0.000 claims description 14
- FHVDTGUDJYJELY-UHFFFAOYSA-N 6-{[2-carboxy-4,5-dihydroxy-6-(phosphanyloxy)oxan-3-yl]oxy}-4,5-dihydroxy-3-phosphanyloxane-2-carboxylic acid Chemical class O1C(C(O)=O)C(P)C(O)C(O)C1OC1C(C(O)=O)OC(OP)C(O)C1O FHVDTGUDJYJELY-UHFFFAOYSA-N 0.000 claims description 11
- 235000013305 food Nutrition 0.000 abstract description 7
- 239000003814 drug Substances 0.000 abstract description 2
- 239000002253 acid Substances 0.000 abstract 1
- 229940079593 drug Drugs 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 42
- 150000002632 lipids Chemical class 0.000 description 22
- 108010052522 livetin Proteins 0.000 description 15
- 239000006228 supernatant Substances 0.000 description 14
- -1 dextran sulfates Chemical class 0.000 description 12
- 238000012360 testing method Methods 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 235000004252 protein component Nutrition 0.000 description 8
- IXPNQXFRVYWDDI-UHFFFAOYSA-N 1-methyl-2,4-dioxo-1,3-diazinane-5-carboximidamide Chemical compound CN1CC(C(N)=N)C(=O)NC1=O IXPNQXFRVYWDDI-UHFFFAOYSA-N 0.000 description 6
- 239000000661 sodium alginate Substances 0.000 description 6
- 235000010413 sodium alginate Nutrition 0.000 description 6
- 229940005550 sodium alginate Drugs 0.000 description 6
- 229920001223 polyethylene glycol Polymers 0.000 description 5
- 238000011084 recovery Methods 0.000 description 5
- 239000012134 supernatant fraction Substances 0.000 description 5
- 239000002202 Polyethylene glycol Substances 0.000 description 4
- 229960000633 dextran sulfate Drugs 0.000 description 4
- 235000013601 eggs Nutrition 0.000 description 4
- 238000000265 homogenisation Methods 0.000 description 4
- DNIAPMSPPWPWGF-UHFFFAOYSA-N monopropylene glycol Natural products CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 4
- 230000001766 physiological effect Effects 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 238000003756 stirring Methods 0.000 description 4
- HDSBZMRLPLPFLQ-UHFFFAOYSA-N Propylene glycol alginate Chemical compound OC1C(O)C(OC)OC(C(O)=O)C1OC1C(O)C(O)C(C)C(C(=O)OCC(C)O)O1 HDSBZMRLPLPFLQ-UHFFFAOYSA-N 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 239000003960 organic solvent Substances 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 239000000770 propane-1,2-diol alginate Substances 0.000 description 3
- 235000010409 propane-1,2-diol alginate Nutrition 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- JQWAHKMIYCERGA-UHFFFAOYSA-N (2-nonanoyloxy-3-octadeca-9,12-dienoyloxypropoxy)-[2-(trimethylazaniumyl)ethyl]phosphinate Chemical compound CCCCCCCCC(=O)OC(COP([O-])(=O)CC[N+](C)(C)C)COC(=O)CCCCCCCC=CCC=CCCCCC JQWAHKMIYCERGA-UHFFFAOYSA-N 0.000 description 2
- 241000512259 Ascophyllum nodosum Species 0.000 description 2
- 241000271566 Aves Species 0.000 description 2
- 102100027992 Casein kinase II subunit beta Human genes 0.000 description 2
- 101710158100 Casein kinase II subunit beta Proteins 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 238000010908 decantation Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 239000004744 fabric Substances 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 235000013373 food additive Nutrition 0.000 description 2
- 239000002778 food additive Substances 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 150000003904 phospholipids Chemical class 0.000 description 2
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 238000011085 pressure filtration Methods 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- KGKMNZPJZKQEIF-ZIPLSDNGSA-N (2S,3S,4S,5S)-2,3,4,5-tetrahydroxy-6-oxohexanoic acid Chemical compound O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O.O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)O KGKMNZPJZKQEIF-ZIPLSDNGSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- 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 description 1
- 241000272517 Anseriformes Species 0.000 description 1
- 102000006410 Apoproteins Human genes 0.000 description 1
- 108010083590 Apoproteins Proteins 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 102000006395 Globulins Human genes 0.000 description 1
- 108010044091 Globulins Proteins 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- KGKMNZPJZKQEIF-YFRKJXKXSA-N O=C[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O.O=C[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O Chemical compound O=C[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O.O=C[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(=O)O KGKMNZPJZKQEIF-YFRKJXKXSA-N 0.000 description 1
- 241000199919 Phaeophyceae Species 0.000 description 1
- 241000286209 Phasianidae Species 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 229930182558 Sterol Natural products 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 229910052783 alkali metal Inorganic materials 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 102000023732 binding proteins Human genes 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 210000004958 brain cell Anatomy 0.000 description 1
- 229910001424 calcium ion Inorganic materials 0.000 description 1
- 229930183167 cerebroside Natural products 0.000 description 1
- 150000001784 cerebrosides Chemical class 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 210000000991 chicken egg Anatomy 0.000 description 1
- 229960001231 choline Drugs 0.000 description 1
- OEYIOHPDSNJKLS-UHFFFAOYSA-N choline Chemical compound C[N+](C)(C)CCO OEYIOHPDSNJKLS-UHFFFAOYSA-N 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 229960002086 dextran Drugs 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000005484 gravity Effects 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229910017604 nitric acid Inorganic materials 0.000 description 1
- WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 1
- XAEFZNCEHLXOMS-UHFFFAOYSA-M potassium benzoate Chemical compound [K+].[O-]C(=O)C1=CC=CC=C1 XAEFZNCEHLXOMS-UHFFFAOYSA-M 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 108010053455 riboflavin-binding protein Proteins 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 150000003432 sterols Chemical class 0.000 description 1
- 235000003702 sterols Nutrition 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Peptides Or Proteins (AREA)
Abstract
Description
【発明の詳細な説明】
（産業上の利用分野）
本発明は卵黄をリボタンパク質と水溶性タンパク質に分
画する方法に関する。DETAILED DESCRIPTION OF THE INVENTION (Industrial Field of Application) The present invention relates to a method for fractionating egg yolk into riboproteins and water-soluble proteins.
一般的に、新鮮な鶏卵黄は水分 ４８．０％、タンパク
質１７．８％、及び脂質３０５５％よりなる。卵黄脂質
は、その殆どが遊離の形では存在せず、種々の割合でタ
ンパク質と結合した巨大複合体、すなわちリボタンパク
質として存在する。Generally, fresh chicken egg yolk consists of 48.0% water, 17.8% protein, and 3055% fat. Most of the egg yolk lipids do not exist in free form, but exist in various proportions as large complexes bound to proteins, ie, riboproteins.
卵黄中には、脂質と結合していないタンパク質、すなわ
ち水溶性タンパク質も存在する。これらリボタンパク質
及び水溶性タンパク質は、卵黄固形分中の約９６％を占
める。Egg yolk also contains proteins that are not bound to lipids, ie, water-soluble proteins. These riboproteins and water-soluble proteins account for about 96% of the egg yolk solid content.
リボタンパク質は比重の違いにより、高密度リボタンパ
ク質と低密度リボタンパク質に分けられる。−１方、水
溶性タンパク質には、リベチン、ホスビチン及び微量の
りボフラビン結合性タンパク質が存在する。卵黄脂質の
成分としては、トリグリセライド及びホスホリピッドが
主要成分であり卵黄脂質中のそれぞれ６２．３％及び３
２．８％を占める。その他ステロール及びセレブロサイ
ドも存在する。Riboproteins can be divided into high-density riboproteins and low-density riboproteins depending on their specific gravity. -On the other hand, among the water-soluble proteins, there are livetin, phosvitin, and a trace amount of boflavin-binding protein. The main components of egg yolk lipids are triglycerides and phospholipids, which account for 62.3% and 3% of the egg yolk lipids, respectively.
It accounts for 2.8%. Other sterols and cerebrosides also exist.
この様に卵黄は脂質及びタンパク質を豊富に含むため、
従来より栄養的に優れた食品素材として広く利用されて
きた。As egg yolk is rich in fat and protein,
It has been widely used as a nutritionally superior food material.
近年、卵黄中の個々の成分に対する研究がすすみ、それ
ら個々の成分の有する生理活性が明らかかになってきた
。その中で特に注目されているのはリベチン及び卵黄レ
シチン（ホスポリピッド）である。In recent years, research on individual components in egg yolk has progressed, and the physiological activities of these individual components have become clear. Among them, livetin and egg yolk lecithin (phospolipid) have attracted particular attention.
リベチンはα−リベチン、β−リベチン、及び７−リベ
チンに分類される。α−１β−１及び７−リベチンは親
鳥の血清アルブミン、α−グリコプロティン、及び７−
グロブリンと免疫学的に同等であることが証明されてい
る。特に７−リベチンは卵黄中の免疫タンパク質として
、その有効利用が近年話題を集めている。Livetin is classified into α-livetin, β-livetin, and 7-livetin. α-1β-1 and 7-livetin are present in parent bird serum albumin, α-glycoprotein, and 7-
It has been shown to be immunologically equivalent to globulin. In particular, the effective use of 7-livetin as an immune protein in egg yolk has attracted attention in recent years.
卵黄レシチン（ホスポリピッド）は、その約７３％がホ
スファチジルコリンである。ホスファチジルロリンは脂
質二重膜（リポソーム）の主原料である。又、近年脳細
胞へのコリンの供給源としても注目されている。Egg yolk lecithin (phospolipid) is about 73% phosphatidylcholine. Phosphatidylloline is the main raw material for lipid bilayer membranes (liposomes). In recent years, it has also attracted attention as a source of choline to brain cells.
このように、種々の生理活性を有する卵黄成分のそれぞ
れを個別分離し、有効に利用することが卵黄の付加価値
をさらに高める為に必要である。In this way, it is necessary to separate each of the egg yolk components having various physiological activities and use them effectively in order to further increase the added value of egg yolk.
（従来の技術）
卵黄中、個々の成分の総合的な分離精製法は今だ開発さ
れていない。リボタンパク質と水溶性タンパク質との分
離が非常に困難であることが′この開発の遅れている原
因である。卵黄酒質の抽出は従来より有機溶媒を用いて
行なわれている。しかしながら、この方法では有機溶媒
により、卵黄タンパク質がかなりの変性を受けるため、
個々のタンパク質の有する生理活性はほとんど失われる
。(Prior art) A comprehensive separation and purification method for individual components in egg yolk has not yet been developed. The extremely difficult separation of riboproteins and water-soluble proteins is the reason for the delay in this development. Extraction of egg yolk liquor has traditionally been carried out using organic solvents. However, in this method, the egg yolk protein undergoes considerable denaturation due to the organic solvent.
Most of the physiological activities of individual proteins are lost.
従がって、卵黄脂質抽出残有からのこれらタンパク質の
個別分離精製は今だ行なわれていない。Therefore, individual separation and purification of these proteins from the egg yolk lipid extraction residue has not yet been carried out.
本発明者らは、卵黄中の生理活性を有する成分を分離精
製し、それぞれを有効利用することを目的として、卵黄
のりボタンバク質と水溶性タンパク質を分画する研究を
進めてきた。これに関する従来技術として次のものが文
献発表されている。The present inventors have been conducting research on fractionating egg yolk paste protein and water-soluble proteins with the aim of separating and purifying physiologically active components in egg yolk and effectively utilizing each component. The following prior art related to this has been published in literature.
ジエンセニウス（Ｊ、Ｃ，Ｊｅｎｓｅｎｉｕｓ）らは、
デキストラン硫酸とカルシュラムイオンにより卵黄リボ
タンパク質を沈殿許せ、その上清より７−リベチンの精
製を行なっている。［ジャーナル・才ブ・イムノロジカ
ル・メソッズ（Ｊ。J.C. Jensenius et al.
Egg yolk riboproteins are precipitated with dextran sulfate and calcium ions, and 7-libetin is purified from the supernatant. [Journal of Immunological Methods (J.
Ｉｍｍｕｎｏ １ 、Ｍｅｔｈｏｄｓ）４６巻、６３頁
（１９８１）コ ボルソン（Ａ、Ｍ、Ｐｏ１ｓｏｎ）ら
は、ポリエチレングリコールを用いて卵黄リボタンパク
質を沈殿させ、その上清より７−リベチンの精製を行な
っている。［イムノロジカル・コミユニケイジョン（Ｉ
ｍｍｕｎｏｌ、Ｃ。Immuno 1, Methods) Volume 46, Page 63 (1981) Ko Bolson (A, M, Polson) et al. precipitated egg yolk riboprotein using polyethylene glycol and purified 7-livetin from the supernatant. . [Immunological Communication (I)
mmunol, C.
ｍｍｕｎ、）９巻、４９５頁（１９８０）コ（発明が解
決しようとする問題点）
ジエンセニウス（Ｊ 、Ｃ，Ｊｅｎｓｅｎｉ ｕｓ）ら
、あるいはボルソン（Ａ、Ｍ、Ｐｏ１ｓｏｎ）らの方法
により、卵黄リボタンパク質の沈殿分前が可能であるが
、これらの方法は、食品添加物として認められていない
デキストラン硫酸あるいはポリエチレングリコールを用
いている為、食品工業的には利用できないという欠点が
ある。又、食品工業以外の分野でも最終的には、これら
デキストラン硫酸あるいはポリエチレングリコールの除
去が必要であるという煩わしさがある。(Problems to be Solved by the Invention) Egg yolk riboproteins were prepared by the method of Jensenius et al. or Polson A.M. However, these methods have the disadvantage that they cannot be used in the food industry because they use dextran sulfate or polyethylene glycol, which are not approved as food additives. Furthermore, even in fields other than the food industry, there is the inconvenience of finally having to remove these dextran sulfates or polyethylene glycols.
（問題点を序次する為の手段）
上記欠点を解消する為、本発明者らはこれらデキストラ
ン硫酸あるいはポリエチレングリコールと同等の作用を
有する物質を、ポリアニオン系の物質を中心にスクリー
ニングを行なった。その結果、アルギン酸、アルギン酸
塩あるいはアルギン酸誘導体を用いる卵黄リボタンパク
質の沈殿分離方法を開発した。(Means for Sequencing Problems) In order to eliminate the above-mentioned drawbacks, the present inventors screened substances having the same effect as these dextran sulfate or polyethylene glycol, focusing on polyanionic substances. As a result, we developed a method for precipitation and separation of egg yolk riboproteins using alginic acid, alginate salts, or alginic acid derivatives.
すなわち本発明は、卵黄液にアルギン酸、アルギン酸塩
あるいはアルギン酸誘導体の内より選ばれた一種以上を
加えることにより、卵黄リボタンパク質沈殿を生じさせ
、卵黄水溶性タンパク質を含む液性画分と分離すること
を特徴とする卵黄リボタンパク質と卵黄水溶性タンパク
質の分画方法に関する。That is, the present invention involves adding one or more selected from alginic acid, alginate salts, and alginic acid derivatives to the egg yolk liquid to produce an egg yolk riboprotein precipitate, which is then separated from a liquid fraction containing egg yolk water-soluble proteins. This invention relates to a method for fractionating egg yolk riboprotein and egg yolk water-soluble protein.
本発明における卵黄液とは、割卵後に卵白液と分離され
た生卵黄液あるいはそれを水で希釈した卵黄液、あるい
は卵黄粉末に加水し調製された卵黄液、あるいは冷凍卵
黄を邂凍して得られる卵黄液を言う。卵黄はニワトリ、
七面鳥、アヒル等の鳥類の卵から調製されたものであれ
ばよい。In the present invention, the egg yolk liquid refers to raw egg yolk liquid separated from egg white liquid after egg breaking, egg yolk liquid obtained by diluting it with water, egg yolk liquid prepared by adding water to egg yolk powder, or egg yolk liquid prepared by adding water to egg yolk powder, or by freezing frozen egg yolk. Refers to the resulting egg yolk liquid. Egg yolk is chicken,
It may be prepared from eggs of birds such as turkeys and ducks.
本発明におけるアルギン酸とは、Ｄ−マンヌロン酸（Ｄ
−Ｍａｎｎｕｒｏｎｉｃ ａｃｉｄ）とＬ−グルロン
酸（Ｌ−Ｇｕｌｕｒｏｎｉｃ ａｃｉｄ）のヘテロポ
リマーからなる有機高分子である。現在、一般的には昆
布、カジノ、アラメ等の褐藻類より抽出され℃いる。ア
ルギン酸塩とは、アルギン酸ナトリウム塩、カリウム塩
等のアルギン酸アルカリ金属塩、アルギン酸力ルシュウ
ム塩等のアルギン酸アルカリ上族塩、アルギン酸アルミ
ニウム族塩、アルギン酸アンモニウム塩、アルギン酸ト
リエタノールアミン等のアルギン酸のアミン塩、及び、
アルギン酸重金属塩を言う。アルギン酸誘導体とは、ア
ルギン酸プロピレングリコールエステル、アルギン酸の
硫酸エステル、硝酸エステル、及び、脂肪酸エステル等
の誘導体を言う。これらの中では、アルギン酸ナトリウ
ム塩及びアルギン酸プロピレングリコールエステル等、
食品衛生法上使用しうるものを月いることが望ましい。In the present invention, alginic acid refers to D-mannuronic acid (D
-Mannuronic acid) and L-Guluronic acid (L-Guluronic acid). Currently, it is generally extracted from brown algae such as kelp, kelp, and arame. Alginate refers to alginic acid alkali metal salts such as alginate sodium salt and potassium salt, alginate alkali upper group salts such as alginate lysium salt, alginate aluminum group salt, alginate ammonium salt, alginate amine salt such as alginate triethanolamine, as well as,
Refers to alginate heavy metal salts. The alginic acid derivative refers to derivatives such as alginic acid propylene glycol ester, alginic acid sulfate ester, nitric acid ester, and fatty acid ester. Among these, alginate sodium salt and alginate propylene glycol ester, etc.
It is desirable to use products that can be used under the Food Sanitation Act.
アルギン酸、アルギン酸塩あるいはアルギン酸誘導体の
添加量としては、卵黄固形分に対しアルギン酸として０
．１０重量％以上であればよい。The amount of alginic acid, alginate or alginic acid derivative added is 0% as alginic acid relative to the egg yolk solid content.
．． It is sufficient if it is 10% by weight or more.
それ未満では、アルギン酸による卵黄リボタンパク質の
沈殿形成は不充分である。又、卵黄処理液の全液量に対
するアルギン酸の添加量が多くなると卵黄処理液の粘度
が高くなり、卵黄リボタンパク質沈殿の分離が困難とな
る。その為、アルギン酸、アルギン酸塩あるいはアルギ
ン酸誘導体のアルギン酸としての添加量は、卵黄処理液
の全液量に対して０．５重量％以下となる様、加水量を
調整する方がその作業操作上望ましい。If the amount is less than that, precipitation of egg yolk riboprotein by alginic acid is insufficient. Furthermore, if the amount of alginic acid added to the total amount of the egg yolk treatment liquid increases, the viscosity of the egg yolk treatment liquid increases, making it difficult to separate the egg yolk riboprotein precipitate. Therefore, it is desirable for work operations to adjust the amount of water added so that the amount of alginic acid, alginate salt, or alginic acid derivative added as alginic acid is 0.5% by weight or less based on the total amount of the egg yolk treatment solution. .
卵黄リボタンパク質沈殿の分離方法としては、一般的に
は遠心分離が行なわれる。卵黄処理液の粘度が低ければ
、適当な濾布あるいは濾紙を用いた加圧濾過も可能であ
る。セライト等の濾過助剤を用いることにより、濾過効
率がよくなることは言うまでもない。又、デカンテーシ
ョンによる卵黄リボタンパク質の沈殿分離も可能である
。セライト等の濾過助剤を用いることによりさらに効率
よくデカンテーションが行なえる。Centrifugation is generally used to separate the egg yolk riboprotein precipitate. If the viscosity of the egg yolk treatment liquid is low, pressure filtration using a suitable filter cloth or paper is also possible. It goes without saying that the filtration efficiency is improved by using a filter aid such as Celite. It is also possible to separate the egg yolk riboprotein by precipitation by decantation. Decantation can be performed more efficiently by using a filter aid such as Celite.
試験例
卵黄固形分に対するアルギン酸の濃度と、上清中への脂
質及びタンパク質の回収率の関係を調べた。卵黄液Ｌｏ
ｇ（卵黄固形分 ５ｇ）に対して、アルギン酸ナトリウ
ムを溶解した水５０ｇを加える。アルギン酸ナトリウム
の濃度は卵黄固形分に対し、アルギン酸として、 ０
，０．０５，０．１０，０．３０，０．６０．及び１．
２０重量％となる様にした。攪拌による均質化後、遠心
分離（５，０ＯＯＧＸＩＯ分間）を行ない沈殿画分と上
清画分に分画した。その上清画分中の脂質量及びタンパ
ク質量を測定し、はじめの卵黄液中の総脂質量及び総タ
ンパク質量に対する回収率を求めた。Test Example The relationship between the concentration of alginic acid relative to the solid content of egg yolk and the recovery rate of lipids and proteins into the supernatant was investigated. Egg yolk liquid Lo
g (egg yolk solid content 5 g), add 50 g of water in which sodium alginate is dissolved. The concentration of sodium alginate is 0 as alginic acid relative to the egg yolk solid content.
,0.05,0.10,0.30,0.60. and 1.
The content was adjusted to 20% by weight. After homogenization by stirring, the mixture was centrifuged (5,0 OOGXIO minutes) and fractionated into a precipitate fraction and a supernatant fraction. The amount of lipid and protein in the supernatant fraction was measured, and the recovery rate relative to the total amount of lipid and total amount of protein in the initial egg yolk liquid was determined.
総脂質の定量方法は、フォルテ（Ｊ、Ｆｏｌｃｈ）法に
より総脂質を抽出後、有機溶媒を留去し残留物の重量を
総脂質量とした。［ザ・ジャーナル・才ブ・バイオロジ
カル・ケミストリー（Ｊ。To quantify the total lipids, total lipids were extracted by the Folch method, the organic solvent was distilled off, and the weight of the residue was taken as the total lipid amount. [The Journal of Biological Chemistry (J.
Ｂｉ ｏ １ 、Ｃｈｅｍ、）２２６巻、４９７頁（１
９５７）コ
タンパク質の定量方法は、リボタンパク質定量用に改良
されたローリ−（Ｌｏｗｒｙ）法を用いた。［マークウ
ェル（Ｍ、に、Ｍａｒｋｗｅ ｌ １）等、アナリテイ
カル・バイオケミストリー（Ａｎａｌ、Ｂｉｏｃｈｅｍ
、）８７巻、２０６頁（１９７８）］本試験例の結果を
表１に示す。Bio 1, Chem,) volume 226, page 497 (1
957) The method for quantifying coprotein used the Lowry method, which was improved for riboprotein quantification. [Analytical Biochemistry (Anal, Biochem) et al.
) Vol. 87, p. 206 (1978)] The results of this test example are shown in Table 1.
表１ 卵黄固形分に対するアルギン酸濃度と上清中への
タンパク質及び脂質の回収率卵黄固形分に対するアルギ
ン酸の濃度が、０８１０重量％以上では、上清中への脂
質の回収率が３％以下であった。又、その時の上清中へ
のタンパク質の回収率は約２０％であった。すなわち、
この条件下では、卵黄水溶性タンパク質が選択的に上清
中へ回収きれたと考えられる。Table 1 Alginic acid concentration with respect to egg yolk solid content and recovery rate of protein and lipid in supernatant When the concentration of alginic acid with respect to egg yolk solid content is 0.810% by weight or more, the recovery rate of lipid in supernatant is 3% or less. Ta. Moreover, the recovery rate of protein into the supernatant at that time was about 20%. That is,
It is considered that under these conditions, the egg yolk water-soluble protein was selectively recovered into the supernatant.
この点は、それら上清中のタンパク質成分を還元剤存在
化でのドデシル硫酸ナトリウム（ＳＤＳ）−ポリアクリ
ルアミドゲル電気泳動［ラムリー（Ｕ、に、Ｌａｅｍｍ
ｌｉ）ネイチャア−（Ｎａｔｕｒｅ）２２７巻、６８０
頁（１９７０）コで分析することにより確認された。す
なわち、それら上清中のタンパク質成分は、そのほとん
どが、α−リベチン、β−リベチン、及び７−リベチン
であった。 又、アルギン酸ナトリウムの代わりに、ア
ルギン酸プロピレングリコールエステルを用いて行なっ
た同様の試験でも表１とほぼ同様の結果が得られた。In this regard, the protein components in the supernatant were subjected to sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis in the presence of a reducing agent [Lumley et al.
li) Nature Volume 227, 680
This was confirmed by analysis by Page (1970). That is, most of the protein components in these supernatants were α-livetin, β-livetin, and 7-livetin. Further, in a similar test using propylene glycol alginate instead of sodium alginate, almost the same results as in Table 1 were obtained.
以上の事により、卵黄固形分に対するアルギン酸の濃度
が、０．１０重量％以上であれば、卵黄リボタンパク質
はそのほとんどが沈殿し、その上清中には、卵黄水溶性
タンパク質が選択的に回収されることが示された。As a result of the above, if the concentration of alginic acid relative to the egg yolk solid content is 0.10% by weight or more, most of the egg yolk riboproteins will precipitate, and the egg yolk water-soluble proteins will be selectively recovered in the supernatant. It was shown that
（実施例）
以下に本発明の実施例を示すが、これらによって本発明
を制限するものではない。(Example) Examples of the present invention are shown below, but the present invention is not limited by these.
実施例 １
卵黄液１００ｇ（卵黄固形分 ５０ｇ）に対してアルギ
ン酸ナトリウム０．４５ｇを溶解した水４００ｍ１を加
える。攪拌による均質化後、遠心分離（５，０ＯＯＧＸ
ＩＯ分間）を行ない沈殿画分と上清画分に分離した。沈
殿画分には、卵黄中総詣質の９８．５％及びタンパク質
の７８．２％が回収された。又、上清画分には、卵黄中
給脂質の１．０％及びタンパク質の２１．５％が回収さ
れた。Example 1 400 ml of water in which 0.45 g of sodium alginate was dissolved was added to 100 g of egg yolk liquid (50 g of egg yolk solid content). After homogenization by stirring, centrifugation (5,000 GX
IO minutes) to separate into a precipitate fraction and a supernatant fraction. In the precipitate fraction, 98.5% of the total protein and 78.2% of the protein in the egg yolk were recovered. Furthermore, 1.0% of the lipids and 21.5% of the proteins in the egg yolk were recovered in the supernatant fraction.
総脂質の定量及び、タンパク質の定量は試験例中に記載
した方法を用いた。The methods described in the test examples were used for quantifying total lipids and protein.
本実施例で得られた上清中のタンパク質成分を試験例と
同様、ドデシル硫酸ナトリウム（５ＤＳ）−ポリアクリ
ルアミドゲル電気泳動で分析した結果、そのほとんどが
α−リベチン、β−リベチン、及び７−リベチンであっ
た。The protein components in the supernatant obtained in this example were analyzed by sodium dodecyl sulfate (5DS)-polyacrylamide gel electrophoresis in the same manner as in the test example. As a result, most of the protein components were α-livetin, β-livetin, and 7-livetin. It was libetin.
実施例 ２
卵黄液１００ｇ（卵黄固形分 ５０ｇ）に対して、アル
ギン酸ナトリウム０．６ｇを溶解した水９００ｍ１を加
える。攪拌による均質化後、濾布を用いて加圧濾過によ
り、濾液画分と残香画分に分離した。残香画分には、卵
黄中給脂質の９９゜０％及びタンパク質の７５．４％が
回収された。Example 2 900 ml of water in which 0.6 g of sodium alginate was dissolved was added to 100 g of egg yolk liquid (50 g of egg yolk solid content). After homogenization by stirring, the mixture was separated into a filtrate fraction and a residual aroma fraction by pressure filtration using a filter cloth. In the residual aroma fraction, 99.0% of the lipids and 75.4% of the protein in the egg yolk were recovered.
又、濾液画分には、卵黄中給脂質の０．５％及びタンパ
ク質の２３．２％が回収された。Furthermore, 0.5% of the lipids and 23.2% of the proteins in the egg yolk were recovered in the filtrate fraction.
総脂質の定量及び、タンパク質の定量は試験例中に記載
した方法を用いた。The methods described in the test examples were used for quantifying total lipids and protein.
本実施例で得られた上清中のタンパク質成分を試験例と
同様、ドデシル硫酸ナトリウム（ＳＤＳ）−ポリアクリ
ルアミドゲル電気泳動で分析した結果、そのほとんどが
α−リベチン、β−リベチン、及び７−リベチンであっ
た。The protein components in the supernatant obtained in this example were analyzed by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis in the same manner as in the test example. As a result, most of the protein components were α-livetin, β-livetin, and 7-livetin. It was libetin.
実施例 ３
卵黄液１０Ｋｇ（卵黄固形分 ５Ｋｇ）に対してアルギ
ン酸プロピレングリコールエステル５０ｇを溶解した水
５０Ｋｇを加える。攪拌による均質化後、連続遠心分離
（５０００Ｇ）を行ない沈殿画分と上清画分に分離した
。沈殿画分には、卵黄中総詣質の９８．０％及びタンパ
ク質の７７゜８％が回収された。又、上清両分には、卵
黄中給脂質の０．８％及びタンパク質の２２．３％が回
収された。Example 3 To 10 kg of egg yolk liquid (egg yolk solid content: 5 kg), 50 kg of water in which 50 g of propylene glycol alginate was dissolved was added. After homogenization by stirring, continuous centrifugation (5000G) was performed to separate into a precipitate fraction and a supernatant fraction. In the precipitate fraction, 98.0% of the total protein and 77.8% of the protein in the egg yolk were recovered. Furthermore, 0.8% of the lipids and 22.3% of the proteins in the egg yolk were recovered in both supernatants.
総脂質の定量及び、タンパク質の定量は試験例中に記載
した方法を用いた。The methods described in the test examples were used for quantifying total lipids and protein.
本実施例で得られた上清中のタンパク質成分を試験例と
同様、ドデシル硫酸ナトリウム（５ＤＳ）−ポリアクリ
ルアミドゲル電気泳動で分析した結果、そのほとんどが
α−リベチン、β−リベチン、及び７−リベチンであっ
た。The protein components in the supernatant obtained in this example were analyzed by sodium dodecyl sulfate (5DS)-polyacrylamide gel electrophoresis in the same manner as in the test example. As a result, most of the protein components were α-livetin, β-livetin, and 7-livetin. It was libetin.
（発明の効果）
本発明によれば、ポリエチレングリコールやデキストラ
ン硫酸と比較し、より安価であるアルギン酸を用いるこ
とにより、卵黄をリボタンパク質からなる沈殿画分と、
卵黄水溶性タンパク質を含む液性画分に分画することが
できる。しかも、食品添加物として認められているアル
ギン酸ナトリウムあるいは、アルギン酸プロピレングリ
コールエステルを用いれば、本発明の方法により得られ
た卵黄リボタンパク質及び卵黄水溶性タンパク質は、医
薬品、化粧品用途のみならず、食品としても用いること
ができる。(Effects of the Invention) According to the present invention, by using alginic acid, which is cheaper than polyethylene glycol or dextran sulfate, egg yolk is converted into a precipitated fraction consisting of riboproteins.
Egg yolk can be fractionated into a liquid fraction containing water-soluble proteins. Furthermore, by using sodium alginate or propylene glycol alginate, which are approved as food additives, the egg yolk riboprotein and egg yolk water-soluble protein obtained by the method of the present invention can be used not only for pharmaceuticals and cosmetics, but also for foods. can also be used.
本発明により初めて、卵黄成分を個別に精製し、それぞ
れを有効利用することが可能となった。The present invention has made it possible for the first time to individually purify egg yolk components and utilize each component effectively.
即ち、リボタンパク質画分よりは、通常の方法により卵
Ｒレシチン（ホスホリピッド）、卵黄トリグリセライド
等の卵黄脂質及び、脂質のはずれたりボタンバク質（ア
ポタンパク質）あるいは、ホスビチンの精製が可能であ
る。又、水溶性タンパク質を含む液性画分よりはα−リ
ベチン、β−リベチン、７−リベチン、及びリボフラビ
ン結合性タンパク質等の精製が可能となる。That is, from the riboprotein fraction, it is possible to purify egg yolk lipids such as egg R lecithin (phospholipid) and egg yolk triglyceride, as well as lipids such as apoproteins and phosvitin. Furthermore, it is possible to purify α-livetin, β-livetin, 7-livetin, riboflavin-binding protein, etc. from the liquid fraction containing water-soluble proteins.
卵黄水溶性タンパク質の中で７−リベチンは、親鳥の免
疫タンパク質である７−グロブリンと同等である。本発
明の方法により分画された、卵黄水溶性タンパク質両分
は、この７−リベチンを多く含んでいる。従って、この
卵黄水溶性タンパク質画分は、動物あるいは人間、特に
免疫力の低下した老人、あるいは免疫力の弱いに乳幼児
の免疫力を高める食品としての利用が考えられる。Among egg yolk water-soluble proteins, 7-livetin is equivalent to 7-globulin, which is an immune protein of the parent bird. Both egg yolk water-soluble proteins fractionated by the method of the present invention contain a large amount of 7-livetin. Therefore, this egg yolk water-soluble protein fraction can be used as a food to enhance the immunity of animals or humans, especially elderly people with weakened immune systems, or infants with weak immune systems.
さらに、特異抗原により免疫された鳥類の卵を、本発明
の方法により処理すれば、その特異抗原に対する、特異
抗体である７−リベチンを卵黄水溶性タンパク質画分へ
回収することができる。Furthermore, if the eggs of birds immunized with a specific antigen are treated by the method of the present invention, 7-livetin, which is a specific antibody against the specific antigen, can be recovered into the egg yolk water-soluble protein fraction.
以上の様に、本発明によると、卵黄をリボタンパク質画
分及び水溶性タンパク質画分に簡単に分画できる為、そ
れぞれの両分より、個々の卵黄成分をその生理活性を失
うことなく精製することができる。As described above, according to the present invention, since egg yolk can be easily fractionated into a riboprotein fraction and a water-soluble protein fraction, individual egg yolk components can be purified from each of the two fractions without losing their physiological activity. be able to.
Claims (1)
ン酸誘導体の内より選ばれた一種以上を加えることによ
り、卵黄リボタンパク質沈殿を生じさせ、卵黄水溶性タ
ンパク質を含む液性画分と分離することを特徴とする卵
黄リボタンパク質と卵黄水溶性タンパク質の分画方法。 ２、アルギン酸、アルギン酸塩あるいはアルギン酸誘導
体の添加量が卵黄固形分に対し、アルギン酸として、０
．１０重量％以上である特許請求の範囲第一項記載の分
画方法。[Claims] 1. By adding one or more selected from alginic acid, alginate, or alginic acid derivatives to the egg yolk liquid, an egg yolk riboprotein precipitate is produced, and a liquid fraction containing egg yolk water-soluble protein is produced. A method for fractionating egg yolk riboprotein and egg yolk water-soluble protein, the method comprising separating egg yolk riboprotein and egg yolk water-soluble protein. 2. The amount of alginic acid, alginate or alginic acid derivative added is 0 as alginic acid to the egg yolk solid content.
．． The fractionation method according to claim 1, wherein the content is 10% by weight or more.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP4590087A JPS63215699A (en) | 1987-02-28 | 1987-02-28 | Fractionation of egg yolk lipoprotein and egg yolk water-soluble protein |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP4590087A JPS63215699A (en) | 1987-02-28 | 1987-02-28 | Fractionation of egg yolk lipoprotein and egg yolk water-soluble protein |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPS63215699A true JPS63215699A (en) | 1988-09-08 |
Family
ID=12732117
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP4590087A Pending JPS63215699A (en) | 1987-02-28 | 1987-02-28 | Fractionation of egg yolk lipoprotein and egg yolk water-soluble protein |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS63215699A (en) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH03204898A (en) * | 1989-10-16 | 1991-09-06 | Kanebo Ltd | Fractuation of water-soluble yolk protein |
-
1987
- 1987-02-28 JP JP4590087A patent/JPS63215699A/en active Pending
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH03204898A (en) * | 1989-10-16 | 1991-09-06 | Kanebo Ltd | Fractuation of water-soluble yolk protein |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US20200296991A1 (en) | Fresh water methods for reduced fluorine crustacean compositions | |
| JP4181305B2 (en) | Methods for extracting lipids from marine and freshwater animal tissues | |
| EP0368864B1 (en) | Whey protein fractions | |
| DE3767077D1 (en) | METHOD FOR SEPARATING CHOLESTEROL FROM FAT SUBSTANCES OF ANIMAL ORIGIN AND LOW CHOLESTEROL FAT SUBSTANCES. | |
| JPH0678360B2 (en) | Method for fractionating egg yolk lipoprotein and egg yolk water-soluble protein | |
| JP2805522B2 (en) | Method for fractionating and purifying phospholipid fraction derived from milk or dairy products | |
| Hrynets et al. | Impact of citric acid and calcium ions on acid solubilization of mechanically separated turkey meat: Effect on lipid and pigment content | |
| Saunders et al. | The cholesterol solubilizing capacity of lecithins in aqueous solutions of bile salt | |
| JPS63215699A (en) | Fractionation of egg yolk lipoprotein and egg yolk water-soluble protein | |
| DE3422111A1 (en) | METHOD FOR PROCESSING BIOMASS | |
| WO2020213132A1 (en) | Method for producing plasmalogen-containing functional material | |
| US20220064232A1 (en) | Methods of separating phosvitin and hdl from an egg yolk product and resulting compositions | |
| JPH0726287A (en) | Production of yolk lipid | |
| JPH06116297A (en) | Separation of water-soluble protein in egg york | |
| JPH01315337A (en) | Lipid adsorbent | |
| JPH03145500A (en) | Fractionation of egg york water soluble protein | |
| JPH05339168A (en) | Pancreatic lipase inhibitor and cholesterol esterase inhibitor | |
| KR20060013246A (en) | Method of seqeuntial separation and purification of value-added components from chicken egg yolk | |
| JPH07108206B2 (en) | Egg yolk oil manufacturing method | |
| WO1992004974A1 (en) | A lipid absorbent | |
| JPH08205810A (en) | Production of extract | |
| JPH06228197A (en) | Method for fractionating gamma-livetin from egg yolk | |
| JPH08322472A (en) | Concentration of acidic phospholipid |