JPH04210577A - Cholesterol level rise-inhibitory food and production thereof - Google Patents
Cholesterol level rise-inhibitory food and production thereofInfo
- Publication number
- JPH04210577A JPH04210577A JP2412823A JP41282390A JPH04210577A JP H04210577 A JPH04210577 A JP H04210577A JP 2412823 A JP2412823 A JP 2412823A JP 41282390 A JP41282390 A JP 41282390A JP H04210577 A JPH04210577 A JP H04210577A
- Authority
- JP
- Japan
- Prior art keywords
- protein
- food
- silk fibroin
- derived
- fibroin
- 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
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 title claims abstract description 39
- 235000013305 food Nutrition 0.000 title claims abstract description 33
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 7
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 46
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 46
- 108010022355 Fibroins Proteins 0.000 claims abstract description 41
- 150000001413 amino acids Chemical class 0.000 claims abstract description 19
- 230000036961 partial effect Effects 0.000 claims abstract description 6
- 235000012000 cholesterol Nutrition 0.000 claims description 16
- 230000003301 hydrolyzing effect Effects 0.000 claims description 2
- 230000002401 inhibitory effect Effects 0.000 claims description 2
- 230000000694 effects Effects 0.000 abstract description 9
- 230000007062 hydrolysis Effects 0.000 abstract description 6
- 238000006460 hydrolysis reaction Methods 0.000 abstract description 6
- 239000004480 active ingredient Substances 0.000 abstract 2
- 235000018102 proteins Nutrition 0.000 description 35
- 235000001014 amino acid Nutrition 0.000 description 17
- 239000000203 mixture Substances 0.000 description 12
- 239000000835 fiber Substances 0.000 description 10
- 239000000243 solution Substances 0.000 description 9
- 238000000034 method Methods 0.000 description 7
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
- 239000000843 powder Substances 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 108010013296 Sericins Proteins 0.000 description 4
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000012460 protein solution Substances 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- 108090000526 Papain Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
- 229910001628 calcium chloride Inorganic materials 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 102000038379 digestive enzymes Human genes 0.000 description 2
- 108091007734 digestive enzymes Proteins 0.000 description 2
- 229940055729 papain Drugs 0.000 description 2
- 235000019834 papain Nutrition 0.000 description 2
- 230000001766 physiological effect Effects 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 235000019640 taste Nutrition 0.000 description 2
- 241000255789 Bombyx mori Species 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 239000004278 EU approved seasoning Substances 0.000 description 1
- 206010019133 Hangover Diseases 0.000 description 1
- 238000007696 Kjeldahl method Methods 0.000 description 1
- 208000008589 Obesity Diseases 0.000 description 1
- 102000016387 Pancreatic elastase Human genes 0.000 description 1
- 108010067372 Pancreatic elastase Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 238000003723 Smelting Methods 0.000 description 1
- 229910000831 Steel Inorganic materials 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 235000013361 beverage Nutrition 0.000 description 1
- 235000019658 bitter taste Nutrition 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- 235000008429 bread Nutrition 0.000 description 1
- 238000009395 breeding Methods 0.000 description 1
- 230000001488 breeding effect Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000003086 colorant Substances 0.000 description 1
- 150000001879 copper Chemical class 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 235000011850 desserts Nutrition 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 235000019621 digestibility Nutrition 0.000 description 1
- 238000000909 electrodialysis Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 235000011194 food seasoning agent Nutrition 0.000 description 1
- 239000003205 fragrance Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 235000015110 jellies Nutrition 0.000 description 1
- 239000008274 jelly Substances 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 235000010755 mineral Nutrition 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 235000012149 noodles Nutrition 0.000 description 1
- 235000020824 obesity Nutrition 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 235000013324 preserved food Nutrition 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- -1 samoase Proteins 0.000 description 1
- 235000012046 side dish Nutrition 0.000 description 1
- 235000011121 sodium hydroxide Nutrition 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 239000010959 steel Substances 0.000 description 1
- 235000019605 sweet taste sensations Nutrition 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 210000004885 white matter Anatomy 0.000 description 1
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Abstract
Description
[00011 [00011
【産業上の利用分野]本発明は、コレステロール上昇抑
制食品に関する。さらに詳しくは、本発明は綱フィブ[
■イン由来の水溶性蛋白質を含有することを特徴とする
食品およびその製造方法に関する。
[0002]
【従来の技術】絹はフィブロインおよびセリシンを主成
分とする蛋白質で構成され、大行から、繊維としては利
用されていたが、綱玉白質自体は通常の蛋白質とは異な
り、ペプシン、lへリプシン等の消化酵素の影響を受け
にくいため、食品に利用される試みはなされていなかっ
た。そこで、本発明者は、綱フィブロインを中心とする
綱玉白質を食品に利用する技術として、プリン、ゼリー
等のゲル化食品に利用する技術(特開平1256352
号公報)、あるいは二日酔い防止食品に利用する技術(
特開平1−256352号公報)を開示している。また
前述のごとくフィブロインは消化酵素の影響を受けにく
いため、加水分解によって消化・吸収性を向上させ、さ
らに特異なアミノ酸組成を利用してアルコール代謝促進
作用を発現させる技術についても開示している(特開平
2−177864号公報)。
[0003]Lかしながら、綱フィブロインをどの程度
含有せしめた食品に、生体内においてどのような作用が
あるかどうかは、はとんど不明である。とりわけ、最近
では、種々の蛋白質が、そのアミノ酸組成だけでは説明
できない生理作用を摂取された生体内において発現する
ことが知られるようになってきており、綱フィブロイン
を食品として利用した場合にも、そのアミノ酸組成によ
って類推される機能以外の作用が期待されるものである
。
[0004][Industrial Field of Application] The present invention relates to a food that suppresses cholesterol rise. More specifically, the present invention relates to strepta fib [
■It relates to a food product characterized by containing water-soluble protein derived from inn and a method for producing the same. [0002] [Prior Art] Silk is composed of proteins whose main components are fibroin and sericin, and has been used as a fiber since Daigyo. However, the fibroin itself is different from normal proteins, and contains pepsin, sericin, etc. Since it is not easily affected by digestive enzymes such as helipsin, no attempt has been made to use it in foods. Therefore, the present inventor developed a technology to utilize leukemia white matter, mainly fibroin, in foods, as described in Japanese Unexamined Patent Application Publication No. 1256352.
Publication No. 2), or technology used in hangover prevention foods (
JP-A-1-256352). Furthermore, as mentioned above, fibroin is not easily affected by digestive enzymes, so it improves its digestibility and absorption through hydrolysis, and also discloses a technology that utilizes a unique amino acid composition to express an alcohol metabolism promoting effect ( JP-A-2-177864). [0003]However, it is still unclear what kind of action foods containing fibroin have in vivo. In particular, it has recently become known that various proteins express physiological effects in the ingested body that cannot be explained by their amino acid composition alone. It is expected that it will have effects other than those inferred from its amino acid composition. [0004]
【発明が解決しようとする課題】本発明者等は、綱フィ
ブロインを含有する食品について、その生理作用を鋭意
検討した結果、絹フィブロイン由来の蛋白質が、驚くべ
きことに顕著なコレステロール上昇抑制作用を発現する
ことを知見し、本発明を完成させたものである。
[0005][Problems to be Solved by the Invention] As a result of intensive studies on the physiological effects of foods containing silk fibroin, the present inventors found that protein derived from silk fibroin surprisingly has a remarkable effect on suppressing cholesterol rise. The present invention has been completed based on the finding that this phenomenon occurs. [0005]
【課題を解決するための手段】すなわち1本発明によれ
ば、綱フィブロイン由来の蛋白質を含有することを特徴
とするコレステロール上昇抑制食品が提供される。
[0006]前記網フィブロイン由来の蛋白質は、当該
食品中の全蛋白質の]80重量%以」二を占めるよう調
整されてなることが好ましい。
[0007]前記蛋白質は、絹フィブロイン由来蛋白質
の部分加水分解物であることが好ましい。
[0008]前記部分加水分解物の平均分子量は、15
0〜so、oooであることが好ましい。
[0009]また、本発明は、絹フィブロイン由来の蛋
白質を、遊離アミノ酸の生成懺が1〜70%となるまで
部分加水分解し、得られた部分加水分解蛋白質を添加す
ることを特徴とするコレステロール上昇抑制食品の製造
方法を示すものである。
[00101以下、本発明の詳細な説明する。
[0011]絹糸は、蚕の絹糸腺から分泌される繊維状
蛋白質であって、フィブロイン繊維がセリシンで固めら
れたものである。綱フィブロインは、鞘糸から製錬によ
りセリシンを除去することにより得ることができる。絹
フィブロインはグリシン(Gly)とアラニン(A 1
a)を非常に多く含む蛋白質で、 (G1 y3A1
a2X2)n(Xはグリシン、アラニン以外のアミノ
酸)で表される組成だといわれている。その組成の一例
を表1に示す。
[00121[Means for Solving the Problems] According to one aspect of the present invention, there is provided a food product for inhibiting cholesterol elevation, which is characterized by containing a protein derived from the class fibroin. [0006] The otofibroin-derived protein is preferably adjusted to account for 80% by weight or more of the total protein in the food. [0007] The protein is preferably a partial hydrolyzate of silk fibroin-derived protein. [0008] The average molecular weight of the partial hydrolyzate is 15
It is preferable that it is 0-so, ooo. [0009] The present invention also provides a method of producing cholesterol, which is characterized by partially hydrolyzing a protein derived from silk fibroin until the production of free amino acids is 1 to 70%, and adding the obtained partially hydrolyzed protein. This shows a method for producing a food product that suppresses the rise in temperature. [00101 Hereinafter, the present invention will be described in detail. [0011] Silk is a fibrous protein secreted from the silk glands of silkworms, and is composed of fibroin fibers hardened with sericin. Fibroin can be obtained by removing sericin from sheath threads by smelting. Silk fibroin contains glycine (Gly) and alanine (A1
A protein that contains a very large amount of (G1 y3A1
It is said to have a composition represented by a2X2)n (X is an amino acid other than glycine or alanine). An example of the composition is shown in Table 1. [00121
【表1]
[0013]次に、フィブロイン繊維から蛋白質を得る
工程を説明する。
[00143まゆ玉、絹糸等からフィブロイン繊維を得
るには、公知の方法を用いればよく、例えば溶解、沈殿
、抽出、精製、培養等の処理を行うことにより得られる
。本発明においては、このフィブロイン繊維そのものを
蛋白質として用いることも可能であるが、好ましくは、
以下の方法に従って部分加水分解を行う。
[0015]すなわち、得られたフィブロイン繊維を塩
酸、硫酸、リン酸等から選ばれた鉱酸の濃厚液に加熱溶
解し、部分加水分解した後、中和、脱塩して絹フィブロ
イン由来の水溶性蛋白質を含有する溶液を得ることがで
きる。゛また、フィブロイン繊維を、例えば、塩化カル
シウム45%溶液、あるいは塩化カルシウムとエタノー
ルと水の重量比が1:2:8である溶液に溶解させ、こ
の溶解液を脱塩することで絹フィブロイン由来の水溶性
蛋白質を含有する溶液を得ることもできる。この溶液を
、例えば、パパイン、サモアーゼ、エラスターゼ、バン
クレアチン等から選はねた蛋白質分解酵素でさらに加水
分解すれば、水に可逆的に溶解する部分加水分解された
水溶性蛋白質が得られる。かかる水溶性蛋白質含有液を
、噴霧乾燥、凍結乾燥等の手法により乾燥して粉末化す
れば、綱フィブロイン由来の水溶性蛋白質粉末が得られ
る。
[0016]加水分解の程度は、部分加水分解された蛋
白質の平均分子量が150〜so、ooo、より好まし
くは200〜20,000の範囲となるようにすること
が好ましい。部分加水分解蛋白質の平均分子量が50゜
000以上の場合には、ゲル化能を有するため、加工が
困難であり、特に飲料タイプの食品に適用するには望ま
しくない。また平均分子量が150以下であると、苦味
や甘味等の呈味性が強くなり、食品へ利用するには好ま
しくなく、またコレステロール上昇抑制効果が十分発現
されなくなる。また、加水分解後の遊離のアミノ酸の生
成量は、原料であるフィブロイン繊維の1〜70重鳳%
重態ることが好ましい。アミノ酸の生成量がフィブロイ
ン繊維の70重量%以上であると、呈味性が強くなり、
またコレステロール上昇抑制効果も低下し、また12%
以下であると、水溶性蛋白質が十分低分子化されないの
で加工性が低下する。
[0017]なお、絹フィブロイン由来の水溶性蛋白質
溶液中の遊離アミノ酸の生成量は、水溶性蛋白質溶液を
塩基性炭酸鋼で処理し、アミノ酸およびペプチドを銅錯
体とし、これを陰イオン交換樹脂に吸着させ、0.05
Mホウ酸緩衝液で溶出された遊離アミノ酸を自動アミノ
酸分析機で定量することにより行った。ただし、酸性ア
ミノ酸については、ホウ酸緩衝液により遊離してこない
ので、水溶性蛋白質溶液をそのままアミノ酸分析機にか
けて定量した。
[00181本発明における食品とは、特に限定した形
態を示すものではなく、例えば、飲料、ゼリー、パン、
麺類、総菜、冷菓ならびに即席食品、缶詰、ビン詰等を
あげることができる。そして、一般の食品に利用されて
いる種々の添加剤(例えば、香料、着色料、乳化剤、膨
止剤、保存料、調味料等)を含んでいてもよい。
[0019]本発明に係るコレステロール上昇抑制食品
における絹フィブロイン由来蛋白質の含有率は、食品の
性状、組成、用途によっても好ましい範囲は異なるが、
−船釣には、綱フィブロイン由来の蛋白質を、1人1回
あたり500mg〜5g程度経口摂取できる程度の含有
率であれば特に限定されるものではない。すなわち、絹
フィブロイン由来蛋白質の含有率が少ないと、十分なコ
レステロール上昇抑制効果を発現するには、当該食品を
多量に摂取しなければならず、好ましくない。また、前
記綱フィブロイン由来の蛋白質は、当該食品中の全蛋白
質の10重量%以上を占めるよう調整されてなることが
好ましい。すなわち、全蛋白質中の絹フィブロイン由来
蛋白質の占有率が10重量%以下であると、他の蛋白質
の性状や組成による影響を大きく受けてしまい、実質的
にコレステロール上昇抑制効果を発現することが困難に
なる。
[00201なお、食品中の全蛋白質含有量は、当該食
品中のN(窒素分)量をキエルダール法等の常法に従っ
て測定し、得られた値に6.25を乗じて算出したもの
をいう。また、絹フィブロイン由来の蛋白質含有溶液(
あるいは粉末)中の蛋白質含有量も、当該溶液中のN量
を前記全蛋白質と同様の方法に従って算出したものをい
う。
[00211次に実施例を示して本発明をさらに詳細に
説明する。
[0022]
【実施例】実施例1.絹糸100g(水分10%)を、
45%塩化カルシウム水溶液中に溶解し、透析してフィ
ブロイン溶液を得た。これに市販のパパイン1gを加え
て、37℃、20分間撹拌した。次いで、90℃、30
分間加熱し、凍結乾燥した。得られた粉末は75gで、
平均分子量は約20,000、遊離アミノ酸生成量は2
.5重置%であり、水に溶けやすい性質を示した。
[0023]実施例2.絹糸100gに(水分10%)
を、濃塩酸に溶解し、水を加えて約2リツトルとし、塩
酸濃度を2Nに調整しながら、50℃、4時間30分加
水分解を行った。次いで、苛性ソーダにて中和し、電気
透析により脱塩後、減圧aw1により約200m1に濃
縮し、凍結乾燥を行った。得られた粉末は82g、平均
分子量300、遊離アミノ値酸生成量は28重量%で、
やや甘みを呈し、水に溶けやすく、飲みやすいものであ
った。
[o o 24]試験例1.実施例2で得られた粉末を
用いて、表1に示す合成飼料Cを作成し、この飼料を用
いてウィスター系雄性ラット (5周齢)を33日間飼
育した。飼育終了後、尾静脈より採血して、常法に従っ
て血清コレステロール値を測定した。対照として、表1
に示す合成飼料AおよびBを作成し、同様に飼育して、
血清コレステロール値を測定した。これらの結果を表3
に示す。なお、表中のアミノ酸混合物は、表1に示すフ
ィブロイン組成にあわせてアミノ酸を混合したものであ
り、基本飼料は、無蛋白質無繊維飼料(オリエンタル酵
母工業社製)を示すものである。
[0025][Table 1] [0013] Next, the process of obtaining protein from fibroin fibers will be explained. [00143 Fibroin fibers can be obtained from cocoons, silk threads, etc. by any known method, such as by dissolving, precipitation, extraction, purification, culturing, or the like. In the present invention, it is possible to use the fibroin fiber itself as a protein, but preferably,
Partial hydrolysis is carried out according to the following method. [0015] That is, the obtained fibroin fibers are heated and dissolved in a concentrated solution of mineral acids selected from hydrochloric acid, sulfuric acid, phosphoric acid, etc., partially hydrolyzed, and then neutralized and desalted to obtain an aqueous solution derived from silk fibroin. A solution containing the protein can be obtained.゛It is also possible to dissolve fibroin fibers, for example, in a 45% calcium chloride solution or in a solution in which the weight ratio of calcium chloride, ethanol, and water is 1:2:8, and then desalinate this solution to obtain silk fibroin-derived fibers. It is also possible to obtain a solution containing water-soluble proteins. If this solution is further hydrolyzed with a proteolytic enzyme selected from papain, samoase, elastase, vancreatin, etc., a partially hydrolyzed water-soluble protein that is reversibly soluble in water can be obtained. If such a water-soluble protein-containing liquid is dried and powdered by a method such as spray drying or freeze drying, a water-soluble protein powder derived from class fibroin can be obtained. [0016] The degree of hydrolysis is preferably such that the average molecular weight of the partially hydrolyzed protein is in the range of 150 to so, ooo, more preferably 200 to 20,000. If the average molecular weight of the partially hydrolyzed protein is 50.000 or more, it is difficult to process because of its gelling ability, and is particularly undesirable for application to beverage-type foods. Moreover, if the average molecular weight is 150 or less, taste characteristics such as bitterness and sweetness will be strong, making it undesirable for use in foods, and the effect of suppressing the increase in cholesterol will not be sufficiently expressed. In addition, the amount of free amino acids produced after hydrolysis is 1 to 70% of the raw material fibroin fiber.
Preferably, the patient is in serious condition. When the amount of amino acids produced is 70% by weight or more of the fibroin fiber, the taste will be strong,
The effect of suppressing cholesterol rise also decreased, and by 12%
If it is below, the water-soluble protein will not be reduced to a sufficiently low molecular weight, resulting in poor processability. [0017] The amount of free amino acids produced in a water-soluble protein solution derived from silk fibroin can be determined by treating the water-soluble protein solution with basic carbonate steel, making amino acids and peptides into copper complexes, and converting this into an anion exchange resin. Adsorb, 0.05
This was done by quantifying the free amino acids eluted with M borate buffer using an automatic amino acid analyzer. However, since acidic amino acids were not liberated by the boric acid buffer, the water-soluble protein solution was directly subjected to an amino acid analyzer for quantification. [00181 The food in the present invention does not have a particularly limited form, and includes, for example, beverages, jelly, bread,
Noodles, side dishes, frozen desserts, instant foods, canned foods, bottled foods, etc. can be mentioned. It may also contain various additives used in general foods (for example, fragrances, coloring agents, emulsifiers, swelling agents, preservatives, seasonings, etc.). [0019] The preferable range of the content of silk fibroin-derived protein in the cholesterol increase-suppressing food according to the present invention varies depending on the properties, composition, and use of the food.
- Boat fishing is not particularly limited as long as the protein content derived from rope fibroin is at a level that allows one person to orally ingest 500 mg to 5 g of protein at a time. That is, if the content of silk fibroin-derived protein is low, a large amount of the food must be ingested in order to exhibit a sufficient cholesterol rise suppressing effect, which is not preferable. Further, it is preferable that the protein derived from the class fibroin is adjusted to account for 10% by weight or more of the total protein in the food. In other words, if the occupancy of silk fibroin-derived protein in the total protein is 10% by weight or less, it will be greatly influenced by the properties and composition of other proteins, and it will be difficult to substantially exhibit the effect of suppressing cholesterol rise. become. [00201 The total protein content in a food is calculated by measuring the amount of N (nitrogen) in the food according to a conventional method such as the Kjeldahl method, and multiplying the obtained value by 6.25. . In addition, a protein-containing solution derived from silk fibroin (
Alternatively, the protein content in the powder) refers to the amount of N in the solution calculated according to the same method as for the total protein. [00211] Next, the present invention will be explained in more detail with reference to Examples. [0022] [Example] Example 1. 100g of silk thread (moisture 10%),
It was dissolved in a 45% calcium chloride aqueous solution and dialyzed to obtain a fibroin solution. 1 g of commercially available papain was added to this, and the mixture was stirred at 37°C for 20 minutes. Then, 90°C, 30
Heat for 1 minute and lyophilize. The powder obtained was 75 g.
The average molecular weight is approximately 20,000, and the amount of free amino acids produced is 2
.. 5%, indicating that it is easily soluble in water. [0023] Example 2. 100g of silk thread (10% moisture)
was dissolved in concentrated hydrochloric acid, water was added to make a total volume of about 2 liters, and hydrolysis was carried out at 50°C for 4 hours and 30 minutes while adjusting the hydrochloric acid concentration to 2N. Next, the mixture was neutralized with caustic soda, desalted by electrodialysis, concentrated to about 200 ml under reduced pressure aw1, and freeze-dried. The obtained powder was 82 g, average molecular weight was 300, free amino acid production amount was 28% by weight,
It had a slightly sweet taste, was easily soluble in water, and was easy to drink. [o o 24] Test example 1. Synthetic feed C shown in Table 1 was prepared using the powder obtained in Example 2, and male Wistar rats (5 weeks old) were raised using this feed for 33 days. After the breeding was completed, blood was collected from the tail vein, and serum cholesterol levels were measured according to a conventional method. As a control, Table 1
Synthetic feeds A and B shown in the following were prepared and reared in the same manner.
Serum cholesterol levels were measured. These results are shown in Table 3.
Shown below. The amino acid mixture in the table is a mixture of amino acids according to the fibroin composition shown in Table 1, and the basic feed is a protein-free and fiber-free feed (manufactured by Oriental Yeast Industry Co., Ltd.). [0025]
【表2】 [0026][Table 2] [0026]
【表3】
[00271表3に示すように、本発明に係るフィブロ
イン由来蛋白質を含有させた飼料を投与した群では、明
らかに血清コレステロールの上昇が抑制された。
[0028][Table 3] [00271] As shown in Table 3, the increase in serum cholesterol was clearly suppressed in the group to which the feed containing the fibroin-derived protein according to the present invention was administered. [0028]
【発明の効果】以上、詳述したように、本発明に係る綱
フィブロイン由来の水溶性蛋白質を含有する食品は、顕
著なコレステロール上昇抑制効果を有するので、高コレ
ステロール、糖尿病、肥満等の予防、治療等に有用であ
る。Effects of the Invention As detailed above, the food containing the water-soluble protein derived from the class fibroin according to the present invention has a remarkable effect of suppressing the increase in cholesterol, and therefore can be used to prevent high cholesterol, diabetes, obesity, etc. It is useful for treatment, etc.
Claims (5)
とを特徴とするコレステロール上昇抑制食品。1. A food product for suppressing cholesterol rise, characterized by containing a protein derived from silk fibroin.
食品中の全蛋白質の10重量%以上を占めるよう調整さ
れてなる請求項1記載のコレステロール上昇抑制食品。2. The cholesterol rise-suppressing food according to claim 1, wherein the silk fibroin-derived protein is adjusted to account for 10% by weight or more of the total protein in the food.
の部分加水分解物である請求項1又は2記載のコレステ
ロール上昇抑制食品。3. The cholesterol increase-suppressing food according to claim 1, wherein the protein is a partial hydrolyzate of silk fibroin-derived protein.
0〜50,000である請求項3に記載のコレステロー
ル上昇抑制食品。4. The average molecular weight of the partial hydrolyzate is 15
4. The cholesterol increase-inhibiting food according to claim 3, which has a molecular weight of 0 to 50,000.
ノ酸の生成量が1〜70%となるまで部分加水分解し、
得られた部分加水分解蛋白質を添加することを特徴とす
るコレステロール上昇抑制食品の製造方法。5. Partially hydrolyzing a protein derived from silk fibroin until the amount of free amino acids produced is 1 to 70%,
A method for producing a food that suppresses cholesterol rise, which comprises adding the obtained partially hydrolyzed protein.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2412823A JPH04210577A (en) | 1990-12-05 | 1990-12-05 | Cholesterol level rise-inhibitory food and production thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2412823A JPH04210577A (en) | 1990-12-05 | 1990-12-05 | Cholesterol level rise-inhibitory food and production thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH04210577A true JPH04210577A (en) | 1992-07-31 |
Family
ID=18521582
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2412823A Pending JPH04210577A (en) | 1990-12-05 | 1990-12-05 | Cholesterol level rise-inhibitory food and production thereof |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH04210577A (en) |
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH04267861A (en) * | 1991-02-19 | 1992-09-24 | Nagahama Sangyo Kk | Milk powder-containing dressing and production thereof |
| JPH06292595A (en) * | 1993-04-05 | 1994-10-21 | Kiyoshi Hirabayashi | Production of low-molecular weight fibroin |
| JPH11139986A (en) * | 1997-11-04 | 1999-05-25 | Ichimaru Pharcos Co Ltd | Bioactive composition derived from silk protein hydrolyzate |
| KR20020073621A (en) * | 2001-03-15 | 2002-09-28 | 김영호 | The functional bread making by the supplementation with silkpeptide and process for preparation thereof |
| KR100365291B1 (en) * | 2000-06-07 | 2002-12-18 | 주식회사 바이오썸 | An agent for preventing development of alcoholic fatty liver comprising an active substance derived from silk fibroin |
| KR100754276B1 (en) * | 2007-02-22 | 2007-09-03 | 김재현 | Health supplements containing silk peptides and calcium |
| JP2008088185A (en) * | 2007-11-29 | 2008-04-17 | Ichimaru Pharcos Co Ltd | Immunostimulant derived from silk protein hydrolyzate |
| JP2009514783A (en) * | 2004-07-31 | 2009-04-09 | バイオグランド シーオー エル ティー ディー | Silk peptide for improving neuroprotection and nerve function efficacy and method for producing the same |
| JP2012040010A (en) * | 2011-09-14 | 2012-03-01 | Biogrand Co Ltd | Use of composition as additive for food or functional food |
-
1990
- 1990-12-05 JP JP2412823A patent/JPH04210577A/en active Pending
Cited By (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH04267861A (en) * | 1991-02-19 | 1992-09-24 | Nagahama Sangyo Kk | Milk powder-containing dressing and production thereof |
| JPH06292595A (en) * | 1993-04-05 | 1994-10-21 | Kiyoshi Hirabayashi | Production of low-molecular weight fibroin |
| JPH11139986A (en) * | 1997-11-04 | 1999-05-25 | Ichimaru Pharcos Co Ltd | Bioactive composition derived from silk protein hydrolyzate |
| KR100365291B1 (en) * | 2000-06-07 | 2002-12-18 | 주식회사 바이오썸 | An agent for preventing development of alcoholic fatty liver comprising an active substance derived from silk fibroin |
| KR20020073621A (en) * | 2001-03-15 | 2002-09-28 | 김영호 | The functional bread making by the supplementation with silkpeptide and process for preparation thereof |
| JP2009514783A (en) * | 2004-07-31 | 2009-04-09 | バイオグランド シーオー エル ティー ディー | Silk peptide for improving neuroprotection and nerve function efficacy and method for producing the same |
| JP4896017B2 (en) * | 2004-07-31 | 2012-03-14 | バイオグランド シーオー エル ティー ディー | Composition for improving brain disease or brain function |
| KR100754276B1 (en) * | 2007-02-22 | 2007-09-03 | 김재현 | Health supplements containing silk peptides and calcium |
| JP2008088185A (en) * | 2007-11-29 | 2008-04-17 | Ichimaru Pharcos Co Ltd | Immunostimulant derived from silk protein hydrolyzate |
| JP2012040010A (en) * | 2011-09-14 | 2012-03-01 | Biogrand Co Ltd | Use of composition as additive for food or functional food |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN101568552B (en) | Collagen peptide composition and food and drink containing it | |
| CN108410938A (en) | A method of preparing low bitter taste lactalbumin antioxidant peptide powder | |
| JPH04210577A (en) | Cholesterol level rise-inhibitory food and production thereof | |
| JP2737790B2 (en) | Food containing silk protein hydrolyzate and method for producing the same | |
| JPH04210576A (en) | Blood sugar level rise-inhibitory food and production thereof | |
| KR19990074787A (en) | Method for preparing silk powder peptide by enzymatic digestion | |
| JP7787424B2 (en) | Method for producing a deprestatin-containing composition | |
| JP2000102362A (en) | Food additive and food composition containing the same | |
| JPH06511506A (en) | Process for preparing starch esters for clinical, especially parenteral use | |
| JPH06292595A (en) | Production of low-molecular weight fibroin | |
| JP3398490B2 (en) | Whey protein peptide composition and method for producing the same | |
| KR100679712B1 (en) | How to make collagen from starfish | |
| KR102240111B1 (en) | Cosmetic composition for moisturizing skin and improving skin wrinkles containing nano collagen peptide chelate mineral | |
| JP3408739B2 (en) | Calcium absorption promoter and calcium supplement | |
| JPH01256351A (en) | Food using silk protein and production thereof | |
| JP3448344B2 (en) | Peptide composition | |
| JPWO1998042862A1 (en) | Iron-casein hydrolysate complex and method for producing same | |
| NL9400418A (en) | Processes for the preparation of glutamine-rich peptides and nutritional preparations made therewith. | |
| JPH0458947B2 (en) | ||
| KR102224513B1 (en) | Method for manufacturing sashimi jelly | |
| JPH0254061B2 (en) | ||
| JPH0362382B2 (en) | ||
| JP2008118962A (en) | Chewable tablet | |
| CN111493195B (en) | Salted egg white enzymatic hydrolyzate soft candy and preparation method thereof | |
| JP4304267B2 (en) | Functional protein and method for producing the same |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20000328 |