JP4738005B2 - Fish skin pretreatment method - Google Patents
Fish skin pretreatment method Download PDFInfo
- Publication number
- JP4738005B2 JP4738005B2 JP2005026842A JP2005026842A JP4738005B2 JP 4738005 B2 JP4738005 B2 JP 4738005B2 JP 2005026842 A JP2005026842 A JP 2005026842A JP 2005026842 A JP2005026842 A JP 2005026842A JP 4738005 B2 JP4738005 B2 JP 4738005B2
- Authority
- JP
- Japan
- Prior art keywords
- fish skin
- collagen
- fish
- treatment
- skin
- 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.)
- Active
Links
- 238000002203 pretreatment Methods 0.000 title claims description 6
- 241000251468 Actinopterygii Species 0.000 claims description 68
- 102000008186 Collagen Human genes 0.000 claims description 37
- 108010035532 Collagen Proteins 0.000 claims description 37
- 229920001436 collagen Polymers 0.000 claims description 37
- 239000007800 oxidant agent Substances 0.000 claims description 20
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 14
- 238000000034 method Methods 0.000 claims description 13
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 claims description 12
- 239000003960 organic solvent Substances 0.000 claims description 11
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical group OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 claims description 9
- 239000002994 raw material Substances 0.000 claims description 9
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 8
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 claims description 6
- DKGAVHZHDRPRBM-UHFFFAOYSA-N Tert-Butanol Chemical compound CC(C)(C)O DKGAVHZHDRPRBM-UHFFFAOYSA-N 0.000 claims description 6
- 239000012266 salt solution Substances 0.000 claims description 5
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 claims description 4
- CBENFWSGALASAD-UHFFFAOYSA-N Ozone Chemical compound [O-][O+]=O CBENFWSGALASAD-UHFFFAOYSA-N 0.000 claims description 4
- 239000003638 chemical reducing agent Substances 0.000 claims description 4
- 239000012279 sodium borohydride Substances 0.000 claims description 4
- 229910000033 sodium borohydride Inorganic materials 0.000 claims description 4
- 239000012280 lithium aluminium hydride Substances 0.000 claims description 3
- -1 lithium aluminum hydride Chemical compound 0.000 claims description 3
- BDERNNFJNOPAEC-UHFFFAOYSA-N propan-1-ol Chemical compound CCCO BDERNNFJNOPAEC-UHFFFAOYSA-N 0.000 claims description 3
- 235000019688 fish Nutrition 0.000 description 61
- 210000003491 skin Anatomy 0.000 description 53
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 12
- 210000004207 dermis Anatomy 0.000 description 10
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 239000006185 dispersion Substances 0.000 description 8
- 230000001590 oxidative effect Effects 0.000 description 8
- 210000001519 tissue Anatomy 0.000 description 8
- 230000008961 swelling Effects 0.000 description 7
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 6
- 235000002639 sodium chloride Nutrition 0.000 description 6
- 150000003839 salts Chemical class 0.000 description 5
- 108091005804 Peptidases Proteins 0.000 description 4
- 102000035195 Peptidases Human genes 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 210000002615 epidermis Anatomy 0.000 description 4
- 235000013372 meat Nutrition 0.000 description 4
- 241000124008 Mammalia Species 0.000 description 3
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 3
- 230000002378 acidificating effect Effects 0.000 description 3
- 239000007864 aqueous solution Substances 0.000 description 3
- 239000002537 cosmetic Substances 0.000 description 3
- 239000000835 fiber Substances 0.000 description 3
- 229910017053 inorganic salt Inorganic materials 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 108091005658 Basic proteases Proteins 0.000 description 2
- 108010010803 Gelatin Proteins 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 210000001361 achilles tendon Anatomy 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 238000004040 coloring Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 239000008273 gelatin Substances 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 235000011852 gelatine desserts Nutrition 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L sodium carbonate Substances [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- XHFLOLLMZOTPSM-UHFFFAOYSA-M sodium;hydrogen carbonate;hydrate Chemical compound [OH-].[Na+].OC(O)=O XHFLOLLMZOTPSM-UHFFFAOYSA-M 0.000 description 2
- 241000473391 Archosargus rhomboidalis Species 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 235000008733 Citrus aurantifolia Nutrition 0.000 description 1
- 241000252233 Cyprinus carpio Species 0.000 description 1
- 241000252498 Ictalurus punctatus Species 0.000 description 1
- 241001147156 Lates niloticus Species 0.000 description 1
- 241000269821 Scombridae Species 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- 239000005708 Sodium hypochlorite Substances 0.000 description 1
- 244000062793 Sorghum vulgare Species 0.000 description 1
- 241000276707 Tilapia Species 0.000 description 1
- 235000011941 Tilia x europaea Nutrition 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000007605 air drying Methods 0.000 description 1
- 239000012670 alkaline solution Substances 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 238000009360 aquaculture Methods 0.000 description 1
- 244000144974 aquaculture Species 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- AXCZMVOFGPJBDE-UHFFFAOYSA-L calcium dihydroxide Chemical compound [OH-].[OH-].[Ca+2] AXCZMVOFGPJBDE-UHFFFAOYSA-L 0.000 description 1
- 239000000920 calcium hydroxide Substances 0.000 description 1
- 229910001861 calcium hydroxide Inorganic materials 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 230000037319 collagen production Effects 0.000 description 1
- 239000000515 collagen sponge Substances 0.000 description 1
- 239000006103 coloring component Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000009615 deamination Effects 0.000 description 1
- 238000006481 deamination reaction Methods 0.000 description 1
- 238000004042 decolorization Methods 0.000 description 1
- 238000004332 deodorization Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 239000013505 freshwater Substances 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000000227 grinding Methods 0.000 description 1
- DKAGJZJALZXOOV-UHFFFAOYSA-N hydrate;hydrochloride Chemical compound O.Cl DKAGJZJALZXOOV-UHFFFAOYSA-N 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000004571 lime Substances 0.000 description 1
- 235000020640 mackerel Nutrition 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 235000019713 millet Nutrition 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000009965 odorless effect Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- SATVIFGJTRRDQU-UHFFFAOYSA-N potassium hypochlorite Chemical compound [K+].Cl[O-] SATVIFGJTRRDQU-UHFFFAOYSA-N 0.000 description 1
- 238000003825 pressing Methods 0.000 description 1
- 238000010298 pulverizing process Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 235000017550 sodium carbonate Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- SUKJFIGYRHOWBL-UHFFFAOYSA-N sodium hypochlorite Chemical compound [Na+].Cl[O-] SUKJFIGYRHOWBL-UHFFFAOYSA-N 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
Landscapes
- Cosmetics (AREA)
- Peptides Or Proteins (AREA)
Description
本発明は、魚皮よりコラーゲンを利用する際の魚皮の前処理方法に関する。 The present invention relates to a method for pretreating fish skin when using collagen from fish skin.
狂牛病(BSEとも記載する場合もある)の発生あるいは宗教上の理由から、化粧品分野、医療分野等の製品の原料として用いられるコラーゲンについて、哺乳類以外を由来とする、具体的には魚類を由来とするコラーゲンが好まれる場合がある。
従来の哺乳動物の場合にはコラーゲン抽出の原料として真皮層、アキレス腱等が用いられ、一方魚類の場合には魚皮が原料として用いられる。哺乳動物では真皮層、アキレス腱等がある程度の厚み、容積を持つために他の組織の混入を予防することが容易で原料組織を純粋に採取する事が出来るのに対し、魚類の場合には通常魚肉を採取した後の魚皮が原料として用いられる。魚皮にはコラーゲンを多量に含む真皮の他に、表皮、鱗等の組織・器官が含まれるために魚皮より真皮のみを分ける作業が必要となるが、原料とする真皮が薄く取り難い上に、表皮は着色していることが多く、この着色部が混入することによって、最終物であるコラーゲンに着色した異物が混入する及び臭いが残るという問題が生じるため、原料組織の単離に問題があった。
そのために先行文献にも見られるように、魚皮よりコラーゲンを取るためには、脱臭、脱色を目的に前処理を行い出来る限り表皮等の他の組織を除き、真皮のみとする前処理が不可欠な工程であった。
特許文献1には生魚の皮から高品質のゼラチンゲルを得るために、水による皮の洗浄、酸による処理、酸性pHにおける熱抽出を含む工程が開示されている。
特許文献2には原料である魚皮をエタノールにより繰り返し洗浄することにより抽出されるコラーゲンの色と臭いを除去する工程が開示されている。
しかしこれらの方法はコラーゲンではなくゼラチンの製造に関する内容、あるいはコラーゲン製造であっても十分な効果が得られない、有機溶媒の使用による危険性等の課題が残っていた。
In the case of conventional mammals, the dermis layer, the Achilles tendon, etc. are used as the raw material for collagen extraction, while in the case of fish, fish skin is used as the raw material. In mammals, the dermis layer, Achilles tendon, etc. have a certain thickness and volume, so it is easy to prevent contamination of other tissues and the raw tissue can be collected purely. The fish skin after the fish meat is collected is used as a raw material. In addition to the dermis that contains a large amount of collagen, the fish skin contains tissues and organs such as the epidermis and scales, so it is necessary to separate only the dermis from the fish skin. In addition, the epidermis is often colored, and when this colored part is mixed, there is a problem that colored foreign matter is mixed in the final collagen and odor remains, which is a problem in isolation of the raw tissue. was there.
Therefore, as can be seen in the prior literature, in order to remove collagen from fish skin, pretreatment with the dermis only is necessary, except for other tissues such as the epidermis as much as possible, in order to perform pretreatment for the purpose of deodorization and decolorization. It was a difficult process.
Patent Document 1 discloses a process including washing skin with water, treatment with acid, and heat extraction at acidic pH in order to obtain high-quality gelatin gel from raw fish skin.
Patent Document 2 discloses a process of removing the color and odor of collagen extracted by repeatedly washing raw fish skin with ethanol.
However, these methods still have problems related to the production of gelatin, not collagen, or the effects of using organic solvents, in which sufficient effects cannot be obtained even with collagen production.
本発明では、魚皮より出来る限り単純で危険のない方法によって臭い、色の無いコラーゲン原料を得るという課題を解決するための前処理方法の開発を目標とした。 The object of the present invention is to develop a pretreatment method for solving the problem of obtaining a odorless and colorless collagen raw material by a simpler and less dangerous method than fish skin.
本発明者は、上記課題を解決するために鋭意研究を重ねた結果、前処理として水と混合
した有機溶媒あるいは塩溶液のいずれか、あるいは組み合わせによってコラーゲン組織の膨潤を抑え、同時にアルカリ性の条件下酸化剤を作用させることで魚皮より色、臭いを取ることができ、魚皮に含まれるコラーゲンを容易に利用できることを見出し、本発明を完成した。
即ち、本発明の要旨は、魚皮より色、臭いの気にならないコラーゲン原料を得るための魚皮の前処理方法であって、魚皮を水と混合した有機溶媒あるいは塩溶液もしくはこれらを組み合わせた溶液によってコラーゲン組織の膨潤を抑え、同時にアルカリ性の条件下H 2 O 2 あるいはオゾンのいずれかの酸化剤を作用させる工程を含むことを特徴とする魚皮の前処理方法であり、その際、有機溶媒としてメタノール、エタノール、プロパノール、イソプロパノール、ブタノール、t−ブタノール、アセトンから選ばれることが好ましく、更に、ホウ素化水素ナトリウム、リチウムアルミニウムハイドライドから選ばれる還元剤による処理を行うことが好ましい。
As a result of intensive research to solve the above problems, the present inventor has suppressed the swelling of collagen tissue by pre-treatment with either an organic solvent mixed with water or a salt solution, or a combination thereof, and at the same time under alkaline conditions. The inventors have found that the color and odor can be removed from the fish skin by the action of an oxidizing agent, and the collagen contained in the fish skin can be easily used, and the present invention has been completed.
That is, the gist of the present invention is a fish skin pretreatment method for obtaining a collagen raw material that does not have a color or odor from fish skin, and is an organic solvent or salt solution in which fish skin is mixed with water, or a combination thereof. A method for pretreating fish skin characterized by comprising a step of suppressing swelling of collagen tissue with a solution and simultaneously applying an oxidizing agent of either H 2 O 2 or ozone under alkaline conditions , methanol as organic solvent, ethanol, propanol, isopropanol, butanol, t-butanol, be chosen from acetone preferably, further, sodium borohydride, it is preferable to perform the treatment with a reducing agent selected from lithium aluminum hydride.
本発明は単に、魚皮を水と混合した有機溶媒あるいは塩溶液もしくはこれらを組み合わせた溶液に浸漬してコラーゲン組織の膨潤を抑え、アルカリ性の条件下酸化剤を作用させるという簡単な工程によって着色もしくは魚臭の少ない、コラーゲン原料の魚皮を容易に得ることができる。 The present invention is simply colored by a simple process in which the fish skin is immersed in an organic solvent mixed with water or a salt solution or a combination of these to suppress swelling of the collagen tissue and an oxidizing agent is allowed to act under alkaline conditions. Collagen raw fish skin with less fish odor can be easily obtained.
以下に本発明を詳細に説明する。
本発明で用いることが出来る魚種には特に制限はなく、淡水魚、海水魚のいずれにも使用が可能である。また寒流系、暖流系のいずれの魚種であっても本発明が適応される。また養殖等によって大量に得られる魚種が望ましく、具体的にはマグロ、イズミダイ(ティラピア)、コイ、ナイルパーチ、サケ、シタビラメ、タイ、サバ、チャネル・ナマズ等を挙げることができる。
使用する魚皮としては魚肉を剥離した後の皮が使用され、新鮮であっても凍結品あるいは塩付け、石灰付け等の処理が施されていても、コラーゲンの構造が保持されている真皮を有していれば使用することが出来る。また魚皮は剥いだままであっても小片に切った後でも用いることができる。
The present invention is described in detail below.
There is no restriction | limiting in particular in the fish kind which can be used by this invention, It can be used for any of freshwater fish and saltwater fish. In addition, the present invention is applied to any fish species of a cold current system and a warm current system. In addition, fish species obtained in large quantities by aquaculture and the like are desirable, and specific examples include tuna, sea bream (tilapia), carp, nile perch, salmon, millet, Thailand, mackerel, and channel catfish.
The fish skin to be used is the peel after the fish meat is peeled off, and the dermis that retains the structure of the collagen is preserved even if it is fresh or has been frozen, salted, or lime-treated. If it has, it can be used. The fish skin can be used even after being peeled or after being cut into small pieces.
本発明の処理の前に魚皮を水、あるいは0.5%程度の重曹水よる洗浄を行う。水洗の終わった魚皮を水に入れた後に、水と混合する有機溶媒あるいは水に溶解する無機塩を加える。これらを水に加えることによって、魚皮の膨潤を抑えることができる。具体的な有機溶媒としてはメタノール、エタノール、プロパノール、イソプロパノール、ブタノール、t−ブタノール等を挙げることができる。また無機塩としては塩化ナトリウム、塩化カリウム、塩化カルシウム、硫酸ナトリウム、炭酸ナトリウム等を挙げることができる。なお塩溶液を使用する場合に、同時に界面活性剤を併用し効果を高めることも可能である。
加える有機溶媒の量は水との混合後、全量に対して10〜80重量%加えることができ、更には30〜60重量%が望ましい。また加える無機塩の量としては、出来る限り飽和以上の塩を含む溶液が望ましい。
混合あるいは溶解した有機溶媒混合水溶液あるいは塩水溶液に原料となる魚皮を加える。溶液は全量の魚皮が十分に浸る量で有れば問題はない。この溶液に魚皮を入れる。
Before the treatment of the present invention, the fish skin is washed with water or about 0.5% sodium bicarbonate water. After the washed fish skin is put into water, an organic solvent mixed with water or an inorganic salt dissolved in water is added. By adding these to water, swelling of the fish skin can be suppressed. Specific examples of the organic solvent include methanol, ethanol, propanol, isopropanol, butanol, t-butanol and the like. Examples of inorganic salts include sodium chloride, potassium chloride, calcium chloride, sodium sulfate, sodium carbonate and the like. When using a salt solution, it is also possible to enhance the effect by using a surfactant at the same time.
The amount of the organic solvent to be added can be added by 10 to 80% by weight, more preferably 30 to 60% by weight, based on the total amount after mixing with water. The amount of the inorganic salt to be added is preferably a solution containing a saturated salt as much as possible.
Add the fish skin as a raw material to the mixed or dissolved organic solvent mixed aqueous solution or salt aqueous solution. There is no problem as long as the total amount of the fish skin is sufficiently immersed in the solution. Add fish skin to this solution.
次にこの溶液をアルカリ性にする。アルカリ性にするためにはアルカリ性の無機塩を加えることにより行われる。加える塩としては通常使用されるアルカリ性溶液を調製する際に使用される塩を用いることができ、具体的には水酸化ナトリウム、水酸化カリウム、水酸化カルシウム等を挙げることができる。加える量としては溶液のpHが10〜14の間であれば良い。 The solution is then made alkaline. In order to make it alkaline, it is carried out by adding an alkaline inorganic salt. As the salt to be added, a salt used in preparing a commonly used alkaline solution can be used, and specific examples include sodium hydroxide, potassium hydroxide, calcium hydroxide and the like. The amount to be added may be between 10 and 14 pH.
次に酸化剤を加え酸化処理を行う。使用する酸化剤としては過酸化水素、オゾン、次亜塩素酸ナトリウム、次亜塩素酸カリウム等を挙げることができる。これらの内、特に過酸化水素、オゾンは反応の後に酸化剤からの副産物が残ることが無く望ましい。加える酸化剤の量としては使用する酸化剤の種類によって変わるが、例えば過酸化水素であれば0.1%〜1%(g/L)が望ましい。 Next, an oxidizing agent is added and oxidation treatment is performed. Examples of the oxidizing agent used include hydrogen peroxide, ozone, sodium hypochlorite, and potassium hypochlorite. Of these, hydrogen peroxide and ozone are particularly desirable because no by-products from the oxidizing agent remain after the reaction. The amount of oxidizing agent to be added varies depending on the type of oxidizing agent to be used. For example, in the case of hydrogen peroxide, 0.1% to 1% (g / L) is desirable.
このアルカリ性条件下での酸化剤処理によって魚皮の脱色、脱臭を行うことができる。この前処理は酸化剤によって魚皮の内、特に真皮内のコラーゲン分子に分子間架橋が導入され、架橋の導入されない着色成分、臭い成分を容易に除くことができると考えられる。本発明によって脱色、脱臭された魚皮を得ることができるために、この魚皮をそのまま加工することによって、各種コラーゲン製品を製造することが可能となり、従来のように魚皮より真皮のみを剥離し利用する必要が無くなった。
酸化剤による処理はコラーゲンが変性することが無い温度で行うことができるが、処理時間を短縮するためにはできるだけ高い温度による処理が望ましく、具体的にはその魚種のコラーゲンの変性温度より5〜10℃程度低い温度で行うことが望ましい。また処理時間は処理温度、酸化剤の種類、酸化剤の濃度等に依存する。例えば過酸化水素を0.5%g/Lを50%イソプロパノール溶液中で処理した場合、20℃以下で1〜3日間行うことが望ましい。なお処理中は魚皮をゆっくり攪拌する事が望ましい。
By this oxidant treatment under alkaline conditions, fish skin can be decolorized and deodorized. In this pretreatment, it is considered that intermolecular crosslinks are introduced into the collagen molecules in the fish skin, particularly in the dermis, by the oxidizing agent, and coloring components and odor components that are not introduced with crosslinks can be easily removed. Since it is possible to obtain a decolorized and deodorized fish skin according to the present invention, it is possible to produce various collagen products by processing the fish skin as it is, and only the dermis is peeled from the fish skin as in the past. And there is no need to use it.
The treatment with the oxidizing agent can be performed at a temperature at which the collagen is not denatured, but in order to shorten the treatment time, the treatment at a temperature as high as possible is desirable. It is desirable to carry out at a temperature lower by about 10 ° C. The treatment time depends on the treatment temperature, the type of oxidant, the concentration of oxidant, and the like. For example, when 0.5% g / L of hydrogen peroxide is treated in a 50% isopropanol solution, it is desirable to carry out the treatment at 20 ° C. or lower for 1 to 3 days. It is desirable to slowly stir the fish skin during the treatment.
処理が終了し色、臭いが除かれた魚皮を酸性の水溶液に入れ、機械的に粉砕することでコラーゲンの分散液を得ることができる。この際、pHはできる限り真皮の膨潤を抑えるpHであることが望ましく、pH5〜pH7の酸性が適当である。これは先の酸化剤処理の際にアルカリ性条件によって、コラーゲンの構成アミノ酸より脱アミンが起こるためにコラーゲンの等電点が下がることによるためで、天然型のコラーゲンの等電点がpH9付近から下がるために、酸性条件で魚皮の膨潤を抑えることができる。ここで用いられるpHは最も膨潤が起こらないpHに設定される。
このpHで例えばNaHSO3等を加えることによって、先の酸化剤処理から残留している酸化剤を分解することができる。なお残留については、例えば過酸化水素検出試薬等によって確認することも可能である。
After the treatment is finished, the fish skin from which the color and smell are removed is placed in an acidic aqueous solution and mechanically pulverized to obtain a collagen dispersion. At this time, the pH is desirably a pH that suppresses the swelling of the dermis as much as possible, and an acidity of pH 5 to pH 7 is appropriate. This is because the isoelectric point of the collagen is lowered from around pH 9 due to the lowering of the isoelectric point of the collagen due to deamination occurring from the constituent amino acids of the collagen due to alkaline conditions during the previous oxidant treatment. Therefore, the swelling of the fish skin can be suppressed under acidic conditions. The pH used here is set to a pH at which swelling does not occur most.
By adding, for example, NaHSO 3 or the like at this pH, the oxidant remaining from the previous oxidant treatment can be decomposed. The residue can be confirmed by, for example, a hydrogen peroxide detection reagent.
酸化剤による処理の前後のいずれか、あるいは前後ともにアルカリ蛋白質分解酵素処理あるいはホウ素化水素ナトリウム、リチウムアルミニウムハイドライド等還元剤による処理を行うことで、より着色、臭いの少ない魚皮を得ることが可能となる。例えば酸化剤処理の前にアルカリ蛋白質分解酵素処理を行うと、水洗でかなりの着色を取り除けるため酸化剤処理の時間を短縮ができる。また酸化処理の前後どちらでアルカリ蛋白質分解酵素処理を行うことで魚皮を構成する線維を軟らかくすることが可能となる。この蛋白質分解酵素処理工程はpH9〜11のアルカリ条件下、アルカリ蛋白分解酵素(例えばナガセケムテック(株)社製ビオブラーゼ等)により行うことで、線維の分散に優れより本発明の効果を明確にすることができる。また還元剤による処理によりコラーゲンに存在する可逆的な分子間架橋を化学的に還元し、この結合を不可逆的な結合とすることができ、魚皮の機械的な強度を高めることができる。その結果例えば本発明の前処理終了後に機械的粉砕を加えコラーゲン分散液を調製する場合、長い線維のコラーゲン分散液を得ることができる。 It is possible to obtain fish skin with less coloring and odor by performing alkaline proteolytic enzyme treatment or treatment with a reducing agent such as sodium borohydride or lithium aluminum hydride either before or after treatment with an oxidizing agent. It becomes. For example, if the alkaline protease treatment is performed before the oxidant treatment, considerable coloration can be removed by washing with water, so that the time for the oxidant treatment can be shortened. Moreover, it becomes possible to soften the fiber which comprises a fish skin by performing an alkaline proteolytic enzyme process before and after an oxidation process. This proteolytic enzyme treatment step is performed with an alkaline proteolytic enzyme (for example, biolase manufactured by Nagase Chemtech Co., Ltd.) under alkaline conditions of pH 9 to 11, so that the fiber dispersion is excellent and the effect of the present invention is clarified. can do. In addition, reversible intermolecular crosslinks present in collagen can be chemically reduced by treatment with a reducing agent to make this bond an irreversible bond, and the mechanical strength of fish skin can be increased. As a result, for example, when a collagen dispersion is prepared by mechanical pulverization after completion of the pretreatment of the present invention, a collagen dispersion with long fibers can be obtained.
前処理された魚皮は着色、臭いを持つこともなく、魚皮より表皮、真皮を分離する作業も不要となり容易に魚類由来のコラーゲンを利用することができる。
本発明によって得られた魚皮は乾燥後、あるいはそのままで目的の用途、形状に成形、調製される。例えばこの魚皮を機械的に粉砕しコラーゲン分散液を調製できる。これを用いてコーティング液、凍結乾燥の原液等の用途を挙げることができる。更に具体的には化粧品原料、化粧用スポンジ、生化学実験用材料、医療用途のスポンジ等の用途に用いることが可能である。
The pretreated fish skin does not have coloring and odor, and it is not necessary to separate the epidermis and dermis from the fish skin, so that collagen derived from fish can be used easily.
The fish skin obtained by the present invention is molded and prepared into the intended use and shape after drying or as it is. For example, this fish skin can be mechanically pulverized to prepare a collagen dispersion. This can be used for applications such as coating solutions and lyophilized stock solutions. More specifically, it can be used for cosmetic raw materials, cosmetic sponges, biochemical laboratory materials, medical use sponges, and the like.
以下に実施例により本発明を詳細に説明する。
実施例1
食用に魚肉を取り除かれた生皮(魚皮)1kg(イズミダイ)に対し、水1.1kgとイソプロパノール1.5kgを加え、魚皮に良く浸透させる。次に30w/v%NaOH溶液を185mlと30%H2O2を150ml加え25℃で1〜3日振盪する。
この処理により色が抜けていることを確認後、クエン酸と塩酸を併用してpHを5.0に調製する。ここにNaHSO3を適当量加えて残存しているH2O2を分解する。なお過酸化水素検出試薬にて、H2O2の残留を確認することが可能である。処理の終わった生皮をpH5.0の塩酸水もしくはクエン酸/クエン酸Na希釈液で洗浄し魚皮の前処理を終了する。得られた魚皮は色、臭いが無いコラーゲン材料であって、本魚皮を機械的に粉砕することでコラーゲン分散液を調製することが可能となる。
Hereinafter, the present invention will be described in detail by way of examples.
Example 1
Add 1 kg of water and 1.5 kg of isopropanol to 1 kg of raw skin (fish skin) from which fish meat has been removed for consumption, and infiltrate the fish skin well. Next, 185 ml of 30 w / v% NaOH solution and 150 ml of 30% H 2 O 2 are added and shaken at 25 ° C. for 1 to 3 days.
After confirming that the color has disappeared by this treatment, the pH is adjusted to 5.0 using citric acid and hydrochloric acid in combination. An appropriate amount of NaHSO 3 is added thereto to decompose the remaining H 2 O 2 . In addition, it is possible to confirm the residue of H 2 O 2 with a hydrogen peroxide detection reagent. The treated rawhide is washed with pH 5.0 hydrochloric acid water or citric acid / Na-citrate diluted solution to finish the fish skin pretreatment. The obtained fish skin is a collagen material having no color and no odor, and a collagen dispersion can be prepared by mechanically grinding the fish skin.
実施例2
食用に魚肉を取り除かれた生皮(魚皮)1kg(イズミダイ)に0.5%重曹水3Lを加え、ビオブラーゼSP−15FG(アルカリプロテアーゼ、ナガセケムテックス)を1.5g加え、よく揉み込んでから25℃で2〜3時間振盪する。次にホウ素化水素ナトリウムを0.9g加える25℃で30分以上振盪する。処理終了後、魚皮をよく水洗する。この魚皮に水1.1kgとイソプロパノール1.5kgを加え、よく浸透させる。次に30w/v%NaOHを185mlと30%H2O2を12.7ml加え25℃で2〜4日振盪する。これ以降は実施例1と同様に処理し色、臭いが無い魚皮を得ることができる。
得られたコラーゲン分散液を凍結乾燥することによってコラーゲンスポンジを得ることができる。
またこのスポンジをプレスする事でコラーゲンシートを得る。
分散液をトレーに薄く広げそのまま風乾する事で、コラーゲンフィルムを得ることができる。また同様の方法によって容器内面にコラーゲンコートを行うことができる。
Example 2
Add 1 liter of 0.5% sodium bicarbonate water to 1 kg of raw skin (fish skin) from which fish meat has been removed for consumption (Izumimidai), add 1.5 g of biolase SP-15FG (alkaline protease, Nagase ChemteX), and swallow well. Shake at 25 ° C. for 2-3 hours. Next, 0.9 g of sodium borohydride is added and shaken at 25 ° C. for 30 minutes or more. After finishing the treatment, wash the fish skin thoroughly. Add 1.1 kg of water and 1.5 kg of isopropanol to the fish skin and infiltrate well. Next, 185 ml of 30 w / v% NaOH and 12.7 ml of 30% H 2 O 2 are added and shaken at 25 ° C. for 2 to 4 days. Thereafter, the same processing as in Example 1 can be performed to obtain a fish skin having no color and no smell.
A collagen sponge can be obtained by freeze-drying the obtained collagen dispersion.
Moreover, a collagen sheet is obtained by pressing this sponge.
A collagen film can be obtained by spreading the dispersion thinly on a tray and air-drying it as it is. A collagen coating can be applied to the inner surface of the container by the same method.
Claims (3)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2005026842A JP4738005B2 (en) | 2005-02-02 | 2005-02-02 | Fish skin pretreatment method |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2005026842A JP4738005B2 (en) | 2005-02-02 | 2005-02-02 | Fish skin pretreatment method |
Publications (2)
Publication Number | Publication Date |
---|---|
JP2006213624A JP2006213624A (en) | 2006-08-17 |
JP4738005B2 true JP4738005B2 (en) | 2011-08-03 |
Family
ID=36977153
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2005026842A Active JP4738005B2 (en) | 2005-02-02 | 2005-02-02 | Fish skin pretreatment method |
Country Status (1)
Country | Link |
---|---|
JP (1) | JP4738005B2 (en) |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN108314726A (en) * | 2018-04-28 | 2018-07-24 | 贵阳学院 | A kind of giant salamander collagen extracting method and the collagen product extracted by this method |
CN110054683A (en) * | 2019-04-24 | 2019-07-26 | 青岛科技大学 | A kind of extraction pre-treating method of Java tilapia skin macromolecular collagen |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2008104398A (en) * | 2006-10-25 | 2008-05-08 | Nippi:Kk | Low-temperature gelling gelatin |
CN101942204B (en) * | 2010-09-16 | 2012-09-05 | 集美大学 | Production method of collagen membrane |
JP6265350B2 (en) * | 2016-06-03 | 2018-01-24 | 有限会社松下海産 | Extraction method of collagen and gelatin |
CN113201064A (en) * | 2020-10-09 | 2021-08-03 | 海南翔泰生物科技有限公司 | Method for preparing fish skin collagen powder from fresh fish skin |
Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH03209395A (en) * | 1988-08-04 | 1991-09-12 | Univ Bar Ilan | Production of gelatin from fish skin |
JP2000050811A (en) * | 1998-08-11 | 2000-02-22 | Ihara Suisan Kk | Production of collagen of fishes |
JP2000189065A (en) * | 1998-12-31 | 2000-07-11 | Skw Biosystems | Production of fish gelatin |
JP2000256398A (en) * | 1999-03-09 | 2000-09-19 | Katakura Chikkarin Co Ltd | Collagen originated from fish skin and cosmetic containing the collagen |
JP2001508301A (en) * | 1997-01-13 | 2001-06-26 | ノバ ジェン,インコーポレーテッド | Preparation of collagen |
JP2004505622A (en) * | 2000-07-28 | 2004-02-26 | コンセホ・スペリオール・デ・インベスティガシオネス・シエンティフィカス | Process for the production of gelatin of marine origin and the products so obtained. |
JP2004141007A (en) * | 2002-10-22 | 2004-05-20 | Nippon Suisan Kaisha Ltd | Method for producing gelatine peptide derived from fish |
-
2005
- 2005-02-02 JP JP2005026842A patent/JP4738005B2/en active Active
Patent Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH03209395A (en) * | 1988-08-04 | 1991-09-12 | Univ Bar Ilan | Production of gelatin from fish skin |
JP2001508301A (en) * | 1997-01-13 | 2001-06-26 | ノバ ジェン,インコーポレーテッド | Preparation of collagen |
JP2000050811A (en) * | 1998-08-11 | 2000-02-22 | Ihara Suisan Kk | Production of collagen of fishes |
JP2000189065A (en) * | 1998-12-31 | 2000-07-11 | Skw Biosystems | Production of fish gelatin |
JP2000256398A (en) * | 1999-03-09 | 2000-09-19 | Katakura Chikkarin Co Ltd | Collagen originated from fish skin and cosmetic containing the collagen |
JP2004505622A (en) * | 2000-07-28 | 2004-02-26 | コンセホ・スペリオール・デ・インベスティガシオネス・シエンティフィカス | Process for the production of gelatin of marine origin and the products so obtained. |
JP2004141007A (en) * | 2002-10-22 | 2004-05-20 | Nippon Suisan Kaisha Ltd | Method for producing gelatine peptide derived from fish |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN108314726A (en) * | 2018-04-28 | 2018-07-24 | 贵阳学院 | A kind of giant salamander collagen extracting method and the collagen product extracted by this method |
CN108314726B (en) * | 2018-04-28 | 2020-10-30 | 贵阳学院 | Giant salamander skin collagen extraction method and collagen product extracted by same |
CN110054683A (en) * | 2019-04-24 | 2019-07-26 | 青岛科技大学 | A kind of extraction pre-treating method of Java tilapia skin macromolecular collagen |
Also Published As
Publication number | Publication date |
---|---|
JP2006213624A (en) | 2006-08-17 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
AU768832B2 (en) | Process for the preparation of fish gelatin | |
JP5250382B2 (en) | Tannery pre-treatment method and tannery method | |
KR100381741B1 (en) | Collagen product containing collagen of marine origin with a low odor and with improved mechanical properties, and its use in the form of cosmetic or pharmaceutical compositions or products | |
JP2001234128A (en) | Method for manufacturing collagenous film from pig skin | |
JP4738005B2 (en) | Fish skin pretreatment method | |
Saranya et al. | Value addition of fish waste in the leather industry for dehairing | |
PT2179065E (en) | Method of preserving hides and skins | |
FR2501717A1 (en) | METHOD OF PROTECTING THE ENVIRONMENT FOR LIMITING RAW SKINS | |
KR101572919B1 (en) | Natural dyes for leather tanning methods | |
RU2425893C2 (en) | Method to produce tanned half stuff from skin of all kinds of fresh-water fish | |
US4548608A (en) | Depilating composition and method | |
US20080175976A1 (en) | Gelatin Production System | |
JP2005343851A (en) | Peptide derived from fishes and method for producing the same | |
JP3979576B2 (en) | Production method of raw skin to obtain non-brominated collagen and gelatin derived from aquatic animals | |
US4581148A (en) | Depilating composition and method | |
RU2375385C1 (en) | Method of producing protein hydrolysate | |
FR2468649A1 (en) | PROCESS FOR THE REVERDISSAGE OF SKINS IN HAIR OR DEPILED | |
WO1992011391A1 (en) | Method for processing hides or leather, tanning agents and method for manufacturing same | |
CN114787390A (en) | Method for unhairing and liming skins, hides or furs | |
NL2027083B1 (en) | Process for deliming of hides, skins or pelts | |
CN108998588A (en) | A kind of processing method of primate sample hide | |
US1974889A (en) | Preparation of hides or skins for tanning | |
JP2020531637A (en) | How to lick animal skin | |
KR20030006871A (en) | Method for preparation of leather using protease and method for treatment of wastes derived from leather production process using the same | |
RU2222601C1 (en) | Rawstock treatment method |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20080204 |
|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20110105 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20110304 |
|
TRDD | Decision of grant or rejection written | ||
A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20110419 |
|
A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20110426 |
|
R150 | Certificate of patent or registration of utility model |
Ref document number: 4738005 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20140513 Year of fee payment: 3 |
|
S531 | Written request for registration of change of domicile |
Free format text: JAPANESE INTERMEDIATE CODE: R313531 |
|
R360 | Written notification for declining of transfer of rights |
Free format text: JAPANESE INTERMEDIATE CODE: R360 |
|
R360 | Written notification for declining of transfer of rights |
Free format text: JAPANESE INTERMEDIATE CODE: R360 |
|
R371 | Transfer withdrawn |
Free format text: JAPANESE INTERMEDIATE CODE: R371 |
|
S531 | Written request for registration of change of domicile |
Free format text: JAPANESE INTERMEDIATE CODE: R313531 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R360 | Written notification for declining of transfer of rights |
Free format text: JAPANESE INTERMEDIATE CODE: R360 |
|
R370 | Written measure of declining of transfer procedure |
Free format text: JAPANESE INTERMEDIATE CODE: R370 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |