JPS62269689A - Method for stabilizing enzyme - Google Patents
Method for stabilizing enzymeInfo
- Publication number
- JPS62269689A JPS62269689A JP10956786A JP10956786A JPS62269689A JP S62269689 A JPS62269689 A JP S62269689A JP 10956786 A JP10956786 A JP 10956786A JP 10956786 A JP10956786 A JP 10956786A JP S62269689 A JPS62269689 A JP S62269689A
- Authority
- JP
- Japan
- Prior art keywords
- enzyme
- acid
- inhibitor
- detergents
- stabilization method
- 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.)
- Granted
Links
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 46
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 46
- 238000000034 method Methods 0.000 title claims description 12
- 230000000087 stabilizing effect Effects 0.000 title description 6
- 230000006641 stabilisation Effects 0.000 claims abstract description 11
- 238000011105 stabilization Methods 0.000 claims abstract description 11
- 108091005804 Peptidases Proteins 0.000 claims abstract description 7
- 239000004365 Protease Substances 0.000 claims abstract description 6
- 230000002401 inhibitory effect Effects 0.000 claims abstract description 5
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract 3
- 159000000007 calcium salts Chemical class 0.000 claims description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 6
- 239000002532 enzyme inhibitor Substances 0.000 claims description 5
- 230000002441 reversible effect Effects 0.000 claims description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 claims description 4
- 229940125532 enzyme inhibitor Drugs 0.000 claims description 4
- GRYLNZFGIOXLOG-UHFFFAOYSA-N Nitric acid Chemical compound O[N+]([O-])=O GRYLNZFGIOXLOG-UHFFFAOYSA-N 0.000 claims description 2
- BVKZGUZCCUSVTD-UHFFFAOYSA-N carbonic acid Chemical compound OC(O)=O BVKZGUZCCUSVTD-UHFFFAOYSA-N 0.000 claims description 2
- 229910017604 nitric acid Inorganic materials 0.000 claims description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 claims 2
- 229910000147 aluminium phosphate Inorganic materials 0.000 claims 1
- 150000001768 cations Chemical class 0.000 claims 1
- 229920000137 polyphosphoric acid Polymers 0.000 claims 1
- 150000003839 salts Chemical class 0.000 claims 1
- 239000003599 detergent Substances 0.000 abstract description 25
- 239000000203 mixture Substances 0.000 abstract description 7
- MRXDGVXSWIXTQL-HYHFHBMOSA-N (2s)-2-[[(1s)-1-(2-amino-1,4,5,6-tetrahydropyrimidin-6-yl)-2-[[(2s)-4-methyl-1-oxo-1-[[(2s)-1-oxo-3-phenylpropan-2-yl]amino]pentan-2-yl]amino]-2-oxoethyl]carbamoylamino]-3-phenylpropanoic acid Chemical compound C([C@H](NC(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C=O)C1NC(N)=NCC1)C(O)=O)C1=CC=CC=C1 MRXDGVXSWIXTQL-HYHFHBMOSA-N 0.000 abstract description 5
- OLVPQBGMUGIKIW-UHFFFAOYSA-N Chymostatin Natural products C=1C=CC=CC=1CC(C=O)NC(=O)C(C(C)CC)NC(=O)C(C1NC(N)=NCC1)NC(=O)NC(C(O)=O)CC1=CC=CC=C1 OLVPQBGMUGIKIW-UHFFFAOYSA-N 0.000 abstract description 5
- OSGAYBCDTDRGGQ-UHFFFAOYSA-L calcium sulfate Chemical compound [Ca+2].[O-]S([O-])(=O)=O OSGAYBCDTDRGGQ-UHFFFAOYSA-L 0.000 abstract description 5
- 108010086192 chymostatin Proteins 0.000 abstract description 5
- 239000013037 reversible inhibitor Substances 0.000 abstract description 5
- 108010056079 Subtilisins Proteins 0.000 abstract description 3
- 102000005158 Subtilisins Human genes 0.000 abstract description 3
- 238000002156 mixing Methods 0.000 abstract description 3
- 239000003513 alkali Substances 0.000 abstract 1
- 229940088598 enzyme Drugs 0.000 description 39
- 239000003112 inhibitor Substances 0.000 description 14
- 230000000694 effects Effects 0.000 description 8
- 102000035195 Peptidases Human genes 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 108091005658 Basic proteases Proteins 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- 108090000787 Subtilisin Proteins 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- 239000003945 anionic surfactant Substances 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 230000009849 deactivation Effects 0.000 description 2
- 239000010985 leather Substances 0.000 description 2
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 2
- 108010052968 leupeptin Proteins 0.000 description 2
- 239000002075 main ingredient Substances 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 229910052938 sodium sulfate Inorganic materials 0.000 description 2
- 235000011152 sodium sulphate Nutrition 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- RRONHWAVOYADJL-HNNXBMFYSA-N (2s)-3-phenyl-2-(phenylmethoxycarbonylamino)propanoic acid Chemical compound C([C@@H](C(=O)O)NC(=O)OCC=1C=CC=CC=1)C1=CC=CC=C1 RRONHWAVOYADJL-HNNXBMFYSA-N 0.000 description 1
- DLFSPRHQGAULBQ-UHFFFAOYSA-N 1,1-dibenzylurea Chemical compound C=1C=CC=CC=1CN(C(=O)N)CC1=CC=CC=C1 DLFSPRHQGAULBQ-UHFFFAOYSA-N 0.000 description 1
- 108010087765 Antipain Proteins 0.000 description 1
- 101100311270 Arabidopsis thaliana STI gene Proteins 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 101100124982 Glycine max HOP1 gene Proteins 0.000 description 1
- 239000005909 Kieselgur Substances 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 108700018667 Streptomyces subtilisin inhibitor Proteins 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 description 1
- SDNYTAYICBFYFH-TUFLPTIASA-N antipain Chemical compound NC(N)=NCCC[C@@H](C=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 SDNYTAYICBFYFH-TUFLPTIASA-N 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000009990 desizing Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- KTUFNOKKBVMGRW-UHFFFAOYSA-N imatinib Chemical compound C1CN(C)CCN1CC1=CC=C(C(=O)NC=2C=C(NC=3N=C(C=CN=3)C=3C=NC=CC=3)C(C)=CC=2)C=C1 KTUFNOKKBVMGRW-UHFFFAOYSA-N 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- HXITXNWTGFUOAU-UHFFFAOYSA-N phenylboronic acid Chemical compound OB(O)C1=CC=CC=C1 HXITXNWTGFUOAU-UHFFFAOYSA-N 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000009991 scouring Methods 0.000 description 1
- 235000019812 sodium carboxymethyl cellulose Nutrition 0.000 description 1
- 235000019832 sodium triphosphate Nutrition 0.000 description 1
- 239000004753 textile Substances 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical class [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
Landscapes
- Enzymes And Modification Thereof (AREA)
- Detergent Compositions (AREA)
Abstract
Description
【発明の詳細な説明】
３、発明の詳細な説明
［産業上の利用分野］
この発明は酵素の安定化法、詳しく言えば待に洗剤中の
プロテアーゼの安定化法に関するものである。[Detailed Description of the Invention] 3. Detailed Description of the Invention [Field of Industrial Application] This invention relates to a method for stabilizing enzymes, and more specifically, to a method for stabilizing proteases in detergents.
［従来の技術］
近年、通常の洗剤のみでは充分に洗浄することができな
い生体の蛋白質（垢、血液等）に由来する汚れを洗浄す
る目的で、酵素の蛋白分解作用を加味した酵素入り洗剤
が脚光を浴びている。[Prior Art] In recent years, enzyme-containing detergents that incorporate the proteolytic action of enzymes have been developed for the purpose of cleaning stains originating from biological proteins (dirt, blood, etc.) that cannot be adequately cleaned with ordinary detergents alone. is in the spotlight.
酵素入り洗剤は、一般の洗剤基材、例えばアニオン系界
面活性剤を洗剤主剤とし、ビルダーとしてトリポリ燐酸
ナトリウム、硫酸ナトリウム、カルボキシメチルセルロ
ース、ケイソウ土等を添加したものに酵素を配合したも
のである。酵素としては一般に洗剤水溶液のＤＨ条件下
で活性なアルカリプロテアーゼが使用されている。Enzyme-containing detergents are made by blending enzymes into general detergent base materials, such as anionic surfactants as the detergent main ingredient, with added builders such as sodium tripolyphosphate, sodium sulfate, carboxymethyl cellulose, and diatomaceous earth. As the enzyme, alkaline protease, which is active under the DH conditions of an aqueous detergent solution, is generally used.
［発明が解決しようとする問題点］
洗剤の主剤であるアニオン系界面活性剤は、酵素の部分
的失活を招き、酵素の安定性を弱める傾向がある等の好
ましくない性質を伴なっており、このため実用上は保存
時の活性低下をできるだけ少なくすることが望まれ、種
々の安定化法か提案されている。[Problems to be solved by the invention] Anionic surfactants, which are the main ingredients of detergents, have undesirable properties such as partial deactivation of enzymes and a tendency to weaken the stability of enzymes. Therefore, in practice, it is desirable to minimize the decrease in activity during storage, and various stabilization methods have been proposed.
酵素は通常乾燥状態では安定であるため、粒剤とした場
合には比較的容易に安定化できるが、水の存在下では不
安定となりやすく、特に液体洗剤の場合には種々の提案
にもかかわらず充分な解決には至っていないのが実情で
ある。Enzymes are normally stable in a dry state, so they can be stabilized relatively easily when made into granules, but they tend to become unstable in the presence of water, and despite various proposals, this is especially true in the case of liquid detergents. The reality is that no satisfactory solution has yet been reached.
Ｅ問題点を解決するための手段］
本発明者は、各種洗剤に配合される酵素の失活を抑制す
る化合物を探索し、酵素に対してその可逆的阻害剤を結
合させた場合には溶液および粉末状態において酵素の安
定性が向上することを見出し、本発明を完成した。Means for Solving Problem E] The present inventor searched for a compound that inhibits the deactivation of enzymes that are blended into various detergents, and found that when a reversible inhibitor is bound to the enzyme, the solution The present invention was completed based on the discovery that the stability of the enzyme is improved when it is in a powdered state.
すなわち、本発明は酵素の可逆的阻害剤を酵素に対して
０．５当量から使用条件下で実際上阻害効果を示さない
範囲までの量添加することを特徴とする酵素の安定化法
を提供したものである。That is, the present invention provides a method for stabilizing an enzyme, which comprises adding a reversible enzyme inhibitor in an amount ranging from 0.5 equivalents to a range that does not actually exhibit an inhibitory effect under the conditions of use. This is what I did.
本発明の酵素安定化法においては、酵素の可逆的阻害剤
として一般に知られているものが使用可能であるが、特
にキモスタチン、ロイペプチン、アンチパイン、ホスホ
ラミトン等のペプチド性低分子量阻害剤、大豆トリプシ
ンインヒビター（以下、ＳＴＩと略す。）、ストレプト
マイセススブチリシンインヒビター、オポインヒビター
等のタンパク性高分子但阻害剤、およびカルボベンジル
オキシフエールアラニン（以下、Ｚ−Ｐｈｅと略す。）
、フェニルホウ酸、Ｎ、Ｎ−ジベンジル尿素等の非生物
起源で酵素の可逆的阻害作用のある化合物か洗剤中の酵
素の安定化にすぐれた効果を示し、これらを酵素ととも
に洗剤に添加した場合に酵素と阻害剤が複合体を形成し
活性が長時間持続し、酵素活性の低下が少なく、酵素入
り洗剤として十分に実用化できることを見出した。In the enzyme stabilization method of the present invention, generally known reversible inhibitors of enzymes can be used, and in particular, peptidic low molecular weight inhibitors such as chymostatin, leupeptin, antipain, phosphoramitone, soybean trypsin, etc. inhibitor (hereinafter abbreviated as STI), Streptomyces subtilisin inhibitor, proteinaceous polymer inhibitors such as opoinhibitor, and carbobenzyloxyphealalanine (hereinafter abbreviated as Z-Phe).
, phenylboric acid, N,N-dibenzylurea, and other non-biological compounds that have a reversible inhibitory effect on enzymes have shown excellent effects in stabilizing enzymes in detergents, and when added to detergents together with enzymes, It was discovered that the enzyme and inhibitor form a complex, the activity lasts for a long time, there is little decrease in enzyme activity, and it can be put to practical use as an enzyme-containing detergent.
洗剤用として使用される蛋白分解酵素（プロテアーゼ）
には種々のものがあり、工業的資源として、食品工業、
皮革工業、医薬品工業、繊維工業、水産加工業などの各
方面において用いられているプロテアーゼはいずれも使
用可能でおるが、特に洗剤水溶液のアルカリ性条件下で
活性なアルカリプロテアーゼ、例えばスブチリシン・カ
ールスベルグ（Ｓｕｂｔｉｌｉｓｉｎ Ｃａｒｌｓｂｅ
ｒｇ） 、スブチリシンＢＰＮ （以下ＢＰＮと略記
する。） 、ＡＰＩ−２１等が適している。Proteolytic enzymes (proteases) used for detergents
There are various types of resources, including the food industry,
All proteases used in various fields such as the leather industry, pharmaceutical industry, textile industry, and fisheries processing industry can be used, but alkaline proteases that are particularly active under the alkaline conditions of aqueous detergent solutions, such as subtilisin Carlsberg ( Subtilisin Carlsbe
rg), subtilisin BPN (hereinafter abbreviated as BPN), API-21, etc. are suitable.
本発明では、酵素の可逆的阻害剤に加えて、更にカルシ
ウム塩、例えば酢酸、硫酸、炭酸、塩酸、硝酸および燐
酸のカルシウム塩、好ましくは硫酸カルシウム塩を併用
することにより、酵素の保存安定性を一層向上させるこ
とができる。In the present invention, in addition to a reversible enzyme inhibitor, calcium salts such as acetic acid, sulfuric acid, carbonic acid, hydrochloric acid, nitric acid, and phosphoric acid calcium salts, preferably calcium sulfate salts, are used in combination to improve the storage stability of the enzyme. can be further improved.
本発明の酵素安定化法で用いる酵素の可逆的阻害剤の添
加量は、保存状態では阻害剤として有効に動き、希釈さ
れた実使用条件下では実際上阻害効果を示さない濃度で
あり、例えば酵素としてＡＩＩ’−２１、阻害剤として
キモスタチンを組合わせた場合、酵素に対して０．５当
量以上から、実使用条件下での酵素阻害剤濃度が１μＭ
以下となる範囲の岳である。 −
また、安定化助剤でおるカルシウム塩は、酵素に対して
０〜４０重量％添加して用いるのが好ましい。The amount of the enzyme reversible inhibitor used in the enzyme stabilization method of the present invention is such that it acts effectively as an inhibitor under storage conditions, but does not actually show an inhibitory effect under diluted conditions of actual use. When combining AII'-21 as the enzyme and chymostatin as the inhibitor, the concentration of the enzyme inhibitor under actual use conditions is 1 μM from 0.5 equivalent or more to the enzyme.
The mountain range is as follows. - Moreover, it is preferable to use calcium salt, which is a stabilizing aid, in an amount of 0 to 40% by weight relative to the enzyme.
本発明による酵素の安定化は、具体的には酵素と酵素の
可逆的阻害剤を混合し、醇素−阻害剤複合体を形成し、
更に所望によりカルシウム塩を加えて安定化された酵素
組成物とすることにより行なわれる。このようにして得
られる安定化された組成物は、これを洗剤用またはその
他の用途、例えば絹精練、皮革加工、衣料のり抜き等に
用いることができる。Specifically, stabilization of an enzyme according to the present invention involves mixing an enzyme and a reversible inhibitor of the enzyme to form a sulfur-inhibitor complex,
Further, if desired, a calcium salt may be added to obtain a stabilized enzyme composition. The stabilized composition thus obtained can be used in detergents or other applications such as silk scouring, leather processing, clothing desizing, etc.
［実施例］
以下、実施例によって本発明の酵素安定化法の効果を、
粉末洗剤および液体洗剤の場合につき具体的に説明する
。[Example] Hereinafter, the effects of the enzyme stabilization method of the present invention will be explained using Examples.
The case of powder detergent and liquid detergent will be specifically explained.
（１）′Ｉ９Ｊ末洗剤
酵素（ＢＰＮ’） ０．０５ｇと、表１に示すような阻
害剤／酵素当量比となる量の阻害剤（キモスタチンおよ
び１−Ｐｈｅ ）および硫酸ナトリウムの混合物とを容
器にとり、よく混合し、これに洗剤（市販洗剤二ニュー
ビーズ）５ｇを加え混合し、温度４０°Ｃ１相対湿度８
０％の恒温恒湿槽に入れて４０時間後、１１０時間後お
よび１６０時間後に各試料の酵素の残存活性を測定しく
特公昭６０−５５１１８号参照）、表１に示す結果を得
た。表１には硫酸カルシウムを添加した場合および比較
のために阻害剤を使用しない場合の結果をも示した。(1) 0.05 g of 'I9J powder detergent enzyme (BPN') and a mixture of inhibitors (chymostatin and 1-Phe) and sodium sulfate in an amount that gives the inhibitor/enzyme equivalent ratio shown in Table 1 are placed in a container. Mix well, add 5g of detergent (commercially available detergent Ninu Beads) and mix. Temperature: 40°C, relative humidity: 8.
The residual enzyme activity of each sample was measured 40 hours, 110 hours and 160 hours after being placed in a 0% constant temperature and humidity chamber (see Japanese Patent Publication No. 55118/1983), and the results shown in Table 1 were obtained. Table 1 also shows the results when calcium sulfate was added and for comparison, the results when no inhibitor was used.
（２）液体洗剤
ＬＡＳ １０重ｆｆｉ％、アルコキシエトキシレート３
３重量％、トリエタノールアミン８重量％、エタノール
８重Ｈ％および水４１重量％からなる液体洗剤３０ｒｎ
ｌに、酵素（８ＰＮおよびトリプシン） ３０ｍ＝Ｊと
、表２に示すような阻害剤／酵素当量比となるｍの阻害
剤（キモスタチン、ロイペプチン、ＳＴＩ ）を加え、
よく混合し、温度４５℃の恒温槽に入れて４８時間後、
９０時間後および１８７時間後に各試料の酵素残存活性
を測定し、表２に示す結果を得た。表２には比較のため
に阻害剤を使用しない場合の結果をも示した。(2) Liquid detergent LAS 10% ffi, alkoxyethoxylate 3
Liquid detergent 30rn consisting of 3% by weight, 8% by weight of triethanolamine, 8% by weight of ethanol and 41% by weight of water.
1, add enzyme (8PN and trypsin) 30m=J and m inhibitors (chymostatin, leupeptin, STI) with an inhibitor/enzyme equivalent ratio as shown in Table 2,
Mix well and place in a constant temperature bath at 45°C for 48 hours.
The residual enzyme activity of each sample was measured after 90 hours and 187 hours, and the results shown in Table 2 were obtained. Table 2 also shows the results when no inhibitor was used for comparison.
表１および表２から、酵素阻害剤を用いることによって
洗剤中での酵素の安定性か向上することが明らかであり
、その効果はカルシウム塩の添加により一層顕著となっ
ている。From Tables 1 and 2, it is clear that the use of enzyme inhibitors improves the stability of enzymes in detergents, and the effect is even more pronounced with the addition of calcium salts.
Claims (1)
ら使用条件下で実際上阻害効果を示さない範囲までの量
添加することを特徴とする酵素の安定化法。 ２）酵素がプロテアーゼである特許請求の範囲第１項に
記載の安定化法。 ３）更にカルシウム塩を、酵素に対して４０重量％まで
の量添加する特許請求の範囲第１項または第２項に記載
の安定化法。 ４）カルシウム塩が、酢酸、硫酸、炭酸、塩酸、硝酸、
燐酸、およびポリ燐酸のカルシウム塩から選ばれる少な
くとも１種類以上の塩である特許請求の範囲第３項に記
載の安定化法。[Claims] 1) Enzyme stabilization characterized by adding a reversible enzyme inhibitor in an amount ranging from 0.5 equivalents to a range that does not actually show an inhibitory effect under the conditions of use. cation law. 2) The stabilization method according to claim 1, wherein the enzyme is a protease. 3) The stabilization method according to claim 1 or 2, wherein a calcium salt is further added in an amount of up to 40% by weight based on the enzyme. 4) Calcium salts include acetic acid, sulfuric acid, carbonic acid, hydrochloric acid, nitric acid,
The stabilization method according to claim 3, wherein the stabilization method is at least one salt selected from phosphoric acid and calcium salts of polyphosphoric acid.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61109567A JPH0657151B2 (en) | 1986-05-15 | 1986-05-15 | Enzyme stabilization method |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61109567A JPH0657151B2 (en) | 1986-05-15 | 1986-05-15 | Enzyme stabilization method |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS62269689A true JPS62269689A (en) | 1987-11-24 |
| JPH0657151B2 JPH0657151B2 (en) | 1994-08-03 |
Family
ID=14513515
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP61109567A Expired - Lifetime JPH0657151B2 (en) | 1986-05-15 | 1986-05-15 | Enzyme stabilization method |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0657151B2 (en) |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH01502957A (en) * | 1987-04-10 | 1989-10-12 | アムジエン・インコーポレーテツド | subtilisin analog |
| EP0640687A1 (en) * | 1993-08-27 | 1995-03-01 | Holland Sweetener Company V.O.F. | Methods of using, storing and transporting metal protease enzyme in a stabilized form |
| US5527487A (en) * | 1991-11-27 | 1996-06-18 | Novo Nordisk A/S | Enzymatic detergent composition and method for enzyme stabilization |
| WO1998013459A1 (en) * | 1996-09-24 | 1998-04-02 | The Procter & Gamble Company | Liquid detergents containing proteolytic enzyme, peptide aldehyde and calcium ions |
| EP0968707A2 (en) * | 1998-07-03 | 2000-01-05 | Beiersdorf Aktiengesellschaft | Compositions against acne and inflamed comedones containing serine proteases and one or more calcium salts |
| JP2013192526A (en) * | 2012-03-22 | 2013-09-30 | Sanyo Chem Ind Ltd | Protein solution, method for restoring protease activity of protein solution, and detergent composition containing the same protein solution |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5913187A (en) * | 1982-07-13 | 1984-01-23 | 松下冷機株式会社 | Vacuum heat-insulating composite body and its manufacture |
-
1986
- 1986-05-15 JP JP61109567A patent/JPH0657151B2/en not_active Expired - Lifetime
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5913187A (en) * | 1982-07-13 | 1984-01-23 | 松下冷機株式会社 | Vacuum heat-insulating composite body and its manufacture |
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH01502957A (en) * | 1987-04-10 | 1989-10-12 | アムジエン・インコーポレーテツド | subtilisin analog |
| US5527487A (en) * | 1991-11-27 | 1996-06-18 | Novo Nordisk A/S | Enzymatic detergent composition and method for enzyme stabilization |
| EP0640687A1 (en) * | 1993-08-27 | 1995-03-01 | Holland Sweetener Company V.O.F. | Methods of using, storing and transporting metal protease enzyme in a stabilized form |
| US5739023A (en) * | 1993-08-27 | 1998-04-14 | Holland Sweetener Company V.O.F. | Stabilized neutral metalloprotease composition, a method of making the composition, and a method of transporting the composition |
| KR100326477B1 (en) * | 1993-08-27 | 2002-07-04 | 비그만 피. | How to use, store and transport metal protease enzymes in stabilized form |
| WO1998013459A1 (en) * | 1996-09-24 | 1998-04-02 | The Procter & Gamble Company | Liquid detergents containing proteolytic enzyme, peptide aldehyde and calcium ions |
| EP0968707A2 (en) * | 1998-07-03 | 2000-01-05 | Beiersdorf Aktiengesellschaft | Compositions against acne and inflamed comedones containing serine proteases and one or more calcium salts |
| EP0968707A3 (en) * | 1998-07-03 | 2003-08-13 | Beiersdorf Aktiengesellschaft | Compositions against acne and inflamed comedones containing serine proteases and one or more calcium salts |
| JP2013192526A (en) * | 2012-03-22 | 2013-09-30 | Sanyo Chem Ind Ltd | Protein solution, method for restoring protease activity of protein solution, and detergent composition containing the same protein solution |
Also Published As
| Publication number | Publication date |
|---|---|
| JPH0657151B2 (en) | 1994-08-03 |
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