JPS6246140B2 - - Google Patents
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- Publication number
- JPS6246140B2 JPS6246140B2 JP173579A JP173579A JPS6246140B2 JP S6246140 B2 JPS6246140 B2 JP S6246140B2 JP 173579 A JP173579 A JP 173579A JP 173579 A JP173579 A JP 173579A JP S6246140 B2 JPS6246140 B2 JP S6246140B2
- Authority
- JP
- Japan
- Prior art keywords
- protein
- soluble
- solution
- acid
- proteins
- 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.)
- Expired
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- 235000018102 proteins Nutrition 0.000 claims description 32
- 102000004169 proteins and genes Human genes 0.000 claims description 32
- 108090000623 proteins and genes Proteins 0.000 claims description 32
- 108010073771 Soybean Proteins Proteins 0.000 claims description 12
- 239000000796 flavoring agent Substances 0.000 claims description 11
- 235000019634 flavors Nutrition 0.000 claims description 11
- 238000000034 method Methods 0.000 claims description 8
- 239000000203 mixture Substances 0.000 claims description 8
- 239000002253 acid Substances 0.000 claims description 7
- 229920001184 polypeptide Polymers 0.000 claims description 5
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 5
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 5
- 235000019710 soybean protein Nutrition 0.000 claims description 5
- 108091005804 Peptidases Proteins 0.000 claims description 4
- 102000035195 Peptidases Human genes 0.000 claims description 4
- 235000013305 food Nutrition 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 claims description 3
- 108091005573 modified proteins Proteins 0.000 claims description 2
- 102000035118 modified proteins Human genes 0.000 claims description 2
- 235000013361 beverage Nutrition 0.000 description 13
- 239000000243 solution Substances 0.000 description 13
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 102000004190 Enzymes Human genes 0.000 description 8
- 108090000790 Enzymes Proteins 0.000 description 8
- 230000002378 acidificating effect Effects 0.000 description 8
- 229940088598 enzyme Drugs 0.000 description 8
- 235000019640 taste Nutrition 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 7
- 239000003795 chemical substances by application Substances 0.000 description 7
- 229940001941 soy protein Drugs 0.000 description 7
- 235000015205 orange juice Nutrition 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 235000010469 Glycine max Nutrition 0.000 description 5
- 239000012141 concentrate Substances 0.000 description 5
- 230000007071 enzymatic hydrolysis Effects 0.000 description 5
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 5
- 230000007935 neutral effect Effects 0.000 description 5
- 239000002002 slurry Substances 0.000 description 5
- FALRKNHUBBKYCC-UHFFFAOYSA-N 2-(chloromethyl)pyridine-3-carbonitrile Chemical compound ClCC1=NC=CC=C1C#N FALRKNHUBBKYCC-UHFFFAOYSA-N 0.000 description 4
- 235000007688 Lycopersicon esculentum Nutrition 0.000 description 4
- 239000003929 acidic solution Substances 0.000 description 4
- 235000011121 sodium hydroxide Nutrition 0.000 description 4
- 229940014800 succinic anhydride Drugs 0.000 description 4
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 3
- 244000068988 Glycine max Species 0.000 description 3
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 3
- 230000010933 acylation Effects 0.000 description 3
- 238000005917 acylation reaction Methods 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 238000004448 titration Methods 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 241000227653 Lycopersicon Species 0.000 description 2
- 240000003768 Solanum lycopersicum Species 0.000 description 2
- 150000008064 anhydrides Chemical class 0.000 description 2
- 229960004543 anhydrous citric acid Drugs 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 235000019658 bitter taste Nutrition 0.000 description 2
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 2
- 238000000354 decomposition reaction Methods 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- -1 fuicin Proteins 0.000 description 2
- 235000021578 orange juice drink Nutrition 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 239000003531 protein hydrolysate Substances 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- RFWFOJDAIRDAPK-VKHMYHEASA-N (3s)-3-aminooxane-2,6-dione Chemical compound N[C@H]1CCC(=O)OC1=O RFWFOJDAIRDAPK-VKHMYHEASA-N 0.000 description 1
- ODIGIKRIUKFKHP-UHFFFAOYSA-N (n-propan-2-yloxycarbonylanilino) acetate Chemical group CC(C)OC(=O)N(OC(C)=O)C1=CC=CC=C1 ODIGIKRIUKFKHP-UHFFFAOYSA-N 0.000 description 1
- 102000004400 Aminopeptidases Human genes 0.000 description 1
- 108090000915 Aminopeptidases Proteins 0.000 description 1
- 235000017060 Arachis glabrata Nutrition 0.000 description 1
- 244000105624 Arachis hypogaea Species 0.000 description 1
- 235000010777 Arachis hypogaea Nutrition 0.000 description 1
- 235000018262 Arachis monticola Nutrition 0.000 description 1
- 108090000145 Bacillolysin Proteins 0.000 description 1
- 108091005658 Basic proteases Proteins 0.000 description 1
- 240000002791 Brassica napus Species 0.000 description 1
- 235000004977 Brassica sinapistrum Nutrition 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 102000000496 Carboxypeptidases A Human genes 0.000 description 1
- 108010080937 Carboxypeptidases A Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 240000002319 Citrus sinensis Species 0.000 description 1
- 235000005976 Citrus sinensis Nutrition 0.000 description 1
- 229920000742 Cotton Polymers 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 102000018389 Exopeptidases Human genes 0.000 description 1
- 108010091443 Exopeptidases Proteins 0.000 description 1
- 241000219146 Gossypium Species 0.000 description 1
- OFOBLEOULBTSOW-UHFFFAOYSA-N Malonic acid Chemical compound OC(=O)CC(O)=O OFOBLEOULBTSOW-UHFFFAOYSA-N 0.000 description 1
- 108091005507 Neutral proteases Proteins 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010009736 Protein Hydrolysates Proteins 0.000 description 1
- 244000000231 Sesamum indicum Species 0.000 description 1
- 235000003434 Sesamum indicum Nutrition 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
- 239000006286 aqueous extract Substances 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 235000014171 carbonated beverage Nutrition 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 150000001244 carboxylic acid anhydrides Chemical class 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 235000014156 coffee whiteners Nutrition 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 229940066758 endopeptidases Drugs 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 235000013312 flour Nutrition 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- XMGQYMWWDOXHJM-UHFFFAOYSA-N limonene Chemical compound CC(=C)C1CCC(C)=CC1 XMGQYMWWDOXHJM-UHFFFAOYSA-N 0.000 description 1
- FPYJFEHAWHCUMM-UHFFFAOYSA-N maleic anhydride Chemical compound O=C1OC(=O)C=C1 FPYJFEHAWHCUMM-UHFFFAOYSA-N 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 235000021565 orange beverage Nutrition 0.000 description 1
- 239000007968 orange flavor Substances 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 235000020232 peanut Nutrition 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 235000011118 potassium hydroxide Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- WYVAMUWZEOHJOQ-UHFFFAOYSA-N propionic anhydride Chemical compound CCC(=O)OC(=O)CC WYVAMUWZEOHJOQ-UHFFFAOYSA-N 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000001223 reverse osmosis Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
Description
【発明の詳細な説明】
2〜6の範囲のPHを有する酸性食品のたん白強
化は、満足できる栄養的および味の特性を示すた
ん白を利用できない点で厄介である。油糧たん
白、特に大豆たん白は酸可溶性に変換された場
合、青くさくそして苦いなど色々記載される好ま
しくない味の特性を有することを特徴とする。い
やなフレーバーは、2〜8%もしくはそれより多
いたん白濃度で強いフレーバーを十分マスクでき
る程の他の成分を含まない酸性飲料で特に顕著で
ある。DETAILED DESCRIPTION OF THE INVENTION Protein fortification of acidic foods with a PH in the range of 2 to 6 is complicated in that proteins exhibiting satisfactory nutritional and taste properties are not available. Oilseed proteins, particularly soybean proteins, when converted to acid-soluble form, are characterized by undesirable taste characteristics variously described as green and bitter. Offensive flavors are particularly noticeable in acidic beverages where protein concentrations of 2-8% or more do not contain enough other ingredients to mask strong flavors.
たん白分解酵素の作用による種実たん白の加水
分解は、周知の処理であり、酸性条件下で可溶性
もしくは部分的に可溶性を保持することができる
水溶性生成物を生ずる。酸素分解の既知方法は特
許第3814816号、特許第3830942号、特許第
3843802号および特許第3846560号各号明細書に記
載される。 Hydrolysis of seed proteins by the action of proteolytic enzymes is a well-known process that yields water-soluble products that can remain soluble or partially soluble under acidic conditions. Known methods of oxygen decomposition are disclosed in Patent No. 3814816, Patent No. 3830942, and Patent No.
3843802 and Patent No. 3846560.
常法によれば、たん白は水スラリーで種実から
分離する。たん白分解酵素を添加し、スラリーの
PHを調整して、使用する特定酵素に対し反応条件
を最適にする。スラリーは酵素の添加前および酵
素の分解中加熱することができる。 According to conventional methods, the protein is separated from the seeds in a water slurry. Add proteolytic enzyme to the slurry.
Adjust the pH to optimize reaction conditions for the specific enzyme used. The slurry can be heated before addition of the enzyme and during enzyme decomposition.
酵素加水分解により生成したポリペプチド混合
物は酸性もしくは中性PHで水溶性であるが、初め
の分離たん白よりも強いフレーバーを有する。従
つて強いもしくは若いフレーバーを減少させ、し
かも酸溶解性を保持することが好ましい。 The polypeptide mixture produced by enzymatic hydrolysis is water soluble at acidic or neutral pH, but has a stronger flavor than the initial protein isolate. Therefore, it is desirable to reduce strong or young flavors while retaining acid solubility.
本発明は油糧たん白の酵素加水分解により得た
加水分解物の味特性を改良させる。加水分解物は
アシル化剤、好ましくは無水琥珀酸のようなジカ
ルボン酸無水物との反応により化学的に修正され
る。この方法により、ポリペプチドの遊離アミノ
基はアシル化され、特に酸性溶液で実質的に味を
改良する。 The present invention improves the taste characteristics of hydrolysates obtained by enzymatic hydrolysis of oilseed proteins. The hydrolyzate is chemically modified by reaction with an acylating agent, preferably a dicarboxylic acid anhydride such as succinic anhydride. By this method, free amino groups of the polypeptide are acylated, which substantially improves taste, especially in acidic solutions.
たん白自体のアシル化は周知の処理である。た
とえば特許第3764711号明細書では特許権者は未
加水分解大豆たん白をアシル化することによりコ
ーヒー用ホワイトナーを得ている。しかし予じめ
加水分解したたん白をアシル化すると好ましくな
い味特性を有する生成物を生ずることを同一特許
権者は示している。又アシル化加水分解たん白は
酸性溶液に不溶性である旨記載されている。 Acylation of proteins themselves is a well-known process. For example, in Patent No. 3764711, the patentee obtains a coffee whitener by acylating unhydrolyzed soy protein. However, the same patentee has shown that acylation of pre-hydrolyzed proteins results in products with undesirable taste characteristics. It is also stated that acylated hydrolyzed proteins are insoluble in acidic solutions.
予期しないことに酵素加水分解物のアシル化は
味特性に実質的改良を生じ、一方では生成物は酸
性溶液で可溶性を保有することが分つた。 It was unexpectedly found that acylation of enzymatic hydrolysates resulted in substantial improvements in taste properties, while the products remained soluble in acidic solutions.
本発明は酵素加水分解の酸可溶性大豆たん白に
適用できる。当然、落花生、棉実、とうもろこ
し、菜種およびごまの同様に分離したたん白に全
く同様に適用することが予期されるであろう。本
発明方法は動物たん白には適用できないことがわ
かつた。 The present invention is applicable to enzymatic hydrolysis of acid-soluble soybean protein. Naturally, one would expect application in exactly the same way to similarly isolated proteins of peanut, cotton, corn, rapeseed and sesame. It has been found that the method of the invention cannot be applied to animal proteins.
大豆のような種実は初めにたん白を分離するた
めに処理する。たとえば大豆粉は約7.5〜約9.5の
PHを有する弱アルカリで抽出することができる。
水性抽出物は固形フラクシヨンから分離し、次に
PHは約4.5に調整してたん白を沈澱する。沈澱た
ん白は洗滌することができ、ついで酵素加水分解
に供することができる。 Seed seeds, such as soybeans, are first processed to separate the protein. For example, soybean flour has a rating of about 7.5 to about 9.5.
It can be extracted with a weak alkali having a PH.
The aqueous extract is separated from the solid fraction and then
Adjust the pH to approximately 4.5 to precipitate the protein. Precipitated proteins can be washed and then subjected to enzymatic hydrolysis.
大豆たん白の水性スラリーは最終生成物の完壁
なフレーバーを劣下させることのない時間約93゜
〜約129.5℃(約200〓〜約265〓)の温度で加熱
することができる。1〜約25秒の加熱時間は温度
によるが一般に十分である。 The aqueous slurry of soy protein can be heated at temperatures of about 93° to about 129.5°C (about 200° to about 265°) for a period of time without degrading the full flavor of the final product. Heating times of 1 to about 25 seconds, depending on the temperature, are generally sufficient.
次に部分的変性たん白はたん白分解酵素、好ま
しくは微酸性もしくは塩基性条件下で処理され
る。適当な酵素は植物もしくは動物の中性および
アルカリ性プロテアーゼ酵素、ペプシン、フイシ
ン、パパイン、レイニン、トリプシンおよびキモ
トリプシンのようなエンドペプチダーゼと共にア
ミノペプチダーゼおよびカルボキシペプチダーゼ
AおよびBのような微生物エキソペプチダーゼを
含む。 The partially denatured protein is then treated with a proteolytic enzyme, preferably under slightly acidic or basic conditions. Suitable enzymes include plant or animal neutral and alkaline protease enzymes, endopeptidases such as pepsin, fuicin, papain, reinin, trypsin and chymotrypsin, as well as microbial exopeptidases such as aminopeptidases and carboxypeptidases A and B.
スラリーのPHおよび濃度は選択された酵素の周
知の原理による最高活性を確保するために調整す
ることができる。好ましくはたん白濃度は20%を
超えるべきではない。酵素の使用量および分解時
間は使用酵素のタイプ、温度、PHで変化し得る
が、そのような要素は当業者に決定できる。一般
に温度は室温以上のレベルに上がるが、酵素を失
活させもしくは変性させる値、一般に約71℃(約
160〓)以下に保持される。 The PH and concentration of the slurry can be adjusted to ensure maximum activity of the selected enzyme according to well-known principles. Preferably the protein concentration should not exceed 20%. The amount of enzyme used and the degradation time may vary depending on the type of enzyme used, temperature, PH, and such factors can be determined by one skilled in the art. The temperature is generally raised to a level above room temperature, but at a level that deactivates or denatures the enzyme, generally around 71°C (approx.
160〓) or less.
酵素加水分解はたん白の主要割合、好ましくは
60〜85%が加水分解されるまで継続され、そこで
終結される。生成ポリペプチド混合物は広範囲の
PH値を有する溶液に溶解するであろう。しかし本
発明の目的に対しては混合物は2〜6のPHを有す
る溶液に溶解するであろう。任意の不溶性フラク
シヨン除去後に溶液は乾燥することができる。 Enzymatic hydrolysis is a major proportion of protein, preferably
Continue until 60-85% is hydrolyzed and then terminate. The resulting polypeptide mixture has a wide range of
It will dissolve in a solution with a PH value. However, for purposes of the present invention, the mixture will dissolve in a solution having a pH of 2 to 6. After removing any insoluble fractions, the solution can be dried.
次に分離たん白は溶液にし、通例の方法でアシ
ル化される。アシル化剤は、この剤と反応するた
めの位置を供する置換性水素原子を有する酸素、
硫黄もしくは窒素のようなたん白加水分解物の官
能基をアシル化できる化合物である。適当な剤は
無水酢酸および無水プロピオン酸を含むモノカル
ボン酸無水物、又無水琥珀酸、無水グルタミン酸
および無水マレイン酸のようなジカルボン酸無水
物同様にこれらの混合物のような内部もしくは外
部のいずれかのカルボン酸無水物を含む。無水琥
珀酸は好ましく、約7.0〜約7.2の中性PHに維持さ
れた加水分解物溶液に固体として添加される。溶
液は反応中約1〜約15℃の温度に冷却するのが好
ましい。 The isolated protein is then brought into solution and acylated in the customary manner. The acylating agent is oxygen with a substitutable hydrogen atom that provides a site for reacting with the agent;
It is a compound that can acylate functional groups in protein hydrolysates, such as sulfur or nitrogen. Suitable agents are either internal or external, such as monocarboxylic anhydrides, including acetic anhydride and propionic anhydride, and dicarboxylic anhydrides, such as succinic anhydride, glutamic anhydride, and maleic anhydride, as well as mixtures thereof. Contains carboxylic acid anhydride. Succinic anhydride is preferably added as a solid to the hydrolyzate solution maintained at a neutral pH of about 7.0 to about 7.2. Preferably, the solution is cooled to a temperature of about 1 to about 15°C during the reaction.
詳細には、反応溶液はたん白加水分解物の約3
〜約15%を含む。十分なアシル化剤は添加され、
加水分解物の重量規準で通例約7〜約18%の利用
できる官能基と実質的に完全に反応する。0.08モ
ル食塩溶液の添加は、そうでなければ中性PHで溶
解せず溶解させるために溶液のイオン強度を増加
させる必要があるポリペプチドを含む溶液に必要
であることができる。アシル化剤はこのように製
造された溶液に添加され、PHは中性もしくは僅か
に上に苛性カリ、苛性ソーダもしくはその他のよ
うな適当な塩基の添加により調整される。PHはア
シル化剤が完全に溶解し、反応が完了するまで連
続滴定によつて7.0〜7.2に維持することが好まし
い。反応によつて生成した無機塩は透析、電気泳
動、逆浸透もしくは他の適当な脱塩技術により除
去することができる。次に溶液は乾燥して固形の
カルボキシアシル化加水分解物を得ることができ
る。 Specifically, the reaction solution contains approximately 30% of the protein hydrolyzate.
Contains ~15%. Sufficient acylating agent is added and
Typically from about 7 to about 18% of the available functional groups, based on the weight of the hydrolyzate, are reacted substantially completely. Addition of a 0.08 Molar saline solution may be necessary for solutions containing polypeptides that would otherwise not dissolve at neutral PH and require increasing the ionic strength of the solution in order to dissolve. The acylating agent is added to the solution thus prepared and the pH adjusted to neutral or slightly above by addition of a suitable base such as caustic potash, caustic soda or the like. The pH is preferably maintained at 7.0 to 7.2 by continuous titration until the acylating agent is completely dissolved and the reaction is complete. Inorganic salts formed by the reaction can be removed by dialysis, electrophoresis, reverse osmosis or other suitable desalting techniques. The solution can then be dried to obtain a solid carboxyacylated hydrolyzate.
こうして得た生成物はきわめて温和なもしくは
口当りのやわらかい臭いおよびフレーバーを有し
約2.0〜6.0のPHを有する酸性溶液に溶解した時に
いやなフレーバーを現さない。このように生成物
は天然もしくは人工酸性果実飲料を含む酸性飲料
に添加するのに特に適する。適当な飲料はたとえ
ば甘橘およびトマト飲料を含む。生成物は炭酸飲
料への添加も適する。 The product thus obtained has a very mild odor and flavor and exhibits no unpleasant flavor when dissolved in acidic solutions having a pH of about 2.0 to 6.0. The product is thus particularly suitable for addition to acidic beverages, including natural or artificially acidic fruit beverages. Suitable beverages include, for example, sweet orange and tomato beverages. The product is also suitable for addition to carbonated drinks.
例
口当りの軟かい酸可溶性たん白の製造におい
て、134gの酵素水解大豆たん白(タイプ1205、
Gunther、Division of Staley)を水溶中の1
の蒸溜水に溶解した。溶液のPHは4.46で、温度は
2.8℃(37〓)であつた。12.5mlNaOH(5N)を
溶液に添加しPHを7.05にした。無水琥珀酸(11.7
g)を反応混合物にゆつくりふりまき、一方
NaOH(5N)により連続滴定して、7.0〜7.2のPH
を維持した。約48mlの苛性ソーダをこの滴定に使
用した。Example: In the production of a soft-tasting acid-soluble protein, 134 g of enzyme-hydrolyzed soy protein (type 1205,
Gunther, Division of Staley) in water.
of distilled water. The pH of the solution is 4.46 and the temperature is
The temperature was 2.8℃ (37〓). 12.5ml NaOH (5N) was added to the solution to bring the pH to 7.05. Succinic anhydride (11.7
Sprinkle g) slowly over the reaction mixture, while
PH of 7.0-7.2 by continuous titration with NaOH (5N)
was maintained. Approximately 48 ml of caustic soda was used for this titration.
PHを一定に保つ場合、反応の完了が示されるな
らば反応混合物は中空繊維透析器を使用し、水を
20分毎に換えながら1ガロン容の蒸溜水を5回に
透析した。次に反応混合物は凍結乾燥した。 If the pH is kept constant, the reaction mixture is diluted with water using a hollow fiber dialyzer once the reaction is indicated to be complete.
One gallon of distilled water was dialyzed five times, changing every 20 minutes. The reaction mixture was then lyophilized.
例
Guntherタイプ1205、Guntherタイプ1043およ
びCentral SoyaタイプFS704の3つの異なるタイ
プの酵素水解大豆たん白を、例に従つて琥珀酸
化した。オレンジ飲料を製造し、3個の部分に分
割した。同量の琥珀酸化部分を等量のオレンジ飲
料に添加し味覚テストした。琥珀酸化しない同量
のたん白を含む同じ試料を比較のために製造し
た。すべての場合に大豆フレーバーおよび苦味の
減少を含む琥珀酸化たん白による味の改良を観察
した。EXAMPLE Three different types of enzymatically hydrolyzed soy protein, Gunther type 1205, Gunther type 1043 and Central Soya type FS704, were amber-oxidized according to the example. An orange drink was prepared and divided into three portions. Equal amounts of amber oxidized moieties were added to equal amounts of orange beverages and taste tested. The same sample containing the same amount of protein without amber oxidation was prepared for comparison. Taste improvements with amber-oxidized protein were observed in all cases, including a reduction in soy flavor and bitterness.
例
3.7%たん白強化の天然オレンジ ジユース飲
料を100mlの再構成凍結オレンジ ジユース濃縮
物に琥珀酸化酸可溶性大豆たん白(分析により80
%たん白)4.66gを添加して製造した。Example Reconstitute 100 ml of natural orange juice beverage fortified with 3.7% frozen orange juice concentrate with amber oxidized acid soluble soy protein (by analysis
% protein) was added to produce 4.66 g.
例
たん白強化、天然オレンジ ジユース濃縮物を
6オンスのオレンジ ジユース濃縮物に琥珀酸化
酸可溶性大豆たん白33.12gを添加して製造し
た。18オンスの水で再構成した場合、この濃縮物
は37%たん白強化の天然オレンジ ジユースを得
る。EXAMPLE A protein enriched, natural orange juice concentrate was prepared by adding 33.12 grams of amber oxidized acid soluble soy protein to 6 ounces of orange juice concentrate. When reconstituted with 18 ounces of water, this concentrate yields 37% protein-enriched natural orange juice.
例
4.0%たん白強化人工オレンジ ジユース飲料
を100mlの冷水に次の処方物を溶解して製造し
た:
蔗糖 11.5g
クエン酸、無水 1.0g
セルロース ガム 0.1g
オレンジ フレーバー 適量
オレンジ色素 適量
琥珀酸化酸可溶性大豆たん白 5.0g
例
3.8%たん白強化の50%天然、50%人工オレン
ジ ジユース飲料を例および記載の等量の飲
料と混合して製造した。Example A 4.0% protein fortified artificial orange juice drink was prepared by dissolving the following formulation in 100ml of cold water: Sucrose 11.5g Citric acid, anhydrous 1.0g Cellulose gum 0.1g Orange flavor as needed Orange color as needed Amber oxidized acid soluble soybean Protein 5.0g Example A 50% natural, 50% artificial orange youth beverage fortified with 3.8% protein was prepared by mixing with an equal amount of the beverage as described in Example and above.
例
4.0%たん白強化の炭酸天然オレンジ ジユー
ス飲料を200mlの再構成凍結オレンジ ジユース
濃縮物に琥珀酸化酸可溶性大豆たん白10.0gを添
加し、次いで飲料を加圧二酸化炭素シリンダーで
炭酸ガスを飽和させて製造した。Example: 4.0% protein fortified carbonated natural orange juice drink reconstituted to 200 ml of frozen orange juice concentrate, 10.0 g of amber oxidized acid soluble soy protein was added and the beverage was then carbonated in a pressurized carbon dioxide cylinder. Manufactured by
例
4.0%たん白強化の人工トマト ジユース飲料
を8オンスの冷水に次の処方物を分散させて製造
した:
トマト粉末 30.0g
食塩 1.2g
クエン酸、無水 1.0g
トマト フレーバー 適量
琥珀酸化酸可溶性大豆たん白 12.0g
例乃至記載の飲料は本発明の修正たん白を
含むことができる代表的酸飲料である。すべての
これら飲料は美味で過度の苦味およびいやな大豆
フレーバーを含まない。Example A 4.0% protein-enriched artificial tomato youth beverage was prepared by dispersing the following formulation in 8 ounces of cold water: Tomato powder 30.0 g Salt 1.2 g Citric acid, anhydrous 1.0 g Tomato flavor as needed Amber oxidized acid soluble soybean protein White 12.0g The beverages described in the examples and descriptions are representative acidic beverages that can contain the modified protein of the present invention. All these beverages are delicious and free from excessive bitterness and unpleasant soy flavors.
Claims (1)
製造において、初めに油糧種実から得たたん白を
たん白分解酵素により加水分解して酸可溶性ポリ
ペプチド混合物を形成させ、次にこの混合物をア
シル化してアシル化加水分解物を形成させること
を特徴とする、上記たん白食品の製造法。 2 たん白は大豆たん白である、特許請求の範囲
第1項記載の方法。 3 アシル化加水分解物は約2〜約6のPHを有す
る酸溶液に可溶性である、特許請求の範囲第1項
記載の方法。[Claims] 1. In the production of a modified protein food having a mild flavor, the protein obtained from oilseed seeds is first hydrolyzed with a proteolytic enzyme to form an acid-soluble polypeptide mixture; A method for producing the protein food described above, characterized in that the mixture is acylated to form an acylated hydrolyzate. 2. The method according to claim 1, wherein the protein is soybean protein. 3. The method of claim 1, wherein the acylated hydrolyzate is soluble in an acid solution having a pH of about 2 to about 6.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP173579A JPS5596060A (en) | 1979-01-10 | 1979-01-10 | Acid soluble acylated protein and production |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP173579A JPS5596060A (en) | 1979-01-10 | 1979-01-10 | Acid soluble acylated protein and production |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS5596060A JPS5596060A (en) | 1980-07-21 |
JPS6246140B2 true JPS6246140B2 (en) | 1987-09-30 |
Family
ID=11509814
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP173579A Granted JPS5596060A (en) | 1979-01-10 | 1979-01-10 | Acid soluble acylated protein and production |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPS5596060A (en) |
Families Citing this family (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CA3118136A1 (en) * | 2018-11-02 | 2020-05-07 | Cargill, Incorporated | Corn protein hydrolysates and methods of making |
-
1979
- 1979-01-10 JP JP173579A patent/JPS5596060A/en active Granted
Also Published As
Publication number | Publication date |
---|---|
JPS5596060A (en) | 1980-07-21 |
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