KR100492371B1 - Method for manufacturing mild water-soluble collagen - Google Patents
Method for manufacturing mild water-soluble collagen Download PDFInfo
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- KR100492371B1 KR100492371B1 KR10-2002-0023965A KR20020023965A KR100492371B1 KR 100492371 B1 KR100492371 B1 KR 100492371B1 KR 20020023965 A KR20020023965 A KR 20020023965A KR 100492371 B1 KR100492371 B1 KR 100492371B1
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- 102000008186 Collagen Human genes 0.000 title claims abstract description 68
- 108010035532 Collagen Proteins 0.000 title claims abstract description 68
- 229920001436 collagen Polymers 0.000 title claims abstract description 68
- 238000000034 method Methods 0.000 title claims abstract description 18
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 14
- 239000002994 raw material Substances 0.000 claims abstract description 22
- 235000015277 pork Nutrition 0.000 claims abstract description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 9
- 238000001035 drying Methods 0.000 claims abstract description 3
- 230000001954 sterilising effect Effects 0.000 claims abstract description 3
- 102000004190 Enzymes Human genes 0.000 claims description 30
- 108090000790 Enzymes Proteins 0.000 claims description 30
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 12
- 108091005804 Peptidases Proteins 0.000 claims description 12
- 102000035195 Peptidases Human genes 0.000 claims description 8
- 239000004365 Protease Substances 0.000 claims description 4
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 4
- 239000000126 substance Substances 0.000 claims description 4
- 238000001914 filtration Methods 0.000 claims description 2
- 238000002156 mixing Methods 0.000 claims description 2
- 238000010306 acid treatment Methods 0.000 abstract description 9
- 238000005406 washing Methods 0.000 abstract description 9
- 230000002255 enzymatic effect Effects 0.000 abstract description 2
- 238000004659 sterilization and disinfection Methods 0.000 abstract description 2
- 235000013305 food Nutrition 0.000 abstract 1
- 238000002203 pretreatment Methods 0.000 abstract 1
- 239000000243 solution Substances 0.000 description 12
- 238000011033 desalting Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 5
- 230000000052 comparative effect Effects 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 238000007796 conventional method Methods 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 229910001385 heavy metal Inorganic materials 0.000 description 3
- 150000007522 mineralic acids Chemical class 0.000 description 3
- 231100000331 toxic Toxicity 0.000 description 3
- 230000002588 toxic effect Effects 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 230000037319 collagen production Effects 0.000 description 2
- 238000010612 desalination reaction Methods 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- OHVLMTFVQDZYHP-UHFFFAOYSA-N 1-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-2-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]ethanone Chemical compound N1N=NC=2CN(CCC=21)C(CN1CCN(CC1)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F)=O OHVLMTFVQDZYHP-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 101710118538 Protease Proteins 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000006243 chemical 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
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 108010088062 lincosaminide O-nucleotidyltransferase Proteins 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 230000009965 odorless effect Effects 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 231100000719 pollutant Toxicity 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000007065 protein hydrolysis Effects 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 235000021067 refined food Nutrition 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 238000004065 wastewater treatment Methods 0.000 description 1
Classifications
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- 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
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- 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
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- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
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Abstract
본 발명은 돈피(pig skin)를 원료로 하여 보다 손쉽고 간편한 방법으로 마일드한 수용성 콜라겐을 제조하는 방법에 관한 것이다.The present invention relates to a method for producing mild water-soluble collagen in an easier and simpler manner using pig skin as a raw material.
본 발명에 따른 수용성 콜라겐은 돈피를 잘게 초핑한 후 종래의 산처리 및 세척과정의 전처리 과정을 거치지 않고 1, 2차에 걸친 효소처리 과정을 거쳐 저분자화된 수용성 콜라겐을 얻은 후 통상의 살균, 건조 과정을 거침으로써 제조될 수 있다.The water-soluble collagen according to the present invention is obtained by chopping pork skin finely and then undergoing the first and second enzymatic treatment without undergoing the pre-treatment of the acid treatment and washing process, and then obtaining normalized sterilization and drying. It can be prepared by going through the process.
본 발명에 따른 수용성 콜라겐은 인체에 흡수가 빠르고 차가운 물에도 쉽게 녹을 수 있는 마일드한 수용성 콜라겐으로 각종 기능성 음료 및 식품에 이용될 수 있다.The water-soluble collagen according to the present invention is a mild water-soluble collagen that can be readily dissolved in cold water and absorbed quickly by the human body, and can be used in various functional drinks and foods.
Description
본 발명은 마일드한 수용성 콜라겐의 제조방법에 관한 것으로, 보다 상세하게는 돈피를 효소처리하여 저분자화함으로써 약품처리 및 탈염처리를 하지 않은 마일드한 수용성 콜라겐을 제조할 수 있는 방법에 관한 것이다. The present invention relates to a method for producing mild water-soluble collagen, and more particularly, to a method for producing mild water-soluble collagen without chemical treatment and desalting by enzymatically treating donpi.
일반적인 콜라겐 제조방법은 크게 원료 선별 단계, 원료의 전처리 단계, 추출 단계, 추출물을 이용한 수용성 콜라겐 제조 단계 및 정제 단계로 구성되어 있다. 보다 구체적으로 살펴보면, 선별된 돈피(pig skin)를 전처리 단계에서 산처리를 행한 다음, 추출을 용이하도록 하기 위하여 과량 투입된 약품을 다량의 물로 세척하는 공정을 거친다. 세척공정을 마친 돈피로부터 콜라겐을 추출하고 이 추출물을 이용하여 수용성 콜라겐을 제조한 후 순도를 높이기 위한 정제 공정으로 탈염처리 공정을 거침으로써 수용성 콜라겐을 제조하게 된다. 따라서 종래의 돈피로부터 콜라겐을 제조하는 방법은 전처리 단계 및 세척공정에서 발생하는 폐수처리를 위한 부가적인 장치가 요구되며, 산처리시 사용되는 독성이 강한 무기산을 제거하는 별도의 탈염과정이 필요하여 전체 제조 공정이 복잡하고 여러 단계를 거침으로써 수득 효율 또한 좋지 못하다. The general collagen production method is largely composed of raw material selection step, raw material pretreatment step, extraction step, water-soluble collagen production step using the extract and purification step. In more detail, the selected pig skin (pig skin) is subjected to an acid treatment in a pretreatment step, and then subjected to a process of washing the injected chemical with a large amount of water in order to facilitate extraction. Collagen is extracted from the donpi after the washing process, water-soluble collagen is prepared using this extract, and then water-soluble collagen is prepared by desalting treatment as a purification process to increase purity. Therefore, the conventional method for producing collagen from pig skin requires additional equipment for wastewater treatment in the pretreatment step and washing process, and requires a separate desalting process to remove the highly toxic inorganic acid used in the acid treatment. The production process is complicated and the yield efficiency is poor due to several steps.
따라서, 약품처리나 중금속 처리를 포함하는 복잡한 제조공정을 단순화하는 수용성 콜라겐의 제조방법이 절실히 요구된다.Therefore, there is an urgent need for a method for producing water-soluble collagen that simplifies complex manufacturing processes including chemical treatment and heavy metal treatment.
이에 본 발명은 상술한 종래 기술의 문제점을 해결하기 위하여 안출된 것으로 원료물질인 돈피를 산처리 단계 및 이에 따른 세척 공정 등의 중간 처리 공정을 거치지 않는 보다 단순화된 공정으로 수용성 콜라겐을 제조할 수 있는 방법을 제공하는데 그 목적이 있다. Accordingly, the present invention has been made to solve the above-mentioned problems of the prior art that can produce a water-soluble collagen in a more simplified process that does not go through the intermediate treatment step such as acid treatment step and washing process according to the raw material pork skin The purpose is to provide a method.
상기 목적을 달성하기 위한 본 발명에 따른 마일드한 수용성 콜라겐의 제조방법은 돈피를 초핑하여 콜라겐의 원료를 준비하는 단계, 상기 콜라겐의 원료에 물을 70 : 30 내지 50 : 50의 비율로 혼합한 다음, 상기 콜라겐의 원료의 용액의 pH를 6.5 내지 8.5로 조절한 후, 상기 콜라겐의 원료에 대하여 0.1 내지 1중량%의 제1 단백질 가수분해 효소를 첨가하여 55 내지 70℃에서 처리하는 제1 효소 처리 단계, 상기 제1 효소 처리된 콜라겐의 원료의 용액의 pH를 5.5 내지 7.5로 조절한 후, 상기 콜라겐의 원료에 대하여 0.1 내지 0.5중량%의 제2 단백질 가수분해 효소를 첨가하여 45 내지 55℃에서 처리하는 제2 효소 처리 단계 및 상기 제2 효소 처리된 콜라겐 용액을 여과하여 이물질을 제거한 후, 진공 농축, 살균 및 건조하는 단계를 포함하는 것을 특징으로 한다.Method for preparing a mild water-soluble collagen according to the present invention for achieving the above object is to prepare a raw material of collagen by chopping donpi, mixing water in the ratio of 70: 30 to 50: 50 to the raw material of collagen After adjusting the pH of the solution of the raw material of collagen to 6.5 to 8.5, the first enzyme treatment to be treated at 55 to 70 ℃ by adding 0.1 to 1% by weight of the first proteolytic enzyme to the raw material of collagen Step, after adjusting the pH of the solution of the raw material of the first enzyme-treated collagen to 5.5 to 7.5, by adding a second proteolytic enzyme of 0.1 to 0.5% by weight based on the raw material of the collagen at 45 to 55 ℃ The second enzyme treatment step of treating and the second enzyme-treated collagen solution by filtration to remove foreign matters, characterized in that it comprises a step of vacuum concentration, sterilization and drying.
상기 제1 단백질 가수분해효소와 제2 단백질 가수분해효소는 모두 상기 콜라겐의 원료를 저분자화하기 위한 효소로 각각 바실러스 린체니포미츠((Bacillus licheniformits)와 바실러스 아밀로퀘파시엠(Bacillus amyloquefaciems) 유래의 효소를 사용하는 것이 바람직하다.The first protease and the second protease are both enzymes for lowering the molecular weight of the collagen, respectively, derived from Bacillus licheniformits and Bacillus amyloquefaciems. It is preferable to use the enzyme.
또한, 상기 제1 효소 처리 단계와 제2 효소 처리 단계는 각각의 효소들이 최적활동을 나타낼 수 있는 pH로 조절한 후 처리하는 것이 보다 바람직하며, 각각 pH 6.5 내지 8.5와 pH 5.5 내지 7.5로 조절하는 것이 좋다.In addition, the first enzyme treatment step and the second enzyme treatment step is more preferably treated after adjusting to a pH at which each enzyme exhibits optimal activity, it is adjusted to pH 6.5 to 8.5 and pH 5.5 to 7.5, respectively It is good.
이하에서 본 발명을 보다 상세히 설명한다.Hereinafter, the present invention will be described in more detail.
본 발명은 원료물질인 돈피를 일정한 온도 및 pH 조건 하에서 특정 효소처리를 행하여 분자량 1,000 내지 2,000정도의 저분자 물질로 전환시킴으로써 산처리나 그에 따른 세척공정 및 탈염공정을 거치지 않고 간단하게 인체에 흡수가 빠른 마일드한 수용성 콜라겐을 얻는데 그 특징이 있다.The present invention converts the raw pork material into a low molecular weight material having a molecular weight of 1,000 to 2,000 by performing a specific enzyme treatment under a constant temperature and pH conditions, so that it is easily absorbed by the human body without undergoing an acid treatment or a washing process and a desalting process accordingly. It is characterized by obtaining mild water-soluble collagen.
본 발명의 원료물질인 돈피는 냉동 또는 냉장 처리된 것이며, 이물질을 제거한 다음 파쇄기에 넣어 초핑하여 사용된다.Pork, which is a raw material of the present invention, is frozen or refrigerated, and is then removed by chopping and then chopped into a crusher.
상기 초핑된 콜라겐의 원료에 물을 70 : 30 내지 50 : 50의 비율로 혼합하여 균일하게 한 다음, 특정 단백질 가수분해 효소를 사용한 효소처리공법을 이용하여 콜라겐내의 친수성이 강한 성분을 뽑아냄으로써 수용성 콜라겐을 제조할 수 있다. 상기 단백질 가수분해 효소는 콜라겐을 체내 흡수가 빠른 분자량인 1,000 내지 2,000정도의 범위를 갖도록 저분자화할 수 있으며, 무엇보다 독성이 강한 무기산의 사용을 최소화하기 위하여 pH 중성범위에서 최적활성을 나타내는 것으로 바람직하게는 제1 단백질 가수분해 효소로 바실러스 린체니포미츠의 선택된 계통의 수중발효에 의해 생산된 효소가 사용될 수 있으며, 제2 단백질 가수분해 효소로 바실러스 아밀로퀘파시엠의 선택 체인에 의해 생산되는 박테리아적 효소로 특히 엔도-프로테아제(endo-protease)가 사용될 수 있다. 이때 상기 바실러스 린체니포미츠 효소는 pH 6.5 내지 8.5, 온도 55 내지 70℃에서 최적 활동을 나타내며, 상기 바실러스 아밀로퀘파시엠은 pH 5.5 내지 7.5, 온도 45 내지 55℃에서 단백질의 가수분해가 가장 잘 일어나므로 상기 콜라겐의 원료의 용액의 pH를 각각의 최적 조건에 맞도록 조절하면서 처리하는 것이 바람직하다.Water is mixed with the raw material of the chopped collagen at a ratio of 70:30 to 50:50 to make it uniform, followed by extracting a hydrophilic component in collagen using an enzyme treatment method using a specific proteolytic enzyme. Can be prepared. The proteolytic enzyme can lower the collagen to have a molecular weight in the range of 1,000 to 2,000, which is a fast molecular weight absorption, and above all, to show the optimum activity in the neutral pH range to minimize the use of toxic inorganic acids. Can be used as the first protease, the enzyme produced by the water fermentation of the selected strains of Bacillus lincheniformites, the bacteria produced by the selection chain of Bacillus amyloquefaciem as the second proteolytic enzyme As an enzyme, in particular, endo-protease can be used. In this case, the Bacillus lincheniformis enzyme exhibits an optimal activity at pH 6.5 to 8.5 and a temperature of 55 to 70 ° C., and the Bacillus amyloquefaciem has the highest hydrolysis of protein at a pH of 5.5 to 7.5 and a temperature of 45 to 55 ° C. Since it happens well, it is preferable to treat the solution while adjusting the pH of the solution of the raw material of collagen to each optimum condition.
상기 효소처리는 콜라겐의 분자량이 약 1,000 내지 2,000 정도가 되면 콜라겐 용액의 온도를 85℃ 정도로 급격히 상승시켜 잔여 효소를 실활시킴으로써 종료되는데, 이때의 분자량은 반응기의 측면에 점성계를 부착하여 콜라겐의 점성도를 측정함으로써 확인할 수 있다. The enzyme treatment is terminated by inactivating the residual enzyme by rapidly increasing the temperature of the collagen solution to about 85 ℃ when the molecular weight of the collagen is about 1,000 to 2,000, wherein the molecular weight is attached to the side of the reactor by attaching a viscometer to the viscosity of the collagen It can be confirmed by measuring.
본 발명에서는 상기 효소처리된 콜라겐 용액을 원심분리기를 이용하여 이물질을 제거한 후 여과한 콜라겐 용액을 진공 농축관을 이용하여 농도 40%정도까지 농축하고 살균처리 및 건조시킴으로써 마일드한 콜라겐 분말 제품을 완성한다.In the present invention, the enzyme-treated collagen solution is removed by using a centrifugal separator, and then the filtered collagen solution is concentrated to a concentration of about 40% using a vacuum concentrator, sterilized and dried to complete the mild collagen powder product. .
이하에서 실시예를 통하여 본 발명을 보다 상세히 설명할 것이다. 그러나, 이하의 실시예는 단지 예시를 위한 것이므로, 본 발명의 범위를 국한시키는 것으로 이해되어서는 안 될 것이다.Hereinafter, the present invention will be described in more detail with reference to Examples. However, the following examples are for illustration only and should not be understood as limiting the scope of the invention.
[실시예]EXAMPLE
냉장 처리된 돈피를 파쇄기로 초핑하여 콜라겐의 원료를 준비한 후, 물과 상기 콜라겐을 30 : 70의 비율로 균일하게 혼합한 다음 상기 콜라겐 용액의 pH를 7.5로 조정하면서 콜라겐 대비 0.4중량%의 바실러스 린체니포미츠 유래의 효소를 첨가하고 60℃에서 4시간동안 처리하였다. 처리된 상기 콜라겐 용액을 다시 pH 6.5로 조정하면서 바실러스 아밀로퀘파시엠 유래의 효소를 0.2중량% 첨가하고 45℃에서 2시간동안 효소처리하면서 콜라겐의 점도 측정을 통하여 분자량이 1,000정도가 되면 온도를 85℃로 급격하게 상승시켜 여분의 효소를 실활시켜 반응을 종결하였다. 효소처리된 콜라겐 추출물을 원심분리기로 이물질을 제거한 후 필터프레스 여지필터를 사용하여 여과한 다음 농도 40%까지 진공 농축하였다. 농축된 콜라겐을 UHT TYPE 살균기를 이용하여 121℃에서 0.8초동안 연속적으로 순간 살균한 후 스프레이 드라이어를 이용하여 건조하여 품질 검사를 시행한 후 멸균 포장하여 원하는 마일드한 수용성 콜라겐을 제조하였다.Chopped refrigerated pork skin with a crusher to prepare the raw material of collagen, and then uniformly mixed with water and the collagen in a ratio of 30: 70 and then adjusted the pH of the collagen solution to 7.5 while 0.4% by weight of Bacillus lin Enzyme from Chenipomit was added and treated at 60 ° C. for 4 hours. When the treated collagen solution was adjusted to pH 6.5 again, 0.2 wt% of Bacillus amyloquefaciem-derived enzyme was added, and the enzyme was treated at 45 ° C. for 2 hours to measure the viscosity of the collagen. The reaction was terminated by ramping up to 85 ° C. to inactivate the excess enzyme. The enzyme-treated collagen extract was removed by a centrifuge, filtered using a filter press filter, and then concentrated in vacuo to a concentration of 40%. The concentrated collagen was sterilized continuously for 0.8 seconds at 121 ° C. using a UHT TYPE sterilizer, dried using a spray dryer, subjected to a quality test, and then sterilized and packaged to prepare mild water-soluble collagen.
[비교예][Comparative Example]
돈피를 2×5㎝의 크기로 절단하여 1.1% 황산 수용액이 담긴 원료처리 탱크에서 60시간동안 처리한 후 상기 원료 돈피의 약 10배의 세척수로 12시간동안 세척하였다. 상기 산처리 및 세척 과정을 거친 원료물질에 물을 넣고 중탕으로 각각 55℃, 65℃, 80℃의 온도에서 3회에 걸쳐 추출하여 원료 콜라겐을 얻은 후, 이 원료 콜라겐에 B 타입의 효소를 첨가하여 2시간동안 처리하고 펄프여과기를 사용하여 여과한 다음 2시간동안 양이온탑과 음이온탑을 통과시켜 탈염 정제하였다. 이후, 탈염된 콜라겐 용액을 40%까지 진공농축하고 고온살균 및 건조하여 수용성 콜라겐을 제조하였다.The pork skin was cut to a size of 2 × 5 cm and treated for 60 hours in a raw material treatment tank containing 1.1% sulfuric acid aqueous solution, and then washed for 12 hours with about 10 times the washing water of the raw pork skin. Water was added to the raw material subjected to the acid treatment and washing, and extracted three times at a temperature of 55 ° C., 65 ° C. and 80 ° C. with a hot bath to obtain raw collagen, and then B-type enzyme was added to the raw collagen. The mixture was treated for 2 hours, filtered using a pulp filter, and then desalted and purified by passing through a cation tower and an anion tower for 2 hours. Thereafter, the desalted collagen solution was concentrated in vacuo to 40%, sterilized and dried to prepare water-soluble collagen.
상기 실시예와 비교예에 따른 수용성 콜라겐의 제조시 공정별 처리시간을 측정하여 다음의 [표1]에 나타내었으며, 제조된 수용성 콜라겐의 물성을 측정하여 다음의 [표2]에 나타내었다.In the preparation of the water-soluble collagen according to the Examples and Comparative Examples was measured in the process shown in the following [Table 1], and measured in the physical properties of the prepared water-soluble collagen is shown in the following [Table 2].
상기 [표1]에서 나타낸 바와 같이, 본 발명에 따른 수용성 콜라겐의 제조방법(실시예)은 종래의 수용성 콜라겐의 제조방법(비교예)과 비교하여 산처리 및 세척단계를 거치지 않고 바로 효소처리를 행하며, 효소처리 후에 탈염정제 과정 또한 거칠 필요가 없어 총소요시간이 15 내지 20배 정도 단축됨을 알 수 있다.As shown in Table 1, the method for preparing water-soluble collagen according to the present invention (example) is compared to the conventional method for preparing water-soluble collagen (comparative example), without undergoing an acid treatment and washing step, without performing enzymatic treatment. In addition, the desalting and purification process after the enzyme treatment also does not need to be rough, so that the total time is reduced by 15 to 20 times.
또한 [표2]에서 알 수 있듯이, 상기 실시예에 따르면 중금속 처리를 위한 별도의 탈염 정제 과정을 거치지 않아도 회분의 양이 최대 2.5를 넘지 않으며 기타 다른 물성이 양호한 마일드한 콜라겐을 제조할 수 있다. In addition, as can be seen from Table 2, according to the embodiment, even without a separate desalination purification process for treating heavy metals, the amount of ash does not exceed 2.5, and other mild physical collagen may be prepared.
본 발명에 따르면, 종래의 콜라겐 제조과정에서 요구되는 전처리 단계를 거치지 않고 원료 돈피로부터 직접 수용성 콜라겐을 얻을 수 있어 전처리를 위한 장치 및 설비가 요구되지 않아 원가절감의 효과, 제조시간의 단축 효과 및 환경오염물질의 배출을 줄이는 효과가 있다. According to the present invention, the water-soluble collagen can be directly obtained from raw pork skin without undergoing the pretreatment step required in the conventional collagen manufacturing process, so that no equipment and equipment for the pretreatment are required, so that the cost reduction effect, the shortening time, and the environment are not required. It has the effect of reducing pollutant emissions.
또한, 상기 방법으로 제조된 수용성 콜라겐은 산처리 및 탈염 공정을 거치지 않아 독성이 강한 무기산이나 중금속이 없는 마일드한 수용성 콜라겐으로 기능성 음료, 영양보조 식품 또는 각종 가공식품의 단백강화제로서 사용이 용이하다.In addition, the water-soluble collagen prepared by the above method is a mild water-soluble collagen free of toxic inorganic acids or heavy metals without undergoing acid treatment and desalination, and is easy to use as a protein enhancer for functional drinks, nutritional supplements or various processed foods.
이상에서 본 발명은 기재된 구체예에 대해서만 상세히 기술되었지만, 본 발명의 기술사상 범위 내에서 다양한 변형 및 수정이 가능함은 당업자에게 있어서 명백한 것이며, 이러한 변형 및 수정이 첨부된 특허청구범위에 속함은 당연한 것이다. While the invention has been described in detail only with respect to the described embodiments, it will be apparent to those skilled in the art that various modifications and variations are possible within the spirit of the invention, and such modifications and variations belong to the appended claims. .
도1은 종래 방법에 따른 돈피 수용성 콜라겐의 제조방법을 나타낸 공정흐름도이다.1 is a process flow diagram illustrating a method for preparing donpi water-soluble collagen according to a conventional method.
도2는 본 발명에 따른 마일드한 수용성 콜라겐의 제조방법을 나타낸 공정흐름도이다.Figure 2 is a process flow diagram showing a method for producing mild water-soluble collagen according to the present invention.
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| KR20170033622A (en) | 2015-09-17 | 2017-03-27 | 한국식품연구원 | Method of lowing collagen molecular weight of pig leather, Hide Splits, fishskin and pig leather produced by the same |
| KR101960300B1 (en) | 2018-11-08 | 2019-03-20 | 김경림 | Gelatine manufacturing system using pulp filter apparatus |
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| ATE417121T1 (en) * | 2003-04-11 | 2008-12-15 | Ecodynamic Biolab Inc | METHOD FOR COLLAGEN EXTRACTION WHICH INCLUDES MICROBIAL FERMENTATION |
| 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 |
| NO320736B1 (en) * | 2005-03-08 | 2006-01-23 | Wahl Process Systems As | Enzymatic hydrolysis process for collagen and proteinaceous resins and a clarification 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 |
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| US5670369A (en) * | 1996-06-25 | 1997-09-23 | Ranpak Corporation | Method for the production of soluble collagen |
| US5686262A (en) * | 1993-06-16 | 1997-11-11 | Ranpak Corporation | Recycle process for the production of low-cost soluble collagen |
| KR20000020305A (en) * | 1998-09-19 | 2000-04-15 | 이정식 | Preparation method for protein solution of low molecular using leather scrap |
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| US5686262A (en) * | 1993-06-16 | 1997-11-11 | Ranpak Corporation | Recycle process for the production of low-cost soluble collagen |
| US5670369A (en) * | 1996-06-25 | 1997-09-23 | Ranpak Corporation | Method for the production of soluble collagen |
| KR20000020305A (en) * | 1998-09-19 | 2000-04-15 | 이정식 | Preparation method for protein solution of low molecular using leather scrap |
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| KR20170033622A (en) | 2015-09-17 | 2017-03-27 | 한국식품연구원 | Method of lowing collagen molecular weight of pig leather, Hide Splits, fishskin and pig leather produced by the same |
| KR101960300B1 (en) | 2018-11-08 | 2019-03-20 | 김경림 | Gelatine manufacturing system using pulp filter apparatus |
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