JPH04210576A - Blood sugar level rise-inhibitory food and production thereof - Google Patents
Blood sugar level rise-inhibitory food and production thereofInfo
- Publication number
- JPH04210576A JPH04210576A JP2412822A JP41282290A JPH04210576A JP H04210576 A JPH04210576 A JP H04210576A JP 2412822 A JP2412822 A JP 2412822A JP 41282290 A JP41282290 A JP 41282290A JP H04210576 A JPH04210576 A JP H04210576A
- Authority
- JP
- Japan
- Prior art keywords
- water
- blood sugar
- food
- soluble protein
- 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
- 235000013305 food Nutrition 0.000 title claims abstract description 30
- 239000008280 blood Substances 0.000 title claims abstract description 21
- 210000004369 blood Anatomy 0.000 title claims abstract description 21
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 5
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 36
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 36
- 108010022355 Fibroins Proteins 0.000 claims abstract description 34
- 150000001413 amino acids Chemical class 0.000 claims abstract description 20
- 238000000034 method Methods 0.000 claims description 8
- 230000003301 hydrolyzing effect Effects 0.000 claims description 2
- 230000000694 effects Effects 0.000 abstract description 9
- 230000007062 hydrolysis Effects 0.000 abstract description 5
- 238000006460 hydrolysis reaction Methods 0.000 abstract description 5
- 239000004480 active ingredient Substances 0.000 abstract 2
- 235000018102 proteins Nutrition 0.000 description 27
- 235000001014 amino acid Nutrition 0.000 description 18
- 239000000243 solution Substances 0.000 description 13
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 9
- 239000000835 fiber Substances 0.000 description 9
- 239000008103 glucose Substances 0.000 description 9
- 239000000203 mixture Substances 0.000 description 8
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 108010013296 Sericins Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 239000012460 protein solution Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 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
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 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
- 239000000872 buffer Substances 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 238000012937 correction Methods 0.000 description 2
- 238000011033 desalting Methods 0.000 description 2
- 102000038379 digestive enzymes Human genes 0.000 description 2
- 108091007734 digestive enzymes Proteins 0.000 description 2
- 230000001965 increasing effect Effects 0.000 description 2
- 235000015110 jellies Nutrition 0.000 description 2
- 239000008274 jelly Substances 0.000 description 2
- 230000001766 physiological effect Effects 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 235000019640 taste Nutrition 0.000 description 2
- 238000012360 testing method Methods 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
- 208000008589 Obesity Diseases 0.000 description 1
- 102000016387 Pancreatic elastase Human genes 0.000 description 1
- 108010067372 Pancreatic elastase Proteins 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 239000004365 Protease Substances 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
- 235000019658 bitter taste Nutrition 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
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 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
- 235000011850 desserts Nutrition 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 235000019621 digestibility Nutrition 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 235000010855 food raising agent Nutrition 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
- 201000001421 hyperglycemia Diseases 0.000 description 1
- 230000002218 hypoglycaemic effect Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000005259 measurement Methods 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
- 238000006386 neutralization reaction Methods 0.000 description 1
- 235000012149 noodles Nutrition 0.000 description 1
- 235000020824 obesity Nutrition 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 235000013324 preserved food Nutrition 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
- 235000011962 puddings Nutrition 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
- 238000000926 separation method Methods 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
- 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)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Abstract
Description
[00011 [00011
【産業上の利用分野]本発明は、血糖上昇抑制食品に関
する。さらに詳しくは、本発明は絹フィブロイン由来の
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】綱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、大昔から、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、ト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1−256352
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、絹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 foods that suppress blood sugar rise. More specifically, the present invention relates to a food product characterized by containing water-soluble protein derived from silk fibroin, and a method for producing the food product. [0002] [0002] [0002] The fibers are composed of proteins whose main components are fibroin and sericin, and have been used as fibers since ancient times. Because it is not easily affected by digestive enzymes such as, there have been no attempts to use it in foods. Therefore, the present inventor has developed a technology for using leukemia white matter, mainly fibroin, in foods, such as in gelatinized foods such as pudding and jelly (Japanese Patent Laid-Open No. 1-256352).
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 ( (Japanese Unexamined Patent Publication No. 177864/1999). [0003]However, it is still unclear what effect foods containing silk 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、絹フィ
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水溶性蛋白質が、
驚くべきことに顕著な血糖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 water-soluble proteins derived from silk fibroin
Surprisingly, the present invention was completed based on the finding that it exerts a remarkable effect of suppressing blood sugar rise. [0005]
【課題を解決するための手段】すなわち、本発明によれ
ば、絹フィブロイン由来の水溶性蛋白質を含有すること
を特徴とする血糖上昇抑制食品が提供される。
[0006]前記水溶性蛋白質の平均分子量は、150
〜so、oooであることが好ましい。
[0007]前記水溶性蛋白質は、絹フィブロイン由来
蛋白質の加水分解物であることが好ましい。
[0008]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量が1〜70%となるまで
加水分解し、得られた部分加水分解蛋白質を添加するこ
とを特徴とする血糖上昇抑制食品の製造方法を示すもの
である。
[00091以下、本発明の詳細な説明する。
[00101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。絹フィブロインは、絹糸から製錬によ
りセリシンを除去することにより得ることができる。綱
フィブロインはグリシン(G l y)とアラニン(A
1a)を非常に多く含む蛋白質で、(Gly3A1a
zX2)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。
[00111[Means for Solving the Problems] That is, according to the present invention, there is provided a food product for suppressing blood sugar rise characterized by containing water-soluble protein derived from silk fibroin. [0006] The average molecular weight of the water-soluble protein is 150
~so, ooo are preferred. [0007] The water-soluble protein is preferably a hydrolyzate of silk fibroin-derived protein. [0008] The present invention also provides a method for increasing blood sugar, characterized by hydrolyzing a protein derived from silk fibroin until the amount of free amino acids produced is 1 to 70%, and adding the obtained partially hydrolyzed protein. This shows a method for producing a suppressed food. [00091 Hereinafter, the present invention will be described in detail. [00101 Silk thread is a fibrous protein secreted from the silk gland of a silkworm, and is made by solidifying fibroin fibers with sericin. Silk fibroin can be obtained by removing sericin from silk thread by smelting. Class fibroin contains glycine (Gly) and alanine (A
1a), and contains a large amount of (Gly3A1a
zX2)n (X is an amino acid other than glycine or alanine)
It is said that the composition is expressed by An example of the composition is shown in Table 1. [00111
【表1]
[001,2]この絹フィブロインから水溶性蛋白質を
得る工程について説明する。
[0013]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
。
[0014]フィブロイン繊維から水溶性蛋白質を得る
には、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、脱塩して綱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
ことで綱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
ばれ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、絹フィブロイ
ン由来の水溶性蛋白質粉末が得られる。
[0015]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、また血糖上昇効果が十分発言されなくなる。
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玉量%であることが好
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−にであると、呈味性が強くなり、また血糖上昇
抑制効果も低下し、また1%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。
[0016]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
N1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。
[0017]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、ピン詰等を
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
化剤、保存料、調味料等)を含んでいてもよい。
[001,8]当該食品中の、綱フィブロイン由来の水
溶性蛋白質の含有率としては、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
ィブロイン由来の水溶性蛋白質を、1人1回あたり50
0mg〜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。綱フィブロイン由来の水
溶性蛋白質の含有率が少ないと、十分な血糖上昇抑制効
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。なお、特に可消化糖質が主成分で
ある食品に適用する場合には、水溶性蛋白質の含有率は
当該糖質に対し5重量%以上とされることが好ましい。
[00191次に実施例を示して本発明をさらに詳細に
説明する。
[00201
【実施例]
実施例1.絹糸100gを2規定塩酸に溶解し、70℃
、1時間処理した後、
苛性ソーダにて中和し、透析してフィブロイン溶液を得
た。これを噴霧乾燥し、白色粉末72gを得た。このも
のの平均分子量は約1200、遊離アミノ酸生成量は5
.8重量%であり、水に溶けやすく、わずかに甘みを呈
し、飲みやすい性質を示した。
[00211
試験例1.ウィスター系雄性ラッ1−(5周齢)を用い
て、耐糖性を低下させる
ためラードを添加した表2に示す飼料を与えて、2週間
飼育した後、各グループ間の平均体重が等しくなるよう
に群分を行った。なお基本飼料としては、無蛋白質無繊
維飼料(オリエンタル酵母工業社製)を用いた。各群の
平均体重はすべて175gとした。またラットは、測定
開始24時間前から絶食させておいた。
[0022]
【表2】
[0023]試料としては、9%(重量/容量)グルコ
ース溶液の群(試料1)、3%(N量/容量)のフィブ
ロイン構成アミノ酸にあわせたアミノ酸混合物を含む9
%(重量/容量)のグルコース溶液の群(試料2)、3
%(重量/容量)の実施例1で得た水溶性蛋白質粉末を
含む9%(重量/容量)のグルコース溶液の群(試料3
)を用い、これらの試料各5mlをゾンデで経口投与し
た。投与後、0分、30分、60分、90分経過後に、
尾静脈より採血し、血漿分離後、グルコーステストワコ
ー(和光紬薬社製)を用いて血糖値測定を行った。
その結果を図1に示す。
[0024]図1より、本発明に係る絹フィブロイン由
来の水溶性蛋白質を含有する試料投与群では、顕著な血
糖上昇抑制効果が認められた。
[0025][Table 1] [001,2] The process of obtaining water-soluble protein from this silk fibroin will be explained. [0013] Fibroin fibers can be obtained from cocoons, silk threads, etc. by any known method, such as by dissolving, precipitating, extracting, purifying, culturing, or the like. [0014] In order to obtain water-soluble protein from fibroin fibers, the obtained fibroin fibers are heated and dissolved in a concentrated solution of mineral acids selected from hydrochloric acid, sulfuric acid, phosphoric acid, etc., and after partial hydrolysis, neutralization, A solution containing water-soluble proteins derived from class fibroin can be obtained by desalting. In addition, fibroin fibers can be prepared using, for example, a 45% calcium chloride solution.
Or the weight ratio of calcium chloride, ethanol and water is 1
A solution containing a water-soluble protein derived from class fibroin can also be obtained by dissolving it in a solution with a ratio of 2:8 and desalting this solution. 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 silk fibroin can be obtained. [0015] 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 blood sugar increasing effect will not be sufficiently pronounced. Further, the amount of free amino acids produced after hydrolysis is preferably 1 to 70% by weight of the fibroin fibers as the raw material. If the amount of amino acids produced is more than 70% by weight of the fibroin fiber, the taste will be strong and the effect of suppressing blood sugar rise will be reduced, and if it is less than 1%, the water-soluble protein will have a sufficiently low molecular weight. Since this process is not carried out, workability deteriorates. [0016] 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 N1 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. [0017] The food in the present invention does not have a particularly limited form, and includes, for example, drinks, jelly, bread,
Examples include noodles, side dishes, frozen desserts, instant foods, canned foods, and pinned foods. It may also contain various additives (for example, fragrances, colorants, emulsifiers, leavening agents, preservatives, seasonings, etc.) that are used in general foods. [001,8] The preferable range of the content of water-soluble protein derived from rope fibroin in the food concerned varies depending on the properties, composition, and use of the food. 50 protein per serving per person
There is no particular limitation as long as the content is such that it can be taken orally in the range of 0 mg to 5 g. If the content of water-soluble protein derived from class fibroin is low, a large amount of the food must be ingested in order to exhibit a sufficient blood sugar rise suppressing effect, which is not preferable. In particular, when the present invention is applied to foods whose main component is digestible carbohydrates, the content of water-soluble protein is preferably 5% by weight or more based on the carbohydrates. [00191] Next, the present invention will be explained in more detail by showing examples. [00201 [Example] Example 1. Dissolve 100g of silk thread in 2N hydrochloric acid and heat at 70°C.
After treatment for 1 hour, it was neutralized with caustic soda and dialyzed to obtain a fibroin solution. This was spray-dried to obtain 72 g of white powder. The average molecular weight of this product is approximately 1200, and the amount of free amino acids produced is 5
.. It was 8% by weight, easily soluble in water, had a slightly sweet taste, and was easy to drink. [00211 Test Example 1. Male Wistar rats (5 weeks old) were fed the diet shown in Table 2 with the addition of lard to reduce sugar tolerance, and after being raised for 2 weeks, the average weight of each group was made equal. The group was divided into groups. As the basic feed, a protein-free and fiber-free feed (manufactured by Oriental Yeast Industry Co., Ltd.) was used. The average weight of each group was 175 g. The rats were also fasted for 24 hours before the start of the measurement. [0022] [Table 2] [0023] The samples include a group of 9% (weight/volume) glucose solutions (sample 1), 9 containing an amino acid mixture tailored to the fibroin-constituting amino acids of 3% (N amount/volume)
% (wt/vol) glucose solution group (sample 2), 3
A group of 9% (wt/vol) glucose solutions containing % (wt/vol) water-soluble protein powder obtained in Example 1 (sample 3)
), and 5 ml of each of these samples was orally administered using a probe. After 0 minutes, 30 minutes, 60 minutes, and 90 minutes after administration,
Blood was collected from the tail vein, and after plasma separation, blood sugar levels were measured using Glucose Test Wako (manufactured by Wako Tsumugi Pharmaceutical Co., Ltd.). The results are shown in Figure 1. [0024] From FIG. 1, a significant blood sugar rise suppressing effect was observed in the sample administration group containing the water-soluble protein derived from silk fibroin according to the present invention. [0025]
【発明の効果】以上、詳述したように、本発明に係る絹
フィブロイン由来の水溶性蛋白質を含有する食品は、顕
著な血糖上昇抑制効果を有するので、高血糖、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 silk fibroin according to the present invention has a remarkable effect of suppressing blood sugar rise, so it can prevent hyperglycemia, diabetes, etc.
It is useful for prevention and treatment of obesity, etc.
【提出日】平成3年4月23日[Submission date] April 23, 1991
【手続補正1】[Procedural amendment 1]
【補正対象項目名】明細書[Name of item to be amended] Specification
【補正対象項目名】図面の簡単な説明[Name of item to be corrected] Brief description of the drawing
【補正方法】追加[Correction method] Added
図1は、グルコース溶液のみを投与したラットから経時
的に採取された血液中の血糖値変化、フィブロイン構成
アミノ酸にあわせたアミノ酸混合物を含むグルコース溶
液を投与したラットから経時的に採取された血液中の血
糖値変化、本発明の血糖上昇抑制食品を含むグルコース
溶液を投与したラットから経時的に採取された血液中の
血糖値変化を示す図である。
識別記号Figure 1 shows changes in blood glucose levels collected over time from rats administered only a glucose solution, and changes in blood glucose levels collected over time from rats administered a glucose solution containing an amino acid mixture tailored to the fibroin-constituting amino acids. FIG. 2 is a diagram showing changes in blood sugar levels in blood collected over time from rats to which a glucose solution containing the hypoglycemic food of the present invention was administered. Identification symbol
Claims (4)
することを特徴とする血糖上昇抑制食品。1. A food for suppressing blood sugar elevation, characterized by containing a water-soluble protein derived from silk fibroin.
〜50,000である請求項1記載の血糖上昇抑制食品
。[Claim 2] The average molecular weight of the water-soluble protein is 150.
The food for suppressing blood sugar rise according to claim 1, which has a molecular weight of 50,000 to 50,000.
蛋白質の加水分解物である請求項2記載の血糖上昇抑制
食品。3. The food for suppressing blood sugar rise according to claim 2, wherein the water-soluble protein is a hydrolyzate of silk fibroin-derived protein.
ノ酸の生成量が1〜70%となるまで加水分解し、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血
糖上昇抑制食品の製造方法。4. Production of a food for suppressing blood sugar rise, which comprises hydrolyzing a protein derived from silk fibroin until the amount of free amino acids produced is 1 to 70%, and adding the resulting partially hydrolyzed protein. Method.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2412822A JPH04210576A (en) | 1990-12-05 | 1990-12-05 | Blood sugar level rise-inhibitory food and production thereof |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2412822A JPH04210576A (en) | 1990-12-05 | 1990-12-05 | Blood sugar level rise-inhibitory food and production thereof |
Publications (1)
Publication Number | Publication Date |
---|---|
JPH04210576A true JPH04210576A (en) | 1992-07-31 |
Family
ID=18521581
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2412822A Pending JPH04210576A (en) | 1990-12-05 | 1990-12-05 | Blood sugar level rise-inhibitory food and production thereof |
Country Status (1)
Country | Link |
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JP (1) | JPH04210576A (en) |
Cited By (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH11139986A (en) * | 1997-11-04 | 1999-05-25 | Ichimaru Pharcos Co Ltd | Physiologically active composition derived from hydrolyzate of silk protein |
JP2004269395A (en) * | 2003-03-07 | 2004-09-30 | Minato Pharmaceutical Co Ltd | Hypotensive action-having composition |
KR100770686B1 (en) * | 2006-05-22 | 2007-10-29 | 주식회사 브레인가드 | Compositions for treating or preventing diabetes comprising silk peptides |
JP2008088185A (en) * | 2007-11-29 | 2008-04-17 | Ichimaru Pharcos Co Ltd | Immunostimulant derived from silk protein hydrolysate |
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 |
WO2009083411A3 (en) * | 2007-12-28 | 2009-10-01 | Dsm Ip Assets B.V. | Uses for aqueous streams containing proteins |
JP2012040010A (en) * | 2011-09-14 | 2012-03-01 | Biogrand Co Ltd | Use of composition as additive for food or functional food |
JP2018030781A (en) * | 2016-08-22 | 2018-03-01 | ドクターセラム株式会社 | Glp-1 production accelerator, and insulin secretion promoter, hypoglycemic agent or food and drink containing the glp-1 production accelerator |
-
1990
- 1990-12-05 JP JP2412822A patent/JPH04210576A/en active Pending
Cited By (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH11139986A (en) * | 1997-11-04 | 1999-05-25 | Ichimaru Pharcos Co Ltd | Physiologically active composition derived from hydrolyzate of silk protein |
JP2004269395A (en) * | 2003-03-07 | 2004-09-30 | Minato Pharmaceutical Co Ltd | Hypotensive action-having composition |
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 |
KR100770686B1 (en) * | 2006-05-22 | 2007-10-29 | 주식회사 브레인가드 | Compositions for treating or preventing diabetes comprising silk peptides |
JP2008088185A (en) * | 2007-11-29 | 2008-04-17 | Ichimaru Pharcos Co Ltd | Immunostimulant derived from silk protein hydrolysate |
WO2009083411A3 (en) * | 2007-12-28 | 2009-10-01 | Dsm Ip Assets B.V. | Uses for aqueous streams containing proteins |
JP2012040010A (en) * | 2011-09-14 | 2012-03-01 | Biogrand Co Ltd | Use of composition as additive for food or functional food |
JP2018030781A (en) * | 2016-08-22 | 2018-03-01 | ドクターセラム株式会社 | Glp-1 production accelerator, and insulin secretion promoter, hypoglycemic agent or food and drink containing the glp-1 production accelerator |
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