JP2008220208A - Method for producing low-molecular collagen - Google Patents
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- Coloring Foods And Improving Nutritive Qualities (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
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Abstract
Description
本発明は、魚鱗を煮沸抽出してコラーゲンを抽出した時に発生する副産物である抽出残渣を原料として使用した低分子コラーゲンの製造方法を提供する。更に詳しくは、煮沸抽出残渣の廃棄物を利用して高収率、且つ環境に優しく、低コストの低分子コラーゲンの製造方法を提供する。 The present invention provides a method for producing low-molecular-weight collagen using, as a raw material, an extraction residue that is a byproduct generated when boiled fish scales are extracted by extracting collagen. More specifically, the present invention provides a method for producing low-molecular collagen that is low in cost, high in yield, environmentally friendly, using waste of boiling extraction residue.
コラーゲンは、真皮、靭帯、腱、軟骨などに存在し、総コラーゲン量は全蛋白質の３０％を占める重要な役割を担っている。例えば、切傷や火傷などの皮膚の損傷治療、美容整形、美肌用化粧品、ハンドクリームなどに添加して使用されている。また、健康食品として粉末や錠剤として直接摂取して体内コラーゲンの栄養補給剤としても使用されている。 コラーゲンは、生体蛋白の主要な構成成分であり、殆んど全ての動物の体内に保有しているため、哺乳類、鳥類、魚類などから取り出すことができる。コラーゲンは、牛皮、豚皮、鳥皮、魚皮、魚鱗などのコラーゲン含有量が多い部位から煮沸抽出して取り出して回収（非特許文献１参照。）するのが一般的である。魚類からの低分子コラーゲンの製造は、魚皮や魚鱗を原料に油脂分を取り除いて、塩酸溶液中に浸漬してカルシウムを除去した後、煮沸で抽出してコラーゲン液を採取し、抽出した高分子コラーゲン液にプロテアーゼなどの蛋白分解酵素を作用させて低分子コラーゲンやコラーゲンペプタイドを得ていた。 Collagen is present in the dermis, ligament, tendon, cartilage and the like, and the total collagen amount plays an important role accounting for 30% of the total protein. For example, it is used by adding to skin damage treatment such as cuts and burns, cosmetic surgery, cosmetics for skin care, and hand cream. In addition, it is directly ingested as a powder or tablet as a health food and used as a nutritional supplement for in vivo collagen. Collagen is a major component of biological proteins and is retained in almost all animals, so it can be extracted from mammals, birds, fish and the like. Generally, collagen is boiled and extracted from sites with high collagen content such as cow skin, pig skin, chicken skin, fish skin, fish scales, etc., and collected (see Non-Patent Document 1). Production of low molecular weight collagen from fish is accomplished by removing oils and fats from fish skin and fish scales, soaking in hydrochloric acid solution to remove calcium, extracting by boiling, collecting collagen solution, Proteolytic enzymes such as proteases were allowed to act on the molecular collagen solution to obtain low molecular collagen and collagen peptides.
魚鱗は、魚種によって大きさや配合組成が多少異なるが、概ねカルシウム含有量が３０％程度あり、脱灰鱗からの煮沸によるコラーゲン抽出率は３０％程度で、多くても４０％未満であり、魚鱗からの収率が悪く高価なものとなっていた。 Fish scales are slightly different in size and composition depending on the fish species, but generally have a calcium content of about 30%, the collagen extraction rate by boiling from demineralized scale is about 30%, and at most less than 40%, The yield from fish scales was poor and expensive.
また、煮沸抽出した後の抽出残渣の外観はクリーム色から黄色を呈し、乾燥すると黄褐色から茶褐色となるため、従来は産業廃棄物として捨てられるか乾燥して肥料又は飼料とされて再利用する程度であった。 In addition, the appearance of the extraction residue after boiling extraction has a yellow color from cream to yellow, and from yellowish brown to brown when dried, it is conventionally discarded as industrial waste or dried and reused as fertilizer or feed It was about.
一方、魚鱗から高収率でコラーゲンを製造する方法としては、魚鱗を脱灰せず直接粉砕して蛋白分解酵素を作用させる方法（特許文献１、３参照。）や、蛋白分解酵素の他に魚鱗が分解し易いようにキチナーゼなどの酵素を作用させる方法（特許文献２参照。）が知られている。また、塩基性領域で各種のプロテアーゼを作用させる方法（特許文献４参照。）においては、アルカリの作用で分子量が極めて小さいオリゴペプタイドが得られることが知られている。 On the other hand, as a method for producing collagen from fish scales in high yield, there is a method of directly crushing fish scales without demineralizing them to act on proteolytic enzymes (see Patent Documents 1 and 3). There is known a method (see Patent Document 2) in which an enzyme such as chitinase is allowed to act so that fish scales are easily decomposed. In addition, it is known that an oligopeptide having an extremely small molecular weight can be obtained by the action of an alkali in a method in which various proteases are allowed to act in a basic region (see Patent Document 4).
先行技術における魚鱗を直接粉砕して蛋白分解酵素を作用させる方法は、コラーゲン特有の三重螺旋構造が強固なために魚鱗の粉砕が極めて困難であり、蛋白分解酵素を作用させた後のカルシウムの分離除去が必要であり、高価な粉砕機や分離装置の購入などの問題があった。
また、魚鱗が分解し易いようにキチナーゼなどの酵素を作用させた後に蛋白分解酵素を作用させる方法は、収率はある程度アップするが、かなりの残渣物が残存する。また、分子量の異なる多種の酵素を併用するため、分解物中からの酵素蛋白の除去が難しい。
また、塩基性領域でアルカリプロテアーゼを作用させる方法は、アルカリによる分解が主となりオリゴペプタイド（アミノ酸が３量体以下で分子量２００以下程度）のみしか得られなくなるなどの問題があった。
In the prior art, the method of directly crushing fish scales to act on proteolytic enzymes is extremely difficult to crush fish scales due to the strong triple helix structure unique to collagen, and separation of calcium after the action of proteolytic enzymes Removal was necessary, and there were problems such as the purchase of expensive pulverizers and separators.
In addition, the method in which an enzyme such as chitinase is allowed to act so that fish scales are easily decomposed and then the protease is allowed to act increases the yield to some extent, but a considerable residue remains. In addition, since various enzymes having different molecular weights are used in combination, it is difficult to remove the enzyme protein from the degradation product.
In addition, the method in which an alkaline protease is allowed to act in the basic region has a problem that only oligopeptides (amino acids having a trimer or less and a molecular weight of about 200 or less) can be obtained mainly due to decomposition by alkali.
このように、魚鱗からコラーゲン製造において、環境にやさしく、高収率で安価な低分子コラーゲンの製造方法が望まれていた。 Thus, in the production of collagen from fish scales, there has been a demand for a method for producing low-molecular collagen that is environmentally friendly, high-yield, and inexpensive.
そこで、本発明者らは前記課題を解決すべく、種々検討した結果、魚鱗からコラーゲンを煮沸抽出した後の抽出残渣物（外観がクリーム色から黄色を呈し、乾燥すると黄褐色から茶褐色）を原料にして蛋白分解酵素（酸性プロテアーゼ）を作用させた後、活性炭で脱色することで殆んど白色に近い低分子コラーゲンを高収率で得る製造方法を見いだし、本発明を完成させるに至った。
即ち、本発明は、
Accordingly, as a result of various investigations to solve the above problems, the present inventors have used, as a raw material, an extraction residue obtained by boiling and extracting collagen from fish scales (appearance is cream to yellow, and yellow to brown when dried) Thus, the present inventors have completed the present invention by finding a production method for obtaining a low molecular weight collagen almost white in high yield by decolorizing with activated carbon after acting a protease (acidic protease).
That is, the present invention
（１）魚鱗を脱灰処理し、次いで９０〜１００℃の熱水中にてコラーゲンを煮沸抽出した抽出残渣物を原料にして、蛋白質分解酵素である酸性プロテアーゼを作用させた後、活性炭で脱色することを特徴とする低分子コラーゲンの製造方法、
（２）蛋白質分解酵素を作用させるｐＨが２〜６の酸性域である前項（１）記載の低分子コラーゲンの製造方法、
（３）抽出残渣物からの製造収率が８０％以上である前項（１）又は（２）記載の低分子コラーゲンの製造方法、
（４）抽出残渣物が粒子径５００μｍ以下の乾燥粉砕物である前項（１）ないし（３）のいずれか一項に記載の低分子コラーゲンの製造方法、
（５）製造された低分子コラーゲンの平均分子量が３０００以下である前項（１）ないし（４）のいずれか一項に記載の低分子コラーゲンの製造方法、
に関する。
(1) Decalcification of fish scales, followed by extraction residue obtained by boiling and extracting collagen in hot water at 90 to 100 ° C., using an acidic protease that is a proteolytic enzyme, followed by decolorization with activated carbon A method for producing low molecular weight collagen,
(2) The method for producing low molecular weight collagen according to (1) above, wherein the pH at which the proteolytic enzyme acts is an acidic range of 2 to 6,
(3) The method for producing low-molecular collagen according to (1) or (2) above, wherein the production yield from the extraction residue is 80% or more,
(4) The method for producing low molecular collagen according to any one of (1) to (3) above, wherein the extraction residue is a dry pulverized product having a particle size of 500 μm or less,
(5) The method for producing a low molecular collagen according to any one of (1) to (4), wherein the average molecular weight of the produced low molecular collagen is 3000 or less,
About.
本発明の製造方法により、魚鱗からコラーゲンを煮沸抽出した残渣物を原料にすることにより、産業廃棄物が減少して環境汚染防止に役立つ。また、煮沸残渣物から８０％以上の高収率で低分子コラーゲンの製造が可能となるため、安価な低分子コラーゲンが得られる。 By using the residue obtained by boiling and extracting collagen from fish scales as a raw material by the production method of the present invention, industrial waste is reduced, which helps to prevent environmental pollution. Moreover, since low molecular collagen can be produced from the boiling residue with a high yield of 80% or more, inexpensive low molecular collagen can be obtained.
本発明の低分子コラーゲンの製造方法は、魚鱗を脱灰処理し、次いで９０〜１００℃の熱水中にてコラーゲンを煮沸抽出した抽出残渣物を原料にして、蛋白質分解酵素である酸性プロテアーゼを作用させた後、活性炭で脱色することを特徴とする低分子コラーゲンの製造方法である。
本発明において「低分子コラーゲン」とは、コラーゲン由来の低分子コラーゲンとコラーゲンペプタイドの混合物をあらわす。本願発明の製造方法で得られる「低分子コラーゲン」は、平均分子量が３０００以下で分子量分布の範囲が５０００〜５００の低分子コラーゲンと、平均分子量５００〜２００のコラーゲンペプタイドを含有する。
The method for producing low molecular weight collagen according to the present invention comprises demineralizing fish scales, and then using an extraction residue obtained by boiling and extracting collagen in hot water at 90 to 100 ° C. as a raw material to produce an acidic protease that is a proteolytic enzyme. It is a method for producing low molecular weight collagen, which is decolorized with activated carbon after acting.
In the present invention, “low molecular collagen” refers to a mixture of low molecular collagen derived from collagen and a collagen peptide. The “low molecular collagen” obtained by the production method of the present invention contains low molecular collagen having an average molecular weight of 3000 or less and a molecular weight distribution range of 5000 to 500 and a collagen peptide having an average molecular weight of 500 to 200.
本願発明において、魚鱗の脱灰（カルシウム除去）方法としては、例えば、魚鱗を約２０〜３０倍量の水に浸漬した後、魚鱗含有カルシウムの１．２〜１．５倍量相当分の塩酸を加えて１０〜３０分間撹拌して、塩化カルシウム水溶液として除去する。その後、繰り返し水洗を行なって酸分を洗い流して脱灰鱗とすることで差し支えない。また、酸処理時間が長いと有効成分のコラーゲンが溶出してくるので短時間で脱灰処理を行うことが好ましい。 In the present invention, as a method for demineralizing (calcium removing) fish scales, for example, after immersing fish scales in about 20 to 30 times the amount of water, hydrochloric acid corresponding to 1.2 to 1.5 times the amount of fish scale-containing calcium And stirred for 10-30 minutes to remove as an aqueous calcium chloride solution. Thereafter, washing with water repeatedly may be performed to wash away the acid content to obtain decalcified scale. In addition, when the acid treatment time is long, the active ingredient collagen is eluted, so it is preferable to perform the decalcification treatment in a short time.
本願発明において、コラーゲンの煮沸抽出方法としては、例えば、脱灰鱗を約２０〜３０倍量の沸騰水に投入してガスや水蒸気で数時間煮込んで抽出すればよく、熱水中の温度は約９０〜１００℃に保たれる。次いで得られた抽出物を冷却するとニコゴリ状のコラーゲン寒天が得られる。 In the present invention, as a method for boiling extraction of collagen, for example, demineralized scale may be poured into boiling water of about 20 to 30 times and extracted by boiling with gas or steam for several hours. It is kept at about 90-100 ° C. Next, when the obtained extract is cooled, a collagenous agar in the form of nicogot is obtained.
本発明ではコラーゲンを煮沸抽出して残った残渣物を原料として使用する。
従来、廃棄されていた煮沸残渣物に分子量３０００以下まで分解できるプロテアーゼなどの蛋白分解酵素を最適ｐＨで作用させて低分子化し、分解溶液を活性炭で脱色及び脱臭して濾過し、脱塩して低分子コラーゲン溶液を得た後、最適濃度に濃縮しスプレードライヤーなどで粉末化して低分子コラーゲン粉末を得る。あるいは、煮沸残渣物を含水率１０％以下まで乾燥させて、５００μｍ以下に微粉砕した後、上記同様の操作を行って低分子コラーゲン粉末を得る方法でもよい。
In the present invention, a residue remaining after boiling and extracting collagen is used as a raw material.
Conventionally, proteases such as proteases that can be decomposed to a boiling weight residue of 3000 or less are allowed to act at an optimum pH to lower the molecular weight, and the decomposition solution is decolorized and deodorized with activated carbon, filtered, and desalted. After obtaining a low molecular weight collagen solution, it is concentrated to an optimum concentration and powdered with a spray dryer or the like to obtain a low molecular weight collagen powder. Alternatively, the boiling residue may be dried to a moisture content of 10% or less and finely pulverized to 500 μm or less, and then the same operation as described above may be performed to obtain a low molecular collagen powder.
本発明の製造に用いられる魚鱗の由来としては、淡水魚、海水魚などの魚類の鱗であれば何れでも良く、一般的にはテラピア（イズミダイ）、イトヨリダイ、ナウルパウチ（チカダイ）、真鯛、イワシなどの魚鱗が挙げられる。 The origin of the fish scales used in the production of the present invention may be any scale of fish such as freshwater fish and saltwater fish. Examples include fish scales.
本発明の製造方法で用いられる原料の残渣物は、魚鱗由来であれば何れでもよく、残渣物から８０％以上、脱灰鱗から換算して６０％以上、乾燥鱗から換算して５０％以上の高収率で低分子コラーゲンが得られる。 The raw material residue used in the production method of the present invention may be any as long as it is derived from fish scales, 80% or more from the residue, 60% or more converted from decalcified scale, and 50% or more converted from dry scale. A low molecular weight collagen can be obtained with a high yield of
本発明の製造で用いられるコラーゲンを煮沸抽出した後の抽出残渣物の分子量は、熱水に溶解しない高分子であれば何れでもよく、１０万以上の高分子コラーゲンと推察される。
本発明の製造で用いられるコラーゲンを煮沸抽出した後の抽出残渣物は、例えば表１に示した通り、ヒドロキシプロリン、グリシン、プロリンなどのアミノ酸組成から高分子コラーゲンの組成を有している。また、残渣の乾燥物は、コラーゲン特有の三重螺旋構造が弱くなり微粉砕も容易となる。
The molecular weight of the extracted residue after boiling and extracting the collagen used in the production of the present invention may be any polymer that does not dissolve in hot water, and is estimated to be 100,000 or more polymer collagen.
The extraction residue after boiling and extracting the collagen used in the production of the present invention has a composition of high molecular collagen from amino acid composition such as hydroxyproline, glycine, and proline as shown in Table 1, for example. Further, the dried residue is weak in the triple helix structure peculiar to collagen and is easily pulverized.
表１．煮沸抽出残渣物のアミノ酸分析結果（ナウルパウチ）
アミノ酸組成名 含有率（％） アミノ酸組成名 含有率（％）
アルギニン ６．４６ リジン ３．１０
ヒスチジン ２．１８ フェニルアラニン ２．２６
チロシン １．７２ ロイシン ３．２２
イソロイシン ２．７１ メチオニン １．８０
バリン ２．８０ アラニン ８．５３
グリシン ２１．８ プロリン １１．６
グルタミン酸 １０．８ セリン ３．９６
スレオニン ３．２５ アスパラギン酸 ５．７９
トリプトファン ０．０６ シスチン ０．３２
ヒドロキシプロリン １０．９
Table 1. Amino acid analysis result of boiling extract residue (Nauru pouch)
Amino acid composition name Content rate (%) Amino acid composition name Content rate (%)
Arginine 6.46 Lysine 3.10
Histidine 2.18 Phenylalanine 2.26
Tyrosine 1.72 Leucine 3.22
Isoleucine 2.71 Methionine 1.80
Valine 2.80 Alanine 8.53
Glycine 21.8 Proline 11.6
Glutamic acid 10.8 Serine 3.96
Threonine 3.25 Aspartic acid 5.79
Tryptophan 0.06 Cystine 0.32
Hydroxyproline 10.9
本発明の製造で用いられる原料の残渣物は、粉砕してもしなくてもよいが、蛋白分解酵素との接触面積が大きい方がよく、粉砕して粒子径５００μｍ以下が好ましく、微粉砕して粒子径１００μｍ以下がより好ましい。また、粒子径の下限は通常１０μｍ程度である。 The raw material residue used in the production of the present invention may or may not be pulverized, but it should have a large contact area with the proteolytic enzyme, and is preferably pulverized to have a particle diameter of 500 μm or less. A particle size of 100 μm or less is more preferable. The lower limit of the particle diameter is usually about 10 μm.
本発明で用いられる蛋白分解酵素である酸性プロテアーゼは、高分子コラーゲンを低分子化できるものであり、アミノ酸単体まで分解しないものが好ましく、最適ｐＨが２〜６で活性の高い蛋白分解酵素が好ましい。蛋白分解酵素としては、ニューラーゼ，Ｆ３Ｇ（天野エンザイム）、モルシンＦ（キッコーマン）、プロテアーゼＭ（天野エンザイム）、プロテアーゼＹＰ−ＳＳ（ヤクルト薬品工業）、パパインＷ−４０（天野エンザイム）などの酸性プロテアーゼが挙げられる。 The acidic protease, which is a proteolytic enzyme used in the present invention, can reduce the molecular weight of high molecular collagen, preferably does not degrade amino acids alone, and is preferably a proteolytic enzyme having an optimum pH of 2 to 6 and high activity. . As proteases, acidic proteases such as Newase, F3G (Amano Enzyme), Morsine F (Kikkoman), Protease M (Amano Enzyme), Protease YP-SS (Yakult Pharmaceutical Co., Ltd.), Papain W-40 (Amano Enzyme) Is mentioned.
本発明で用いる活性炭処理による脱色方法としては、酵素で低分子化して酵素失活させた分解溶液に活性炭を加え、通常４０〜８０℃で０．５〜３時間程度撹拌して脱色し、葉状濾過機などで活性炭を分離する。活性炭の添加量としては、活性炭の吸着能力によっても異なるが含有蛋白質量に対して重量比で通常２〜６０％、好ましくは５〜３０％、より好ましくは５〜２０％程度がよい。使用する活性炭としては、如何なるメーカーの如何なるグレードでもよいが、食品に使用可能で脱色力のあるものであれば何れでもよい。活性炭の粒子径は、小さい方がよく、１５０メッシュ以下の表面積の大きい粉末活性炭がよい。また、飛散が少なく容易に分散できるＷｅｔの活性炭が好ましい。 As a decolorization method by the activated carbon treatment used in the present invention, activated carbon is added to a decomposition solution that has been deactivated with an enzyme to deactivate the enzyme, and is usually decolored by stirring at 40 to 80 ° C. for about 0.5 to 3 hours. Separate the activated carbon with a filter. The addition amount of the activated carbon is usually 2 to 60%, preferably 5 to 30%, more preferably about 5 to 20% by weight with respect to the amount of protein contained, although it varies depending on the adsorption ability of the activated carbon. The activated carbon to be used may be any grade from any manufacturer, but may be any as long as it can be used for food and has a decolorizing power. The particle diameter of the activated carbon is preferably small, and powdered activated carbon having a large surface area of 150 mesh or less is preferable. Further, Wet activated carbon that can be easily dispersed with little scattering is preferable.
本発明の分子量測定は、プルランを分子量標準として示差屈折計を検出器としたＧＰＣ分析装置で測定する方法を用いた。また、コラーゲン含量の測定は、ケルダール法による窒素含量より算出した蛋白量をコラーゲン量として置き換えた。
アミノ酸の成分分析値は、外部機関によるアミノ酸自動分析計の測定値を採用した。
The molecular weight measurement of the present invention used a method of measuring with a GPC analyzer using pullulan as a molecular weight standard and a differential refractometer as a detector. The collagen content was measured by replacing the amount of protein calculated from the nitrogen content by the Kjeldahl method with the amount of collagen.
The amino acid component analysis value was measured by an automatic amino acid analyzer measured by an external organization.
本発明の低分子コラーゲンは、低分子化することにより体内への吸収性が高い。
本発明の低分子コラーゲンは、例えば、切傷や火傷などの皮膚の損傷治療、美容整形、美肌用化粧品、ハンドクリームなどに添加して使用することが出来、また、健康食品として粉末や錠剤として直接摂取して体内コラーゲンの栄養補給剤として使用することが出来る。
The low molecular collagen of the present invention is highly absorbable into the body by reducing the molecular weight.
The low molecular collagen of the present invention can be used, for example, by adding to skin damage treatment such as cuts and burns, cosmetic surgery, cosmetics for skin care, hand cream, etc., and as a health food directly as a powder or a tablet. Ingested and can be used as a nutritional supplement for body collagen.
以下に実施例を挙げて本発明を具体的に説明するが、本発明はこれらに限定されるものではない。 EXAMPLES The present invention will be specifically described below with reference to examples, but the present invention is not limited to these examples.
実施例１
イワシの鱗１．８ｋｇを５Ｌの水道水に浸漬して一夜放置した後、濃塩酸１．８Ｌを加えて１０分間撹拌して脱灰し、５Ｌの水道水で５回洗浄した。脱灰鱗に５Ｌの水道水を加えて分散した後、生蒸気を導入して９８〜１００℃で４時間煮沸してコラーゲンを熱水抽出した。抽出コラーゲンと残渣物を分離し、原料となる残渣物を取り出した。残渣物（乾燥物換算１ｋｇ）に、水道水３Ｌを加えて撹拌分散してｐＨ４に調整して５０℃に加温した後、蛋白分解酵素のプロテアーゼＭ（アマノエンザイム製）６０ｇを投入して５時間撹拌した。次に、９５〜１００℃に昇温し１時間撹拌保持して酵素を失活させ、６０℃に冷却後活性炭１００ｇを加えて１時間撹拌してカーボン脱色し、濾過、濃縮を行った後、凍結乾燥して、本発明の低分子コラーゲン９１０ｇを得た。得られた低分子コラーゲンの平均分子量は１２００であった。
Example 1
After 1.8 kg of sardine scales were immersed in 5 L of tap water and left overnight, 1.8 L of concentrated hydrochloric acid was added, stirred for 10 minutes to deash, and washed 5 times with 5 L of tap water. After adding 5 L of tap water to the decalcified scale and dispersing, live steam was introduced and boiled at 98-100 ° C. for 4 hours to extract collagen from hot water. The extracted collagen and the residue were separated, and the residue as a raw material was taken out. To the residue (1 kg in terms of dry matter), 3 L of tap water was added and dispersed by stirring, adjusted to pH 4, heated to 50 ° C., and then charged with 60 g of protease M protease (manufactured by Amano Enzyme). Stir for hours. Next, the temperature was raised to 95 to 100 ° C., and the enzyme was deactivated by stirring for 1 hour. After cooling to 60 ° C., 100 g of activated carbon was added, and the mixture was stirred for 1 hour to decolorize carbon, filtered and concentrated. It was lyophilized to obtain 910 g of low molecular collagen of the present invention. The average molecular weight of the obtained low molecular collagen was 1200.
実施例２
ナウルパウチ鱗３５ｋｇを実施例１と同様の方法で脱灰、熱水抽出を経て残渣物を取り出して乾燥、粉砕し５００μｍの網を通過した残渣粉末２０ｋｇを得た。 水道水３００Ｌを加えて撹拌分散してｐＨ３．５に調整して６０℃に加温した後、蛋白分解酵素のパパインＷ−４０（アマノエンザイム製）０．７ｋｇを投入して５時間撹拌した。次に、９５℃〜１００℃に昇温し１時間撹拌保持して酵素を失活させ、６０℃に冷却後に５０％Ｗｅｔの活性炭１０ｋｇを加えて１時間撹拌してカーボン脱色し、濾過、脱塩、濃縮を行った後、スプレードライヤーにかけて、本発明の低分子コラーゲン１８．５ｋｇを得た。得られた混合物の平均分子量は６００であった。また、アミノ酸分析の結果は表２の結果が得られた。
Example 2
Nauru pouch scale 35 kg was decalcified in the same manner as in Example 1, extracted with hot water, dried, pulverized, and crushed to obtain 20 kg of residual powder passing through a 500 μm net. After adding 300 L of tap water and stirring and dispersing to adjust to pH 3.5 and heating to 60 ° C., 0.7 kg of proteolytic enzyme papain W-40 (manufactured by Amano Enzyme) was added and stirred for 5 hours. Next, the temperature is raised to 95 ° C. to 100 ° C. and stirred for 1 hour to inactivate the enzyme. After salting and concentration, it was applied to a spray dryer to obtain 18.5 kg of the low molecular weight collagen of the present invention. The average molecular weight of the obtained mixture was 600. The results of amino acid analysis were as shown in Table 2.
表２．低分子コラーゲンのアミノ酸分析結果
アミノ酸組成名 含有率（％） アミノ酸組成名 含有率（％）
アルギニン ７．０７ リジン ３．０１
ヒスチジン １．８３ フェニルアラニン ２．４３
チロシン １．４５ ロイシン ２．９３
イソロイシン １．７７ メチオニン １．９２
バリン ２．７５ アラニン ９．１５
グリシン ２２．６ プロリン １２．４
グルタミン酸 １０．１ セリン ３．７１
スレオニン ３．１９ アスパラギン酸 ５．３２
トリプトファン ０．０４ シスチン ０．２３
ヒドロキシプロリン １０．７
Table 2. Amino acid analysis result of low molecular weight collagen Amino acid composition name Content rate (%) Amino acid composition name Content rate (%)
Arginine 7.07 Lysine 3.01
Histidine 1.83 Phenylalanine 2.43
Tyrosine 1.45 leucine 2.93
Isoleucine 1.77 methionine 1.92
Valine 2.75 Alanine 9.15
Glycine 22.6 Proline 12.4
Glutamic acid 10.1 Serine 3.71
Threonine 3.19 Aspartic acid 5.32
Tryptophan 0.04 Cystine 0.23
Hydroxyproline 10.7
実施例３
テラピアの脱灰乾燥鱗１．４ｋｇをガスコンロにかけコラーゲンを煮沸抽出し、抽出コラーゲンと残渣物を分離し、残渣物を乾燥、粉砕して１８０μｍの網を通過した残渣粉末１ｋｇを得た。水道水３Ｌを加えて撹拌分散してｐＨ４に調整し５０℃に加温した後、蛋白分解酵素のプロテアーゼＭ（アマノエンザイム製）５０ｇを投入して２時間撹拌した。次に、９５〜１００℃に昇温し１時間保持して酵素を失活させ、６０℃に冷却後活性炭１００ｇを加えて１時間撹拌してカーボン脱色し、濾過、脱塩、濃縮を行った後、スプレードライヤーにかけて、本発明の低分子コラーゲン０．９ｋｇを得た。得られた低分子コラーゲンの平均分子量は１４００であった。
Example 3
By applying 1.4 kg of tilapia demineralized dry scale to a gas stove, the collagen was boiled and extracted, the extracted collagen and the residue were separated, and the residue was dried and pulverized to obtain 1 kg of a residue powder that passed through a 180 μm net. 3 L of tap water was added and dispersed by stirring, adjusted to pH 4 and heated to 50 ° C., and then 50 g of protease M (manufactured by Amano Enzyme), a protease, was added and stirred for 2 hours. Next, the temperature was raised to 95 to 100 ° C. and held for 1 hour to deactivate the enzyme. After cooling to 60 ° C., 100 g of activated carbon was added and stirred for 1 hour to decolorize carbon, followed by filtration, desalting and concentration. Thereafter, it was applied to a spray dryer to obtain 0.9 kg of low molecular collagen of the present invention. The average molecular weight of the obtained low molecular collagen was 1400.
試験例１
被験者９名を（Ａコラーゲン未摂取、Ｂ高分子コラーゲン３ｇ／日、Ｃ実施例１で得られた本発明の低分子コラーゲン３ｇ／日）各々３名ずつの３群に分けて２週間摂取試験を行った結果、頬の肌荒れについてＡ群には改善が見られず、Ｂ群は２名に改善が見られ、Ｃ群は３名全てに改善が見られた。本発明の低分子コラーゲンは肌荒れの改善において有効であった。
Test example 1
Nine test subjects (A collagen not taken, B high molecular collagen 3 g / day, low molecular collagen of the present invention obtained in Example 1 3 g / day) divided into 3 groups of 3 each for 2 weeks intake test As a result, no improvement was observed in the group A with respect to the rough skin of the cheeks. The low molecular weight collagen of the present invention was effective in improving rough skin.
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2010125910A1 (en) * | 2009-04-28 | 2010-11-04 | 明治製菓株式会社 | Collagen peptide composition having good blood transfer properties, and food and drink containing same |
| CN105030586A (en) * | 2015-07-07 | 2015-11-11 | 海南海润生物科技股份有限公司 | Whitening spot-fading cosmetic containing marine active peptide and preparation method thereof |
| US9873407B2 (en) | 2013-12-13 | 2018-01-23 | Semcon Sweden Ab | Automatic removal of water from vehicle surfaces |
| CN114933648A (en) * | 2022-06-22 | 2022-08-23 | 山东恒鑫生物科技有限公司 | Method for producing collagen dipeptide from fish scales |
| CN115594731A (en) * | 2022-10-31 | 2023-01-13 | 南通紫琅生物医药科技有限公司（Cn） | Glutathione decoloring processing technology |
| KR102560599B1 (en) * | 2022-08-24 | 2023-07-27 | 강경훈 | Manufacturing method of functional feed using waste-treated livestock by-products as raw materials |
Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH11266803A (en) * | 1998-03-20 | 1999-10-05 | Yozo Ishizuka | Production of softened product of hard collagen obtained from scale of fish, and its utilization for food |
| JP2004250421A (en) * | 2003-02-20 | 2004-09-09 | Eco Tech Co Ltd | Cosmetic |
| JP2006000089A (en) * | 2004-06-21 | 2006-01-05 | Jellice Co Ltd | Method for producing collagen peptide from fish scale |
| JP2006151847A (en) * | 2004-11-26 | 2006-06-15 | Nitta Gelatin Inc | Collagen peptide composition, method for producing the same and cosmetic composition |
| JP2006217876A (en) * | 2005-02-14 | 2006-08-24 | Chisso Corp | Method for producing gelatin or collagen peptide derived from fish scale |
| JP2006257014A (en) * | 2005-03-16 | 2006-09-28 | National Institute For Materials Science | Collagen derived from scale and method for obtaining the same collagen |
| JP2006342107A (en) * | 2005-06-09 | 2006-12-21 | Nitta Gelatin Inc | Cosmetic composition containing collagen peptide and method for producing the same |
-
2007
- 2007-03-09 JP JP2007060006A patent/JP2008220208A/en active Pending
Patent Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH11266803A (en) * | 1998-03-20 | 1999-10-05 | Yozo Ishizuka | Production of softened product of hard collagen obtained from scale of fish, and its utilization for food |
| JP2004250421A (en) * | 2003-02-20 | 2004-09-09 | Eco Tech Co Ltd | Cosmetic |
| JP2006000089A (en) * | 2004-06-21 | 2006-01-05 | Jellice Co Ltd | Method for producing collagen peptide from fish scale |
| JP2006151847A (en) * | 2004-11-26 | 2006-06-15 | Nitta Gelatin Inc | Collagen peptide composition, method for producing the same and cosmetic composition |
| JP2006217876A (en) * | 2005-02-14 | 2006-08-24 | Chisso Corp | Method for producing gelatin or collagen peptide derived from fish scale |
| JP2006257014A (en) * | 2005-03-16 | 2006-09-28 | National Institute For Materials Science | Collagen derived from scale and method for obtaining the same collagen |
| JP2006342107A (en) * | 2005-06-09 | 2006-12-21 | Nitta Gelatin Inc | Cosmetic composition containing collagen peptide and method for producing the same |
Cited By (14)
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| US20120040055A1 (en) * | 2009-04-28 | 2012-02-16 | Meiji Co., Ltd. | Collagen peptide composition having good ability to enter the blood and food or beverage containing the same |
| CN102428094A (en) * | 2009-04-28 | 2012-04-25 | 株式会社明治 | Collagen peptide composition having good blood transfer properties, and food and drink containing same |
| JPWO2010125910A1 (en) * | 2009-04-28 | 2012-10-25 | 株式会社明治 | Collagen peptide composition having high blood transferability and food and drink containing the same |
| KR101382758B1 (en) * | 2009-04-28 | 2014-04-08 | 가부시키가이샤 메이지 | Collagen peptide composition having good blood transfer properties, and food and drink containing same |
| CN102428094B (en) * | 2009-04-28 | 2015-07-22 | 株式会社明治 | Collagen peptide composition having good blood transfer properties, and food and drink containing same |
| WO2010125910A1 (en) * | 2009-04-28 | 2010-11-04 | 明治製菓株式会社 | Collagen peptide composition having good blood transfer properties, and food and drink containing same |
| JP5890175B2 (en) * | 2009-04-28 | 2016-03-22 | 株式会社明治 | Collagen peptide composition having high blood transferability and food and drink containing the same |
| US9873407B2 (en) | 2013-12-13 | 2018-01-23 | Semcon Sweden Ab | Automatic removal of water from vehicle surfaces |
| CN105030586A (en) * | 2015-07-07 | 2015-11-11 | 海南海润生物科技股份有限公司 | Whitening spot-fading cosmetic containing marine active peptide and preparation method thereof |
| CN114933648A (en) * | 2022-06-22 | 2022-08-23 | 山东恒鑫生物科技有限公司 | Method for producing collagen dipeptide from fish scales |
| CN114933648B (en) * | 2022-06-22 | 2023-09-08 | 山东恒鑫生物科技有限公司 | Method for producing collagen dipeptide from fish scales |
| KR102560599B1 (en) * | 2022-08-24 | 2023-07-27 | 강경훈 | Manufacturing method of functional feed using waste-treated livestock by-products as raw materials |
| CN115594731A (en) * | 2022-10-31 | 2023-01-13 | 南通紫琅生物医药科技有限公司（Cn） | Glutathione decoloring processing technology |
| CN115594731B (en) * | 2022-10-31 | 2023-09-08 | 南通紫琅生物医药科技有限公司 | Glutathione decoloring processing technology |
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