JPH08266281A - Mussel adhesive protein gene - Google Patents
Mussel adhesive protein geneInfo
- Publication number
- JPH08266281A JPH08266281A JP7075210A JP7521095A JPH08266281A JP H08266281 A JPH08266281 A JP H08266281A JP 7075210 A JP7075210 A JP 7075210A JP 7521095 A JP7521095 A JP 7521095A JP H08266281 A JPH08266281 A JP H08266281A
- Authority
- JP
- Japan
- Prior art keywords
- mussel
- amino acid
- acid sequence
- adhesive
- protein
- 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.)
- Pending
Links
Landscapes
- Peptides Or Proteins (AREA)
- Adhesives Or Adhesive Processes (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
Abstract
Description
【０００１】[0001]
【産業上の利用分野】本発明は水中や湿潤な環境で使用
できる接着剤の原料となるペプチドを組換えＤＮＡ技術
を用いて製造するために用いるＤＮＡに関する。接着蛋
白質をコードするＤＮＡを組み込んだ組換え体ＤＮＡを
含む微生物や培養細胞を培養液中で培養し、該培養物中
に蓄積される該ポリペプチドを採集することにより、得
られる該ペプチドは、接着剤の原料として広い用途で利
用されることが期待される。BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a DNA used for producing a peptide as a raw material of an adhesive which can be used in water or a moist environment by using recombinant DNA technology. The peptide obtained by culturing a microorganism or a cultured cell containing a recombinant DNA incorporating a DNA encoding an adhesion protein in a culture medium and collecting the polypeptide accumulated in the culture, It is expected to be used in a wide range of applications as a raw material for adhesives.
【０００２】[0002]
【従来の技術】乾燥条件下で強い接着力を示す接着剤は
様々な種類のものが開発されている。そのうちの多くの
ものは一旦乾燥条件下で接着してしまえば湿潤環境にお
かれてもその強度を維持できる。しかし、湿潤な条件下
や水中で接着を開始した場合、有効な強度に達すること
ができる接着剤は存在しなかった。2. Description of the Related Art Various types of adhesives have been developed which exhibit strong adhesiveness under dry conditions. Many of them can maintain their strength even in a humid environment once they are bonded under dry conditions. However, no adhesive was able to reach effective strength when the adhesion was initiated under moist conditions or in water.
【０００３】イガイ類は自己を良好な環境に固定するた
めに接着蛋白質を合成して自己を基物に接着させること
ができる。この接着蛋白質はムラサキイガイにおいては
主として数十個のAla-Lys-Pro-Ser-Tyr-Pro-Pro-Thr-Ty
r-Lys という10アミノ酸からなる配列の繰り返しにより
構成されており、海水中で硬化して十分な接着強度に達
することができることが知られている（J.H.Waite,Int.
J.Adhesion and Adhesives,7:9-14,1987）。この10アミ
ノ酸の配列の繰り返しをコードするＤＮＡを人工的に合
成し、微生物に作らせることにより水中で接着可能な接
着剤を製造する方法がすでに報告されている（特開平1-
104180号公報）。また、一部分が明らかにされている天
然のムラサキイガイ接着蛋白質の配列を微生物に組み込
んで接着蛋白質を製造する方法も報告されている（D.R.
Filpula et al.,Biotechnol.Prog.,6:171-177,1990）。
しかし、接着剤の接着強度はより強いことが望ましく、
より強い接着強度を実現するための新たな材料が求めら
れていた。Mussels can synthesize an adhesive protein to attach themselves to a substrate in order to fix themselves in a favorable environment. This adhesion protein is mainly tens of Ala-Lys-Pro-Ser-Tyr-Pro-Pro-Thr-Ty in mussels.
It is composed of a repeating sequence of 10 amino acids called r-Lys and is known to be able to cure in seawater and reach sufficient adhesive strength (JHWaite, Int.
J. Adhesion and Adhesives, 7: 9-14, 1987). A method of artificially synthesizing a DNA encoding this repeat of a sequence of 10 amino acids and producing it by a microorganism to produce an adhesive capable of adhering in water has already been reported (JP-A-1-
No. 104180). Also, a method for producing an adhesion protein by incorporating a sequence of a naturally-occurring mussel adhesion protein into a microorganism has been reported (DR
Filpula et al., Biotechnol. Prog., 6: 171-177, 1990).
However, it is desirable that the adhesive has a stronger adhesive strength,
There has been a demand for new materials to achieve stronger adhesive strength.
【０００４】[0004]
【発明が解決しようとする課題】本発明の目的は、より
接着強度の強いイガイ類の接着蛋白質を提供することに
ある。SUMMARY OF THE INVENTION An object of the present invention is to provide a mussel adhesive protein having a higher adhesive strength.
【０００５】[0005]
【課題を解決するための手段】本発明者等は、従来接着
蛋白質遺伝子について調べられていなかったイガイ（My
tilus coruscus）に着目した。イガイは、従来調べられ
てきたムラサキイガイ（Mytilus edulis）やチレニアイ
ガイ（Mytilus galloprovincialis ）よりも波の荒い海
域を好んで生息する種で、接着強度がこれらの種よりよ
り強いことが知られている。そして、研究の結果、イガ
イの足から抽出したｍＲＮＡから作製したｃＤＮＡライ
ブラリーから、接着蛋白質ｃＤＮＡを単離することに成
功し、本発明を完成した。[Means for Solving the Problems] The present inventors have investigated mussels (My
tilus coruscus). It is known that mussels prefer the mussels (Mytilus edulis) and Tyrrhenian mussels (Mytilus galloprovincialis), which have been investigated so far, to live in areas with rough waves and have stronger adhesion strength than these species. As a result of the research, they succeeded in isolating the adhesion protein cDNA from the cDNA library prepared from the mRNA extracted from the mussel foot, and completed the present invention.
【０００６】即ち、本発明は、配列番号１で示されるア
ミノ酸配列、又は配列番号１で示されるアミノ酸配列と
実質的に同一なアミノ酸配列をコードするイガイ接着蛋
白質遺伝子である。また、本発明は、ＤＮＡ配列が配列
番号２で示される上記記載のイガイ接着蛋白質遺伝子で
ある。That is, the present invention is a mussel adhesion protein gene encoding an amino acid sequence represented by SEQ ID NO: 1 or an amino acid sequence substantially identical to the amino acid sequence represented by SEQ ID NO: 1. Further, the present invention is the above-mentioned mussel adhesion protein gene whose DNA sequence is shown in SEQ ID NO: 2.
【０００７】更に、本発明は、ミチルス・コラスカス
（Mytilus coruscus）を起源とし、Pro-Lys-(Ile又はPr
o)-(Ser又はThr)-Tyr-Pro-Pro-(Thr又はSer)-Tyr-Lysを
含むポリペプチドをコードするイガイ接着蛋白質遺伝子
である。以下、本発明を詳細に説明する。本発明のイガ
イ接着蛋白質遺伝子は、配列番号１で示されるアミノ酸
配列、又は配列番号１で示されるアミノ酸配列と実質的
に同一なアミノ酸配列をコードする。ここで、「配列番
号１で示されるアミノ酸配列と実質的に同一なアミノ酸
配列」とは、配列番号１で示されるアミノ酸配列の幾つ
かのアミノ酸残基について、欠失、置換、付加等の変化
が生じた配列であって、前記配列と同様の接着特性を有
するアミノ酸配列をいう。なお、配列番号１で示される
アミノ酸配列の部分アミノ酸配列も「配列番号１で示さ
れるアミノ酸配列と実質的に同一なアミノ酸配列」に含
まれることはいうまでもない。Furthermore, the present invention originates from Mytilus coruscus, and is derived from Pro-Lys- (Ile or Pr
It is a mussel adhesion protein gene encoding a polypeptide containing o)-(Ser or Thr) -Tyr-Pro-Pro- (Thr or Ser) -Tyr-Lys. Hereinafter, the present invention will be described in detail. The mussel adhesion protein gene of the present invention encodes the amino acid sequence represented by SEQ ID NO: 1 or an amino acid sequence substantially the same as the amino acid sequence represented by SEQ ID NO: 1. Here, “an amino acid sequence substantially the same as the amino acid sequence represented by SEQ ID NO: 1” means changes in some amino acid residues of the amino acid sequence represented by SEQ ID NO: 1 such as deletion, substitution and addition. And the amino acid sequence having adhesive properties similar to those of the above sequence. It goes without saying that the partial amino acid sequence of the amino acid sequence represented by SEQ ID NO: 1 is also included in the “amino acid sequence substantially identical to the amino acid sequence represented by SEQ ID NO: 1”.
【０００８】本発明の遺伝子の塩基配列の一例として
は、配列番号２で示される塩基配列を挙げることができ
る。本発明の遺伝子の特徴としては、Pro-Lys-(Ile又は
Pro)-(Ser又はThr)-Tyr-Pro-Pro-(Thr又はSer)-Tyr-Lys
をコードする塩基配列を繰り返し含むことである。本発
明遺伝子は以下の手順で得ることができる。まずイガイ
の足をチオシアン酸グアニジン等により可溶化し、フェ
ノール／クロロホルムによる抽出を行ない、イソプロパ
ノールにより沈殿させることにより全ＲＮＡを得ること
ができる。全ＲＮＡを得る方法はこの方法に限定される
ものではなく、ＬｉＣｌ沈殿法や塩化セシウム溶液に重
層して遠心することによっても得られる。全ＲＮＡか
ら、オリゴｄＴセルロースカラムを用いてポリアデニル
酸鎖を有するＲＮＡ（ポリＡ−ＲＮＡ）を調製する。こ
のポリＡ−ＲＮＡを鋳型として逆転写酵素を用いて２本
鎖ＤＮＡを調製する。この２本鎖ＤＮＡの合成はＳｌヌ
クレアーゼ法やオカヤマ−バーグ法により行ない得る
が、市販のｃＤＮＡ合成キットを用いて合成することも
可能である。次いで、得られたｃＤＮＡを適当なベクタ
ーに挿入し、このベクターを適当な宿主に導入して増幅
させるとともに目的のＤＮＡを持つクローンを選択す
る。ベクターはλファージ由来の各種ベクター、例えば
λgt10やλZAPII など、あるいはpBR322等のプラスミド
ベクターを用いることができる。目的クローンの選択に
は繰り返し配列の一部に相当するオリゴヌクレオチドを
合成してプローブとして用い、これに強く結合するクロ
ーンを選択すればよい。配列の決定はサンガー法やマキ
サム−ギルバート法等の一般的な方法によって決定でき
る。以上の手順により接着蛋白質ｃＤＮＡを単離するこ
とができる。An example of the base sequence of the gene of the present invention is the base sequence shown in SEQ ID NO: 2. The features of the gene of the present invention include Pro-Lys- (Ile or
Pro)-(Ser or Thr) -Tyr-Pro-Pro- (Thr or Ser) -Tyr-Lys
Is to repeatedly include a nucleotide sequence encoding The gene of the present invention can be obtained by the following procedure. First, total RNA can be obtained by solubilizing mussel feet with guanidine thiocyanate, extracting with phenol / chloroform, and precipitating with isopropanol. The method for obtaining total RNA is not limited to this method, and it can also be obtained by a LiCl precipitation method or a method of overlaying with a cesium chloride solution and centrifuging. RNA having a polyadenylic acid chain (polyA-RNA) is prepared from total RNA using an oligo dT cellulose column. Double-stranded DNA is prepared using this poly A-RNA as a template and reverse transcriptase. This double-stranded DNA can be synthesized by the Sl nuclease method or the Okayama-Berg method, but can also be synthesized by using a commercially available cDNA synthesis kit. Then, the obtained cDNA is inserted into an appropriate vector, this vector is introduced into an appropriate host for amplification, and a clone having the desired DNA is selected. As the vector, various vectors derived from λ phage, such as λgt10 and λZAPII, or a plasmid vector such as pBR322 can be used. To select the target clone, an oligonucleotide corresponding to a part of the repeating sequence is synthesized and used as a probe, and a clone that strongly binds to this may be selected. The sequence can be determined by a general method such as Sanger method or Maxam-Gilbert method. The adhesion protein cDNA can be isolated by the above procedure.
【０００９】この配列は、イガイ接着蛋白質の成熟ポリ
ペプチド領域全長をコードする領域を有しているため、
適当を発現ベクターに挿入し、微生物や培養細胞に導入
して発現させることにより、当該ペプチドを大量調製す
ることが可能である。以下、実施例を用いて本発明を更
に詳細に説明する。但し、本発明の技術的範囲は、これ
らの実施例に限定されるものではない。Since this sequence has a region encoding the entire length of the mature polypeptide region of the mussel adhesion protein,
A large amount of the peptide can be prepared by inserting an appropriate vector into an expression vector and introducing it into a microorganism or a cultured cell for expression. Hereinafter, the present invention will be described in more detail with reference to examples. However, the technical scope of the present invention is not limited to these examples.
【００１０】[0010]
〔実施例１〕 イガイ足ｃＤＮＡライブラリーの作製 北海道戸井町の海岸で採集した殻長４〜５cmのイガイ10
個体の足よりClontech社のTotal RNA Separator Kit を
用いて添付のプロトコールに従って全ＲＮＡを抽出し、
オリゴｄＴセルロースカラムに導通してポリアデニル酸
鎖を有するＲＮＡ（ポリＡ−ＲＮＡ）を調製した。この
操作により約２μｇのポリＡ−ＲＮＡが得られた。次に
このポリＡ−ＲＮＡを鋳型としてStratagene社のUni-ZA
P XR cloning kitを用いて添付のプロトコールに従い、
ｃＤＮＡライブラリーを作製した。[Example 1] Preparation of mussel cDNA library Mussels 10-4 cm in shell length collected on the coast of Toi Town, Hokkaido
Total RNA was extracted from the individual's foot using Clontech's Total RNA Separator Kit according to the attached protocol,
An RNA having a polyadenylic acid chain (polyA-RNA) was prepared by passing through an oligo dT cellulose column. By this operation, about 2 μg of poly A-RNA was obtained. Next, using this poly A-RNA as a template, Uni-ZA from Stratagene
According to the attached protocol using P XR cloning kit,
A cDNA library was created.
【００１１】〔実施例２〕 接着蛋白質ｃＤＮＡを含む
組換えファージの選択 実施例１で得られたｃＤＮＡライブラリーを増幅させ、
得られた2000個のプラークをナイロンメンブレン ハイ
ボンドＮ上に固定した。次いでランダムプライマーＤＮ
Ａ標識キット（寳酒造社製）を用いて[32P]dCTP により
標識したチレニアイガイ（M.galloprovincialis ）接着
蛋白質ｃＤＮＡ（K.Inoue and S.Odo,Biological Bulle
tin 186,349-355,1994）の全長をプローブとして用い
て、プラークハイブリダイゼーションを行なった結果、
50個以上のプラークがプローブと結合した。これらのう
ち10個のプラークを任意に選び、挿入されているｃＤＮ
Ａの長さをアガロース電気泳動により調べて、最も長い
挿入断片を持つものについてSOLR/ExAssist System（St
ratagene社）を用いて挿入断片をプラスミドベクターpB
luescriptSK(+)にサブクローニングした。このプラスミ
ドベクターをE.coli Mcfp1-53 に導入した。E.coli Mcf
p1-53 は、工業技術院生命工学工業技術研究所に寄託番
号FERM P-14865として寄託されている（寄託日：平成７
年３月２７日）。Example 2 Selection of Recombinant Phage Containing Adhesion Protein cDNA The cDNA library obtained in Example 1 was amplified,
The obtained 2000 plaques were fixed on a nylon membrane High Bond N. Then random primer DN
[ 32 P] dCTP-labeled cDNA of the M. galloprovincialis adhesion protein cDNA (K. Inoue and S. Odo, Biological Bulle) labeled with [ 32 P] dCTP using an A labeling kit (manufactured by Takara Shuzo)
tin 186,349-355,1994) using plaque hybridization as a probe,
Over 50 plaques bound to the probe. Any 10 of these plaques have been arbitrarily selected and inserted
The length of A was examined by agarose gel electrophoresis, and for those with the longest insert, the SOLR / ExAssist System (St
ratagene) and insert the insert into the plasmid vector pB
Subcloned into luescript SK (+). This plasmid vector was introduced into E. coli Mcfp1-53. E.coli Mcf
p1-53 has been deposited at the Institute of Biotechnology, Institute of Industrial Science, with the deposit number FERM P-14865 (deposit date: 1995).
March 27, 2013).
【００１２】〔実施例３〕 接着蛋白質遺伝子の配列決
定 実施例２で得られた挿入断片の両端の配列をアプライド
バイオシステムズ社製373ADNA シーケンサー及びPRISM
Dye Terminator cycle sequencing Kit を用いて配列を
決定した。その結果、この挿入断片が接着蛋白質の成熟
ペプチド領域の全長を含む配列であることが判明した。
さらに、寳酒造社製キロシーケンスキットを用いて、接
着蛋白質配列の一部分を欠失させた一連のプラスミドを
作出し、アプライドバイオシステムズ社製373ADNA シー
ケンサー及びPRISM Dye Terminator cycle sequencing
Kit を用いて全長の配列を決定した。その結果、得られ
た接着蛋白質遺伝子は図１及び図２に示した通り、成熟
ペプチドのアミノ末端からカルボキシル末端まで848 ア
ミノ酸の配列及び終止コドンをコードする全長2547bpの
配列を含んでいた。848 アミノ酸のうち上流から101 残
基が非繰り返し領域であり、その下流に接着の機能を持
つPro-Lys-Pro またはIle-Ser またはThr-Tyr-Pro-Pro-
Thr またはSer-Lys という10アミノ酸の基本配列とその
若干の変異配列を合わせて72回含む繰り返し領域であっ
た。また下流側の非翻訳領域にはポリアデニル酸鎖付加
シグナルAATAAAが存在し、そのさらに下流にポリアデニ
ル酸鎖が存在した。Example 3 Sequencing of Adhesion Protein Gene The sequences at both ends of the insert fragment obtained in Example 2 were changed to 373A DNA sequencer and PRISM manufactured by Applied Biosystems.
Sequencing was performed using the Dye Terminator cycle sequencing Kit. As a result, it was revealed that this insert fragment was a sequence containing the entire length of the mature peptide region of the adhesion protein.
Furthermore, a series of plasmids in which a part of the adhesion protein sequence was deleted was created using the Kiro Sequencing Kit manufactured by Takara Shuzo, and 373A DNA Sequencer and PRISM Dye Terminator cycle sequencing manufactured by Applied Biosystems.
The full length sequence was determined using the Kit. As a result, the resulting adhesion protein gene contained a sequence of 848 amino acids from the amino terminus to the carboxyl terminus of the mature peptide and a 2547 bp full length sequence encoding a stop codon, as shown in FIGS. 1 and 2. Of the 848 amino acids, 101 residues from the upstream are non-repetitive regions, and the downstream of them has an adhesion function Pro-Lys-Pro or Ile-Ser or Thr-Tyr-Pro-Pro-
It was a repetitive region containing 72 times including the basic sequence of 10 amino acids, Thr or Ser-Lys, and some of its mutant sequences. A polyadenylate chain addition signal AATAAA was present in the untranslated region on the downstream side, and a polyadenylate chain was present further downstream thereof.
【００１３】[0013]
【発明の効果】本発明は、イガイ接着蛋白質遺伝子を提
供する。本発明の遺伝子から作られる蛋白質は、他のイ
ガイ類の接着蛋白質よりも接着強度が強く、接着剤の原
料として有用である。INDUSTRIAL APPLICABILITY The present invention provides a mussel adhesion protein gene. The protein made from the gene of the present invention has a stronger adhesive strength than the adhesive proteins of other mussels and is useful as a raw material for adhesives.
【００１４】[0014]
配列番号 １ 配列の長さ：８４８ 配列の型 ：アミノ酸 トポロジー：不明 配列の種類：タンパク質 起源 生物名 ：Mytilus coruscus 配列 SEQ ID NO: 1 sequence length: 848 sequence type: amino acid topology: unknown sequence type: protein origin organism name: Mytilus coruscus sequence
【００１５】配列番号 ２ 配列の長さ：２５４７ 配列の型 ：核酸 鎖の数 ：２本鎖 トポロジー：直鎖状 配列の種類：mRNA to cDNA 起源 生物名 ：Mytilus coruscus 配列 SEQ ID NO: 2 Sequence length: 2547 Sequence type: Nucleic acid Number of strands: Double strand Topology: Linear Sequence type: mRNA to cDNA Origin organism name: Mytilus coruscus sequence
【図１】本発明のイガイ接着蛋白質遺伝子の塩基配列を
示す図である。FIG. 1 is a diagram showing the nucleotide sequence of the mussel adhesion protein gene of the present invention.
【図２】本発明のイガイ接着蛋白質遺伝子の塩基配列を
示す図である。FIG. 2 is a diagram showing the nucleotide sequence of the mussel adhesion protein gene of the present invention.
Claims (3)
は配列番号１で示されるアミノ酸配列と実質的に同一な
アミノ酸配列をコードするイガイ接着蛋白質遺伝子。1. A mussel adhesion protein gene encoding an amino acid sequence represented by SEQ ID NO: 1 or an amino acid sequence substantially identical to the amino acid sequence represented by SEQ ID NO: 1.
項１記載のイガイ接着蛋白質遺伝子。2. The mussel adhesion protein gene according to claim 1, wherein the DNA sequence is represented by SEQ ID NO: 2.
us）を起源とし、Pro-Lys-(Ile又はPro)-(Ser又はThr)-
Tyr-Pro-Pro-(Thr又はSer)-Tyr-Lysを含むポリペプチド
をコードするイガイ接着蛋白質遺伝子。3. Mytilus corusc
us) as the origin, and Pro-Lys- (Ile or Pro)-(Ser or Thr)-
A mussel adhesion protein gene encoding a polypeptide containing Tyr-Pro-Pro- (Thr or Ser) -Tyr-Lys.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP7075210A JPH08266281A (en) | 1995-03-31 | 1995-03-31 | Mussel adhesive protein gene |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP7075210A JPH08266281A (en) | 1995-03-31 | 1995-03-31 | Mussel adhesive protein gene |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH08266281A true JPH08266281A (en) | 1996-10-15 |
Family
ID=13569618
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP7075210A Pending JPH08266281A (en) | 1995-03-31 | 1995-03-31 | Mussel adhesive protein gene |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH08266281A (en) |
Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005092920A1 (en) * | 2004-03-26 | 2005-10-06 | Postech Foundation | Mussel bioadhesive |
| WO2006103225A1 (en) * | 2005-03-31 | 2006-10-05 | Basf Aktiengesellschaft | Use of polypeptides in the form of adhesive agents |
| US7799741B2 (en) | 2005-04-01 | 2010-09-21 | Basf Se | Drilling mud containing hydrophobin |
| US7892788B2 (en) | 2005-02-07 | 2011-02-22 | Basf Se | Hydrophobin fusion products, production and use thereof |
| US7910699B2 (en) | 2005-06-10 | 2011-03-22 | Basf Se | Cysteine-depleted hydrophobin fusion proteins, their production and use thereof |
| US8038740B2 (en) | 2005-10-12 | 2011-10-18 | Basf Se | Use of proteins as an antifoaming constituent in fuels |
| US8096484B2 (en) | 2006-08-15 | 2012-01-17 | Basf Se | Method for the production of dry free-flowing hydrophobin preparations |
| US8535535B2 (en) | 2005-04-01 | 2013-09-17 | Basf Se | Use of hydrophobin as a phase stabilizer |
-
1995
- 1995-03-31 JP JP7075210A patent/JPH08266281A/en active Pending
Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005092920A1 (en) * | 2004-03-26 | 2005-10-06 | Postech Foundation | Mussel bioadhesive |
| US7622550B2 (en) | 2004-03-26 | 2009-11-24 | Postech Foundation | Mussel bioadhesive |
| US7892788B2 (en) | 2005-02-07 | 2011-02-22 | Basf Se | Hydrophobin fusion products, production and use thereof |
| WO2006103225A1 (en) * | 2005-03-31 | 2006-10-05 | Basf Aktiengesellschaft | Use of polypeptides in the form of adhesive agents |
| JP4772110B2 (en) * | 2005-03-31 | 2011-09-14 | ビーエーエスエフ ソシエタス・ヨーロピア | Use of polypeptides as adhesion promoters |
| US8859106B2 (en) | 2005-03-31 | 2014-10-14 | Basf Se | Use of polypeptides in the form of adhesive agents |
| US7799741B2 (en) | 2005-04-01 | 2010-09-21 | Basf Se | Drilling mud containing hydrophobin |
| US8535535B2 (en) | 2005-04-01 | 2013-09-17 | Basf Se | Use of hydrophobin as a phase stabilizer |
| US7910699B2 (en) | 2005-06-10 | 2011-03-22 | Basf Se | Cysteine-depleted hydrophobin fusion proteins, their production and use thereof |
| US8038740B2 (en) | 2005-10-12 | 2011-10-18 | Basf Se | Use of proteins as an antifoaming constituent in fuels |
| US8096484B2 (en) | 2006-08-15 | 2012-01-17 | Basf Se | Method for the production of dry free-flowing hydrophobin preparations |
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