JP3720324B2 - Method for producing mild water-soluble collagen - Google Patents
Method for producing mild water-soluble collagen Download PDFInfo
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- JP3720324B2 JP3720324B2 JP2002354015A JP2002354015A JP3720324B2 JP 3720324 B2 JP3720324 B2 JP 3720324B2 JP 2002354015 A JP2002354015 A JP 2002354015A JP 2002354015 A JP2002354015 A JP 2002354015A JP 3720324 B2 JP3720324 B2 JP 3720324B2
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- 102000008186 Collagen Human genes 0.000 title claims description 63
- 108010035532 Collagen Proteins 0.000 title claims description 63
- 229920001436 collagen Polymers 0.000 title claims description 63
- 238000004519 manufacturing process Methods 0.000 title claims description 15
- 102000004190 Enzymes Human genes 0.000 claims description 27
- 108090000790 Enzymes Proteins 0.000 claims description 27
- 239000000126 substance Substances 0.000 claims description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 9
- 241000894006 Bacteria Species 0.000 claims description 6
- 102000004157 Hydrolases Human genes 0.000 claims description 6
- 108090000604 Hydrolases Proteins 0.000 claims description 6
- 238000001035 drying Methods 0.000 claims description 4
- 235000015277 pork Nutrition 0.000 claims description 4
- 102000035195 Peptidases Human genes 0.000 claims description 3
- 108091005804 Peptidases Proteins 0.000 claims description 3
- 238000001914 filtration Methods 0.000 claims description 3
- 230000001954 sterilising effect Effects 0.000 claims description 3
- 241000194108 Bacillus licheniformis Species 0.000 claims description 2
- 241000193830 Bacillus <bacterium> Species 0.000 claims 1
- 238000000034 method Methods 0.000 description 19
- 239000002994 raw material Substances 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 238000010306 acid treatment Methods 0.000 description 8
- 238000005406 washing Methods 0.000 description 7
- 238000011033 desalting Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 238000000746 purification Methods 0.000 description 4
- 230000037319 collagen production Effects 0.000 description 3
- 230000000052 comparative effect Effects 0.000 description 3
- 238000007796 conventional method Methods 0.000 description 3
- 229910001385 heavy metal Inorganic materials 0.000 description 3
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 150000007522 mineralic acids Chemical class 0.000 description 2
- 230000000704 physical effect Effects 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 238000004659 sterilization and disinfection Methods 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 101710118538 Protease Proteins 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 235000015872 dietary supplement Nutrition 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 239000003344 environmental pollutant Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 235000020510 functional beverage Nutrition 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002203 pretreatment Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 235000021067 refined food Nutrition 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 239000002351 wastewater Substances 0.000 description 1
Images
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
- A23J3/342—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of collagen; of gelatin
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/10—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from hair, feathers, horn, skins, leather, bones, or the like
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/04—Animal proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2250/00—Food ingredients
- A23V2250/54—Proteins
- A23V2250/542—Animal Protein
- A23V2250/5422—Collagen
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2300/00—Processes
- A23V2300/28—Hydrolysis, degree of hydrolysis
Description
【0001】
【発明が属する技術分野】
本発明は、マイルドな水溶性コラーゲンの製造方法に関し、より詳細には豚皮を酵素処理して低分子化することによって、薬品処理及び脱塩処理を行わないマイルドな水溶性コラーゲンを製造することができる方法に関する。
【0002】
【従来の技術】
従来、一般的なコラーゲンの製造方法は、大別して原料選別工程、原料の前処理工程、抽出工程、抽出物を利用した水溶性コラーゲン製造工程及び精製工程で構成されている。より具体的に説明すると、選別された豚皮(pig skin)を前処理工程で酸処理を行った後、抽出を容易にするために過量投入された薬品を多量の水で洗浄する工程を経る。洗浄工程を経た豚皮からコラーゲンを抽出し、この抽出物を利用して水溶性コラーゲンを製造した後、純度を高めるための精製工程として脱塩処理工程を行うことによって、水溶性コラーゲンを製造することになる(例えば、図2の工程フローチャート参照)。従って、従来の豚皮からコラーゲンを製造する方法は、前処理工程及び洗浄工程から発生する廃水の処理のための付加的装置が要求され、 酸処理の際に使用される毒性が強い無機酸を除去する別途の脱塩工程を必要とするため、全体の製造工程が複雑であり、多段階の工程を経ることによって、収得効率も低下する(例えば、特許文献1および2参照)。
【0003】
従って、薬品処理や重金属処理を含む複雑な製造工程を単純化することができる水溶性コラーゲンの製造方法が強く要望されている。
【0004】
【特許文献1】
特開昭61−135584号公報
【特許文献2】
特開平13−061474号公報
【0005】
【発明が解決しようとする課題】
本発明は、前記従来技術の問題点を解決するために案出されたものであり、原料物質である豚皮を酸処理工程、及びこれに従う洗浄工程等の中間処理工程を経ることなしに、より単純化された工程で水溶性コラーゲンを製造することができる方法を提供することを目的とする。
【0006】
【課題を解決するための手段】
前記目的を達成するための本発明によるマイルドな水溶性コラーゲンの製造方法は、豚皮をチョッピングして原料コラーゲンを製造する工程、前記原料コラーゲンに、水を質量で70:30乃至50:50の割合で混合した後、前記原料コラーゲンに対し0.1〜1%(質量百分率)の第1蛋白質加水分解酵素を添加して55〜70℃で処理する第1酵素処理工程、前記第1酵素処理工程で処理されたコラーゲン溶液に、前記原料コラーゲンに対し0.1〜0.5%(質量百分率)の第2蛋白質加水分解酵素を添加して45〜55℃で処理する第2酵素処理工程及び、前記第2酵素処理工程で処理されたコラーゲン溶液を瀘過して異物質を除去した後、真空濃縮、殺菌及び乾燥を行う工程を含むことを特徴とする。
【0007】
前記第1蛋白質加水分解酵素と第2蛋白質加水分解酵素は、すべて前記原料コラーゲンを低分子化するための酵素として、それぞれリケニホルミス菌(Bacillus licheniformis)とアミロクエファシエム菌(Bacillus amyloquefaciems)を使用する。
【0008】
なお、前記第1酵素処理工程と第2酵素処理工程は、各々の酵素が最適の活動を示現することができるpHに調節した後に処理することがより好ましく、各々pH6.5〜8.5とpH5.5〜7.5に調節し、この範囲の最適pHに保持しながら処理することが好ましい。
【0009】
そして、前記第2酵素処理工程で処理されたコラーゲンの分子量は1,000〜2,000であることが好ましい。
【0010】
【発明の実施形態】
以下、本発明をより詳細に説明する。
本発明は、原料物質である豚皮を一定の温度及びpH件下で特定酵素処理を行って分子量1,000〜2,000程度の低分子物質に転換させることによって、酸処理やそれに伴う洗浄工程及び脱塩工程を経ることなしに、簡単な工程で人体の吸収が速いマイルドな水溶性コラーゲンを得ることに特徴がある。
【0011】
本発明の原料物質である豚皮は、冷凍又は冷蔵処理されたものであり、異物質を除去した後、破碎器に入れチョッピングすることによって原料コラーゲンとして使用される。
【0012】
前記チョッピングされた原料コラーゲンに、水を質量で70:30〜50:50の割合で均一に混合した後、特定蛋白質加水分解酵素を使用する酵素処理工法を利用して、コラーゲン内の親水性が強い成分を抜き取ることによって、水溶性コラーゲンを製造することができる。前記蛋白質加水分解酵素は、コラーゲンを体内吸収が速い分子量である1,000〜2,000程度の範囲を有するように低分子化することができ、何よりも毒性が強い無機酸の使用を最小化するために、pHが中性範囲で最適の活性を示すもので、好ましくは第1蛋白質加水分解酵素としてリケニホルミス菌の選択された系統の水中発酵によって生産された酵素を使用することができ、第2蛋白質加水分解酵素としてアミロクエファシエム菌の選択チェーンによって生産されるバクテリア的酵素で、特にエンド-プロテアーゼ(endo-protease)が使用されることができる。この時、リケニホルミス菌酵素は、pH6.5〜8.5、温度55〜70℃で最適の活動を示し、前記アミロクエファシエム菌は、pH5.5〜7.5、温度45〜55℃で蛋白質の加水分解が最も活発に生じるため、前記コラーゲン溶液のpHを各々の最適条件に合致するように調節しながら処理することが好ましい。
【0013】
前記酵素処理は、コラーゲンの分子量が約1,000〜2,000程度になれば、コラーゲン溶液の温度を85℃程度に急激に上昇させて、残余の酵素を失活させることによって終了するが、この時の分子量は、反応器の側面に粘性計を付着してコラーゲンの粘性度を測定することによって確認することができる。
【0014】
本発明では前記酵素処理されたコラーゲン溶液を遠心分離器を利用して異物質を除去した後、濾過したコラーゲン溶液を真空濃縮管を利用して濃度40%(質量百分率)程度まで濃縮し、殺菌処理及び乾燥させることによって、マイルドなコラーゲン粉末製品を完成する。
【0015】
【実施例】
以下、実施例によって本発明をより詳細に説明する。しかし、本発明が以下の例示に限定されるものではない。
【0016】
[実施例]
冷蔵処理された豚皮を破碎器でチョッピングして、原料コラーゲンを製造した後、水と前記コラーゲンを質量で30:70の割合で均一に混合し、その後、前記コラーゲン溶液のpHを7.5に調整しながらコラーゲン対比0.4%(質量百分率)のリケニホルミス菌を添加し60℃で4時間の間処理した。処理された前記コラーゲン溶液を再びpH6.5に調整しながらアミロクエファシエム菌をコラーゲン対比0.2%(質量百分率)添加し、45℃で2時間の間酵素処理しながらコラーゲンの粘度測定を通じて分子量が1,000程度になれば、温度を85℃に急激に上昇させ、余分の酵素を失活させて反応を終結した。酵素処理されたコラーゲン抽出物を遠心分離器によって異物質を除去した後、フィルタープレス濾紙フィルターを使用して濾過し、その後、濃度40%(質量百分率)まで真空濃縮した。 濃縮されたコラーゲンをUHT TYPT殺菌器を利用して121℃で0.8秒間連続的に瞬間殺菌した後、スプレードライヤーを利用して乾燥し、品質検査を実施した後、滅菌包装して望むマイルドな水溶性コラーゲンを製造した(図1の工程フローチャート参照)。
【0017】
[比較例]
豚皮を2x5cmのサイズに切断して、1.1%硫酸水溶液が盛られた原料処理タンクで60時間の間処理した後、前記原料豚皮の約10倍の洗浄水で12時間の間洗浄した。前記酸処理及び洗浄工程を経た原料物質に、水を入れ湯煎でそれぞれ55℃、65℃、80℃の温度で3回にかけて抽出し原料コラーゲンを得た後、この原料コラーゲンにBタイプの酵素(ペプシン(pepsine))を添加し2時間の間処理し、パルプ瀘過器を使用して濾過した後、2時間の間、陽イオン塔と陰イオン塔を通過させて脱塩精製した。以後、脱塩されたコラーゲン溶液を40%(質量百分率)まで真空濃縮して、高温殺菌及び乾燥工程を経て水溶性コラーゲンを製造した(図2の工程フローチャート参照)。
【0018】
前記実施例と比較例による水溶性コラーゲンの製造時の工程別処理時間を測定して次の表1に示した。又、製造された水溶性コラーゲンの物性を測定して次の表2に示した。
【0019】
【表1】
【0020】
【表2】
【0021】
前記表1に示されたように、本発明による水溶性コラーゲンの製造方法(実施例)では、従来の水溶性コラーゲンの製造方法(比較例)に比べて酸処理及び洗浄工程なしに、直ちに酵素処理を行い、酵素処理の後に脱塩精製工程も不必要であり、総所要時間が15〜20倍程度短縮されたことが判明された。
なお、表2から分るように、前記実施例によれば、重金属処理のための別途の脱塩精製工程なしでも、灰分の量が最大2.5%(質量百分率)を越えなく、その他の物性が良好のマイルドなコラーゲンを製造することができた。
【0022】
【発明の効果】
本発明によれば、従来のコラーゲン製造工程で要求される前処理工程を経ることなしに、原料豚皮から直接水溶性コラーゲンを得ることができるので、前処理のための装置及び設備が要求されないため、コスト低減の効果、製造時間の短縮効果及び環境汚染物質の排出を減少させる等の効果がある。
【0023】
また、前記方法で製造された水溶性コラーゲンは、酸処理及び脱塩工程なしであるため、毒性が強い無機酸や重金属がないマイルドな水溶性コラーゲンで機能性飲料、栄養補助食又は各種加工食品の蛋白強化剤としての使用が容易である。
【図面の簡単な説明】
【図1】本発明に係るマイルドな水溶性コラーゲンの製造方法を示した工程フローチャートである。
【図2】従来方法による豚皮水溶性コラーゲンの製造方法を示した工程フローチャートである。[0001]
[Technical field to which the invention belongs]
The present invention relates to a method for producing mild water-soluble collagen, and more specifically, to produce mild water-soluble collagen that does not undergo chemical treatment and desalination treatment by enzymatic treatment of pork skin to reduce the molecular weight. It relates to a method that can
[0002]
[Prior art]
Conventionally, a general collagen production method is roughly divided into a raw material selection process, a raw material pretreatment process, an extraction process, a water-soluble collagen production process using an extract, and a purification process. More specifically, after the pig skin that has been selected is subjected to acid treatment in a pre-treatment process, the chemicals that are excessively added are washed with a large amount of water to facilitate extraction. . Collagen is extracted from pig skin that has undergone a washing process, water-soluble collagen is produced using this extract, and then water-soluble collagen is produced by performing a desalting treatment process as a purification process for increasing purity. (For example, see the process flowchart of FIG. 2). Therefore, the conventional method for producing collagen from pig skin requires an additional device for treating the wastewater generated from the pretreatment process and the washing process, and the highly toxic inorganic acid used in the acid treatment is required. Since a separate desalting step to be removed is required, the entire manufacturing process is complicated, and the yield efficiency is reduced by going through a multi-step process (see, for example, Patent Documents 1 and 2).
[0003]
Therefore, there is a strong demand for a method for producing water-soluble collagen that can simplify complicated production processes including chemical treatment and heavy metal treatment.
[0004]
[Patent Document 1]
Japanese Patent Laid-Open No. 61-135584 [Patent Document 2]
Japanese Patent Laid-Open No. 13-061474
[Problems to be solved by the invention]
The present invention has been devised in order to solve the above-mentioned problems of the prior art, without subjecting pig skin as a raw material to an acid treatment step and an intermediate treatment step such as a washing step according to the acid treatment step. An object is to provide a method capable of producing water-soluble collagen by a more simplified process.
[0006]
[Means for Solving the Problems]
In order to achieve the above object, a method for producing mild water-soluble collagen according to the present invention comprises a step of chopping pig skin to produce raw collagen, and water is added to the raw collagen in a mass of 70:30 to 50:50. After mixing at a ratio, 0.1 to 1% (mass percentage) of the first protein hydrolase is added to the raw collagen and treated at 55 to 70 ° C. In the first enzyme treatment step, A second enzyme treatment step of adding 0.1 to 0.5% (mass percentage) of the second protein hydrolase to the treated collagen solution and treating at 45 to 55 ° C., and the second enzyme treatment It includes a step of vacuum concentration, sterilization and drying after filtering the collagen solution treated in the step to remove foreign substances.
[0007]
Wherein the first proteolytic enzyme and a second proteolytic enzyme, all the raw material collagen as an enzyme for low molecular weight, respectively licheniformis bacteria (Bacillus licheniformis) and A MIROKU et file Siem bacteria (Ba c illus amyloquefaciems) We want to use.
[0008]
In addition, it is more preferable that the first enzyme treatment step and the second enzyme treatment step are carried out after adjusting to a pH at which each enzyme can exhibit optimal activity, and pH 6.5 to 8.5 and pH 5. The treatment is preferably carried out while adjusting to 5 to 7.5 and maintaining the optimum pH within this range.
[0009]
The molecular weight of the collagen treated in the second enzyme treatment step is preferably 1,000 to 2,000.
[0010]
DETAILED DESCRIPTION OF THE INVENTION
Hereinafter, the present invention will be described in more detail.
The present invention converts the raw material, pork skin, into a low molecular weight substance having a molecular weight of about 1,000 to 2,000 by performing a specific enzyme treatment under a certain temperature and pH condition, thereby performing an acid treatment and a washing step and desalting associated therewith. It is characterized by obtaining mild water-soluble collagen that is rapidly absorbed by the human body in a simple process without passing through the process.
[0011]
The pig skin, which is a raw material of the present invention, is frozen or refrigerated, and after removing foreign substances, it is put into a breaker and chopped to be used as raw collagen.
[0012]
After the water is uniformly mixed with the chopped raw collagen at a ratio of 70:30 to 50:50 by mass, the hydrophilicity in the collagen is increased by using an enzyme treatment method using a specific protein hydrolase. By extracting strong components, water-soluble collagen can be produced. The protein hydrolase can reduce the molecular weight of collagen so that it has a molecular weight in the range of 1,000 to 2,000, which is a fast-absorbed molecular weight. An enzyme having an optimum activity in a neutral pH range, and preferably an enzyme produced by submerged fermentation of a selected strain of Rikeniformis can be used as the first protein hydrolase. As an enzyme, a bacterial enzyme produced by a selection chain of Amyroxifaciem, particularly an endo-protease can be used. At this time, the Rikeniformis enzyme exhibits optimal activity at pH 6.5 to 8.5 and a temperature of 55 to 70 ° C., and the amylo-faciem bacteria hydrolyze proteins at a pH of 5.5 to 7.5 and a temperature of 45 to 55 ° C. Therefore, it is preferable to perform the treatment while adjusting the pH of the collagen solution to meet each optimum condition.
[0013]
When the molecular weight of the collagen reaches about 1,000 to 2,000, the enzyme treatment is terminated by rapidly increasing the temperature of the collagen solution to about 85 ° C. and inactivating the remaining enzyme. Can be confirmed by attaching a viscometer to the side of the reactor and measuring the viscosity of the collagen.
[0014]
In the present invention, foreign substances are removed from the enzyme-treated collagen solution using a centrifugal separator, and then the filtered collagen solution is concentrated to a concentration of about 40% (mass percentage) using a vacuum concentrating tube. The mild collagen powder product is completed by processing and drying.
[0015]
【Example】
Hereinafter, the present invention will be described in more detail with reference to examples. However, the present invention is not limited to the following examples.
[0016]
[Example]
After chopping the refrigerated pork skin with a breaker to produce raw collagen, water and the collagen are mixed uniformly in a mass ratio of 30:70, and then the pH of the collagen solution is adjusted to 7.5. Then, 0.4% (mass percentage) of Rikeniformis bacterium was added to the collagen and treated at 60 ° C. for 4 hours. While adjusting the treated collagen solution to pH 6.5 again, 0.2% (mass percentage) of amylo-faciem bacteria is added to the collagen, and the molecular weight is determined by measuring the viscosity of the collagen while enzymatically treating at 45 ° C. for 2 hours. When the temperature reached about 1,000, the temperature was rapidly increased to 85 ° C., and the excess enzyme was deactivated to terminate the reaction. The foreign substance was removed from the enzyme-treated collagen extract using a centrifuge, followed by filtration using a filter press filter, and then vacuum concentration to a concentration of 40% (mass percentage). Concentrated collagen is instantly sterilized for 0.8 seconds at 121 ° C using a UHT TYPT sterilizer, dried using a spray dryer, subjected to quality inspection, sterilized and packaged to provide the desired mild water solubility. Collagen was produced (see process flow chart in FIG. 1).
[0017]
[Comparative example]
The pig skin was cut to a size of 2 × 5 cm, treated in a raw material treatment tank filled with 1.1% sulfuric acid aqueous solution for 60 hours, and then washed with washing water about 10 times that of the raw pig skin for 12 hours. The raw material that has undergone the acid treatment and washing step is filled with water and extracted in a hot water bath at temperatures of 55 ° C., 65 ° C., and 80 ° C. three times to obtain raw material collagen. Pepsine) was added and treated for 2 hours, filtered using a pulp filter and then desalted and purified by passing through a cation and anion tower for 2 hours. Thereafter, the desalted collagen solution was vacuum concentrated to 40% (mass percentage) to produce water-soluble collagen through high-temperature sterilization and drying steps (see the process flowchart of FIG. 2).
[0018]
Table 1 below shows the treatment time for each process during the production of water-soluble collagen according to Examples and Comparative Examples. The physical properties of the produced water-soluble collagen were measured and shown in Table 2 below.
[0019]
[Table 1]
[0020]
[Table 2]
[0021]
As shown in Table 1, in the method for producing water-soluble collagen according to the present invention (Example), the enzyme is immediately used without the acid treatment and washing steps as compared with the conventional method for producing water-soluble collagen (Comparative Example). It was found that a desalting and purification step was unnecessary after the enzyme treatment and the total time required was reduced by about 15 to 20 times.
As can be seen from Table 2, according to the above examples, the amount of ash does not exceed a maximum of 2.5% (mass percentage) without other desalting and purification steps for heavy metal treatment, and other physical properties are Good mild collagen could be produced.
[0022]
【The invention's effect】
According to the present invention, since water-soluble collagen can be obtained directly from raw pig skin without going through the pretreatment step required in the conventional collagen production step, no device and equipment for pretreatment are required. Therefore, there are effects such as a cost reduction effect, a shortening of manufacturing time, and an emission of environmental pollutants.
[0023]
Further, since the water-soluble collagen produced by the above method is not subjected to an acid treatment and a desalting step, it is a mild water-soluble collagen free of highly toxic inorganic acids and heavy metals, and is a functional beverage, dietary supplement or various processed foods. It is easy to use as a protein enhancer.
[Brief description of the drawings]
FIG. 1 is a process flowchart showing a method for producing mild water-soluble collagen according to the present invention.
FIG. 2 is a process flowchart showing a method for producing a porcine skin-soluble collagen according to a conventional method.
Claims (2)
前記原料コラーゲンに、水を質量で70:30乃至50:50の割合で混合し、その後、前記コラーゲン溶液のpHを6.5〜8.5に調節した後、前記原料コラーゲンに対し、0.1〜1%(質量百分率)の第1蛋白質加水分解酵素であるリケニホルミス菌 (Bacillus licheniformis)を添加し、55〜70℃で処理する第1酵素処理工程と、
前記第1酵素処理工程で処理されたコラーゲン溶液に、前記コラーゲン溶液のpHを5.5〜7.5に調節した後、前記原料コラーゲンに対し0.1〜0.5%(質量百分率)の第2蛋白質加水分解酵素であるアミロクエファシエム菌 (Bacillus amyloquefaciems)を添加し、45〜55℃で処理する第2酵素処理工程及び、
前記第2酵素処理工程で処理されたコラーゲン溶液を濾過して異物質を除去した後、真空濃縮、殺菌及び乾燥を行う工程を含むことを特徴とするマイルドな水溶性コラーゲンの製造方法。Chopping pork skin to produce raw collagen,
Water is mixed with the raw collagen at a mass ratio of 70:30 to 50:50, and then the pH of the collagen solution is adjusted to 6.5 to 8.5. 1-1% of licheniformis bacteria is first proteolytic enzyme (mass percentage) (Bacillus licheniformis) was added, the first enzyme treatment step of treating at 55 to 70 ° C.,
In the collagen solution treated in the first enzyme treatment step, the pH of the collagen solution is adjusted to 5.5 to 7.5, and then 0.1 to 0.5% (mass percentage) with respect to the raw collagen. A second enzyme treatment step of adding a second protein hydrolase, Bacillus amyloquefaciems , and treating at 45-55 ° C;
A method for producing mild water-soluble collagen comprising the steps of filtering the collagen solution treated in the second enzyme treatment step to remove foreign substances and then vacuum concentrating, sterilizing and drying.
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US7396912B2 (en) * | 2003-04-11 | 2008-07-08 | Ecodynamic Biolab | Collagen production method |
KR100735675B1 (en) * | 2004-10-16 | 2007-07-04 | 유향자 | The Processing Method to Improve Efficacy of Collagen by Low-Molecularization and Hydrophilicity, and Collagen Thereof |
JP2006151847A (en) * | 2004-11-26 | 2006-06-15 | Nitta Gelatin Inc | Collagen peptide composition, method for producing the same and cosmetic composition |
NO20051216A (en) * | 2005-03-08 | 2006-01-23 | Wahl Process Systems As | Enzymatic hydrolysis process for collagen and proteinaceous raw materials and a clearance tank for collagen separation, and applications thereof. |
KR100703947B1 (en) * | 2005-07-20 | 2007-04-06 | 주식회사 글로우젠바이오 | Process for preparing collagen |
DE102009033158A1 (en) * | 2009-07-13 | 2011-01-27 | Gelita Ag | Concentrate for the preparation of a cooling and separating agent as well as such cooling and separating agent |
KR102438147B1 (en) | 2015-09-17 | 2022-08-31 | 한국식품연구원 | Method of lowing collagen molecular weight of pig leather, Hide Splits, fishskin and pig leather produced by the same |
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