JPH0489836A - Production of wool powder - Google Patents
Production of wool powderInfo
- Publication number
- JPH0489836A JPH0489836A JP20582390A JP20582390A JPH0489836A JP H0489836 A JPH0489836 A JP H0489836A JP 20582390 A JP20582390 A JP 20582390A JP 20582390 A JP20582390 A JP 20582390A JP H0489836 A JPH0489836 A JP H0489836A
- Authority
- JP
- Japan
- Prior art keywords
- wool
- wool fibers
- powder
- fiber
- fibers
- 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
- 210000002268 wool Anatomy 0.000 title claims abstract description 46
- 239000000843 powder Substances 0.000 title claims abstract description 18
- 238000004519 manufacturing process Methods 0.000 title claims description 3
- 239000000835 fiber Substances 0.000 claims abstract description 36
- 108091005804 Peptidases Proteins 0.000 claims abstract description 15
- 102000035195 Peptidases Human genes 0.000 claims abstract description 6
- 230000002542 deteriorative effect Effects 0.000 claims abstract description 3
- 239000002245 particle Substances 0.000 abstract description 6
- 238000000227 grinding Methods 0.000 abstract description 4
- 238000003508 chemical denaturation Methods 0.000 abstract description 3
- 241000894006 Bacteria Species 0.000 abstract description 2
- 230000003247 decreasing effect Effects 0.000 abstract description 2
- 239000004365 Protease Substances 0.000 description 13
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 9
- 235000019419 proteases Nutrition 0.000 description 9
- 238000000034 method Methods 0.000 description 8
- 238000011282 treatment Methods 0.000 description 8
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 6
- 210000004209 hair Anatomy 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 239000002253 acid Substances 0.000 description 5
- 150000001413 amino acids Chemical class 0.000 description 5
- 229940088598 enzyme Drugs 0.000 description 5
- 102000004169 proteins and genes Human genes 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- 239000003513 alkali Substances 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- RWSOTUBLDIXVET-UHFFFAOYSA-N Dihydrogen sulfide Chemical compound S RWSOTUBLDIXVET-UHFFFAOYSA-N 0.000 description 3
- 229910021529 ammonia Inorganic materials 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 238000004040 coloring Methods 0.000 description 3
- 230000000052 comparative effect Effects 0.000 description 3
- -1 cystine Chemical class 0.000 description 3
- 229960003067 cystine Drugs 0.000 description 3
- 229910000037 hydrogen sulfide Inorganic materials 0.000 description 3
- 238000010298 pulverizing process Methods 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 102000011782 Keratins Human genes 0.000 description 2
- 108010076876 Keratins Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 230000006835 compression Effects 0.000 description 2
- 238000007906 compression Methods 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 239000002537 cosmetic Substances 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 238000000354 decomposition reaction Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 239000010419 fine particle Substances 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000011593 sulfur Substances 0.000 description 2
- 229910052717 sulfur Inorganic materials 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 238000004061 bleaching Methods 0.000 description 1
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- 239000003093 cationic surfactant Substances 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 230000005484 gravity Effects 0.000 description 1
- 230000020169 heat generation Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 235000019388 lanolin Nutrition 0.000 description 1
- 239000002649 leather substitute Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 230000003020 moisturizing effect Effects 0.000 description 1
- 230000009965 odorless effect Effects 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 238000009991 scouring Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Processes Of Treating Macromolecular Substances (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
Abstract
Description
【発明の詳細な説明】
(産業上の利用分野)
本発胡は新規なウールパウダーの製造方法に関するもの
である。DETAILED DESCRIPTION OF THE INVENTION (Industrial Application Field) The present invention relates to a novel method for producing wool powder.
(従来技術及びその解決すべき課題)
近時、プロティンパウダーは、蛋白質としての性質を利
用した合成皮革や充填材、表面改質用塗布材の分野、保
湿性を利用した化粧品材料等の分野、更に、天然蛋白質
の無害性或は構成アミノ酸の機能を利用した食品材料等
の分野で、用途が拡大多様化している。(Prior art and problems to be solved) Recently, protein powder has been used in the fields of synthetic leather and fillers that utilize its properties as a protein, coating materials for surface modification, cosmetic materials that utilize its moisturizing properties, etc. Furthermore, applications are expanding and diversifying in the field of food materials and the like that utilize the harmlessness of natural proteins or the functions of their constituent amino acids.
羊毛繊維はシスチン、クルタミン酸、ロインン、アルギ
ニンを主体とした各種アミノ酸から構成されたケラチン
という蛋白質に属する。従って、羊毛繊維を効率良く微
小粒度にまで粉末化する事が可能となれば、上記プロテ
ィンパウダーと同様の用途が考えられる。Wool fibers belong to a protein called keratin, which is composed of various amino acids, mainly cystine, curtamic acid, loinine, and arginine. Therefore, if it becomes possible to efficiently powder wool fibers down to a fine particle size, it would be possible to use it in the same way as the above-mentioned protein powder.
従来、羊毛繊維の粉末化は、−船釣には直接機械的に粉
砕する方法、例えば、衝撃式、圧縮式、剪断式、エアー
ジェット式等の各種粉砕機械により行なう方法や、酸、
アルカリ等の化学的処理により羊毛m維を劣化させ、上
記機械的処理により粉砕する方法、更に:ま、液体窒素
を用いて羊毛繊維を低温で脆化させ、上記機械的処理に
より粉砕する方法等により行なわれてし)る。Conventionally, wool fibers have been pulverized by direct mechanical pulverization methods such as impact type, compression type, shear type, air jet type, etc., or acid,
A method in which wool fibers are degraded by chemical treatment such as alkali and crushed by the above mechanical treatment, and furthermore, a method in which wool fibers are embrittled at low temperature using liquid nitrogen and crushed by the above mechanical treatment, etc. (performed by)
巳かしながら、直接機械的粉砕する場合、羊毛繊維の比
重が軽く、伸度が大きく (標準状態25〜35%、湿
潤状態:25〜50%)、更に、ヤング率が小さい(1
30〜300kg/cd)ために、粉砕は困難であり、
粉砕化率が低下し、そのため、微小粒度の粉体を得るこ
とが出来なかった。However, when directly mechanically crushed, the specific gravity of wool fibers is light, the elongation is large (25-35% in standard state, 25-50% in wet state), and Young's modulus is small (1
30-300 kg/cd), it is difficult to crush the
The pulverization rate decreased, and therefore, it was not possible to obtain powder with a fine particle size.
鵞だ、粉砕過程で発熱を伴うたt、発色、発臭等の問題
により品質的にも劣ってし)だ。However, the quality is inferior due to problems such as heat generation during the crushing process, color development, and odor.)
また、酸を用′、また化学的処理と併用する場合、羊毛
繊維が酸j=抵抗性があり、劣化しにくい。また、アル
カリを用−)る場合、高濃度のアルカリにより劣化はす
るが、同時j=アンモニア及び硫化水素を発生し、工業
的に利用可能な品質の粉体を得ることは不可能であった
。Furthermore, when using acids or in combination with chemical treatments, wool fibers are acid resistant and do not easily deteriorate. In addition, when alkali is used, it deteriorates due to high concentration of alkali, but at the same time generates ammonia and hydrogen sulfide, making it impossible to obtain powder of industrially usable quality. .
更;=、低温脆化を併用する場合、液体窒素を用、)な
ければなろなし)ために、イニンヤル及びランニングコ
ストが増大し、安価にウールパウダーを製造することが
できず、また得ろれるウールパウダーは比較的粒度の大
きなものとなり、例えば、化粧品素材として多用される
平均粒度10μm以下の粉体を得ることは困難であった
。Moreover, when low-temperature embrittlement is used together, liquid nitrogen must be used), which increases initial and running costs, making it impossible to produce wool powder at a low cost, and reducing the amount of wool that can be obtained. The powder has a relatively large particle size, and for example, it has been difficult to obtain a powder with an average particle size of 10 μm or less, which is often used as a cosmetic material.
(発胡の目的)
従って、本発明は、従来法に見みれる発色、発臭の問題
がな(、極めて化学的変性の少なし)微小粒度のウール
パウダーを容易に!!!造できる方法を提供することを
目的とする。(Purpose of husking) Therefore, the present invention can easily produce microscopic wool powder without the coloring and odor problems seen in conventional methods (and with extremely little chemical denaturation)! ! ! The purpose is to provide a method that can be used to create
(課題を解決するた灼の手段)
本発明者ろは、上記の目的を達成するために鋭意研究し
た結果、特定の蛋白分解酵素(以下、プロテアーゼ)を
用いて、羊毛繊維を劣化した後、機械的粉砕することに
より、従来得ろれなかった平均粒’!j 10 Atm
以下でしかも化学的変性の少なし)とともに、無色、無
臭のウールパウダーの得ちれることを見出し、本発明に
至ったものである。(Means for Solving the Problem) As a result of intensive research to achieve the above object, the inventor Roha found that after deteriorating wool fibers using a specific protease (hereinafter referred to as protease), Mechanical crushing produces average grains that were previously impossible to obtain! j 10 ATM
The inventors have discovered that it is possible to obtain colorless and odorless wool powder with less chemical modification), and have arrived at the present invention.
即ち、羊毛繊維が粉砕過程にお5)で、発色、発臭する
のは、主に熱の作用による。つまり、羊毛繊維jま熱分
解して、アンモニアと硫化水素を発生する。そして、温
度が90℃以上になると、アンモニア及び硫化水素の発
生量は増大し、発色及び発臭する。しかも、機械的粉砕
のみにおし)では、平均粒度が10μm以下のような微
小粉体を効率良く製造することは不可能であった。That is, the wool fibers develop color and odor during the crushing process in step 5) mainly due to the action of heat. In other words, wool fibers are thermally decomposed to generate ammonia and hydrogen sulfide. When the temperature reaches 90° C. or higher, the amount of ammonia and hydrogen sulfide generated increases, causing color and odor. Moreover, it has been impossible to efficiently produce fine powder with an average particle size of 10 μm or less by using only mechanical pulverization.
一方、羊毛繊維は、酸に対しては一般的に強いが、アル
カリに対しては著しく弱く、分解によりその強度を低下
する。そして、アルカリによる羊毛繊維の分解は、シス
チン中のグイサルファイド基の切断により生じ、その結
果、羊毛繊維かみ硫黄が遊離する。一般j=その量は、
硫黄含量の50%近くに達する。そのために、発色、発
臭を生じる結果となる。これに対して、プロテアーゼに
よる羊毛繊維の劣化;ま、羊毛ケラチンを構成している
アミノ酸のペプチド結合の切断により生じ、シスチン結
合の切断を伴わないので、発色、発臭を生じなし)。葦
だ、その切断は、一部のアミノ酸のペプチド結合に限定
されるので、羊毛繊維の性質を損なう二ともない。Wool fibers, on the other hand, are generally strong against acids, but are extremely weak against alkalis, reducing their strength through decomposition. The decomposition of wool fibers by alkali occurs due to the cleavage of the guisulfide group in cystine, and as a result, wool fibers and sulfur are liberated. General j = the amount is
The sulfur content reaches nearly 50%. This results in coloring and odor. On the other hand, deterioration of wool fibers by protease (well, it occurs due to the cleavage of the peptide bonds of the amino acids that make up wool keratin, and does not involve the cleavage of cystine bonds, so there is no coloring or odor). Since the cutting is limited to the peptide bonds of some amino acids, there is no doubt that it will damage the properties of the wool fiber.
本発明者ろは、熱をかけず又は熱を生じることなくしか
も羊毛繊維の性質に大きな影響を与える二と一;く、そ
の物理的強度を低下させる方法について研究した結果、
羊毛繊維分解能を有するプロテアーゼにより劣化処理す
ることにより、上記目的が達成できることを見い出した
。本発明はかかる知見に基づいてなされたものである。As a result of research into a method for reducing the physical strength of wool fibers without applying heat or generating heat, the present inventor has found that:
It has been found that the above object can be achieved by degrading wool fibers using a protease that has the ability to degrade wool fibers. The present invention has been made based on this knowledge.
以下、本発明について詳述する。The present invention will be explained in detail below.
一般に、羊毛繊維は、細毛型(採毛型)、中毛型、長毛
型、雑種毛型、混合毛型、等の種類により、繊度、繊維
長等の毛質が大きく異なってし)るが、本発明における
羊毛繊維は、羊かろ採取されるものであれば何でも使用
する二とが出来る。In general, wool fibers vary greatly in quality, such as fineness and fiber length, depending on the type, such as fine hair type (collected hair type), medium hair type, long hair type, hybrid hair type, mixed hair type, etc. In the present invention, any wool fiber can be used as long as it is harvested from sheep.
羊毛繊維は、ウールグリースやスイントのような酵素の
阻害因子とも成り得る天然不純物が付着して7)るので
、純粋なウールパウダーを製造する場合には、精練によ
りこれを除去することが好ましい。Since wool fibers are loaded with natural impurities, such as wool grease and suint, which can act as inhibitors of enzymes, it is preferable to remove these by scouring when producing pure wool powder.
また、羊毛繊維をそのまま用し)ると、酵素反応が不均
一になりがちなので、酵素反応の効率化を考えた場合、
使用する羊毛W&維は、0.5コ〜30肥の長さに成型
したものが好ま巳し)。In addition, if wool fibers are used as they are, the enzymatic reaction tends to be uneven, so when considering the efficiency of the enzymatic reaction,
It is preferable that the wool W&fiber used be shaped into a length of 0.5 to 30 mm).
本発明で使用されるプロテアーゼは、アミノ酸のペプチ
ド結合を切断するものであれば、いずれでも使用できる
。このようなプロテアーゼとしては、かび、細菌、動物
、植物等の出所は特に問わない。しかしながら、短時間
でより多くの効果を達成するならば、ペブンン、トリプ
シン、キモトリプンン及びパパインを用ヒ)るよりも、
細菌由来のプロテアーゼを用いる方が好ましい。Any protease used in the present invention can be used as long as it cleaves peptide bonds between amino acids. Such proteases may be from any source such as fungi, bacteria, animals, plants, etc. However, if you want to achieve more effect in a shorter time than using pebun, trypsin, chymotrypone and papain,
Preferably, proteases of bacterial origin are used.
プロテアーゼは、通常、水溶液の形で使用する。Proteases are usually used in the form of aqueous solutions.
なお、プロテアーゼの活性を害しない範囲内に於)で、
ノニオン系、アニオン系、カチオン系等の界面活性剤や
、クエン酸、リン酸、ホウ酸、グリンン等の緩衝液から
なるpH安定剤などを併用してもよし)。In addition, within the range that does not harm the activity of protease),
Nonionic, anionic, cationic surfactants, and pH stabilizers consisting of buffers such as citric acid, phosphoric acid, boric acid, green, etc. may be used in combination).
一般に、羊毛繊維を処理する場合のプロテアーゼの種類
や量は、使用する羊毛繊維の性状により、若干変化する
。一般に、プロテアーゼの濃度:′!、150U/g〜
4000U/gが好まし1.)oまた、処理条件は、一
般にpH4,0〜11.0、温度は30℃〜55℃、そ
して処理時間は10〜48時間力く好ましい。Generally, the type and amount of protease used when treating wool fibers varies slightly depending on the properties of the wool fibers used. In general, the concentration of protease: ′! , 150U/g~
4000U/g is preferred1. ) The treatment conditions are generally pH 4.0 to 11.0, temperature 30°C to 55°C, and treatment time 10 to 48 hours.
上記のようにして得られた酵素処理羊毛m維は、水洗を
充分に行なった後、必要に応じて、漂白と殺菌を兼ねた
過酸化水素処理を行なう。The enzyme-treated wool fibers obtained as described above are thoroughly washed with water, and then, if necessary, treated with hydrogen peroxide for both bleaching and sterilization.
次に、酵素処理した羊毛繊維は機械的な粉砕処理にかけ
られる。粉砕装置としては、衝撃式粉砕機、摩砕式粉砕
機、圧縮式粉砕機械など、粉砕処理に使用されるものは
なんでも使用することが出来る。粉砕時間は、装置によ
っても異なるが、例えば0.5〜6時間、好ましくは2
〜4時間である。The enzyme-treated wool fibers are then subjected to a mechanical grinding process. As the crushing device, any device used for crushing can be used, such as an impact crusher, a grinding crusher, a compression crusher, and the like. The grinding time varies depending on the device, but for example, 0.5 to 6 hours, preferably 2 hours.
~4 hours.
(実施例)
以下、本発明について、実施例により更に詳細に説明す
る。但し、本発明の範囲は、これちの実施例により限定
されるものではな、)。(Example) Hereinafter, the present invention will be explained in more detail with reference to Examples. However, the scope of the present invention is not limited by these examples.)
実施例1
メリノ種原毛を通常法により精練し、ギロチンカッター
により2 mmに成型した。次jこ、市販のプロテアー
ゼく洛東化成■製、エンチロン5A−100)を用い、
酵素濃度40g/Lの水溶液とし、40℃、pH10,
0(M/10グリシン緩衝液にて調整)の条件下で24
時間羊毛繊維を処理し、洗浄した。次いで中央化工機■
製のファインバイブレーンヨンミルにより、羊毛繊維を
1時間粉砕した。Example 1 Merino seed wool was scoured by a conventional method and shaped into 2 mm using a guillotine cutter. Next, using a commercially available protease (manufactured by Rakuto Kasei, Enthiron 5A-100),
An aqueous solution with an enzyme concentration of 40 g/L, 40°C, pH 10,
24 under conditions of 0 (adjusted with M/10 glycine buffer)
The wool fibers were treated and washed for an hour. Then Chuo Kakoki ■
The wool fibers were milled for 1 hour using a Fine Vibrane Yon Mill manufactured by Co., Ltd.
比較例1
酵素処理を行なわないことを除いて、実施例1を繰り返
した。Comparative Example 1 Example 1 was repeated except that no enzyme treatment was performed.
比較例2
粉砕時間を6時間としたことを除いて比較例1と同様の
処理を行った。Comparative Example 2 The same treatment as Comparative Example 1 was performed except that the crushing time was 6 hours.
結果を以下の表1に掲げる。The results are listed in Table 1 below.
本発明によれは、羊毛繊維に熱及び化学的−二変性を与
えることなく、平均粒度が10μm以下の羊毛粉末が得
ちれる。According to the present invention, wool powder having an average particle size of 10 μm or less can be obtained without subjecting the wool fibers to thermal or chemical denaturation.
表 1Table 1
Claims (1)
的粉砕することを特徴とするウールパウダーの製造方法
。A method for producing wool powder, which comprises deteriorating wool fibers with a proteolytic enzyme and then mechanically crushing the fibers.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2205823A JPH0655829B2 (en) | 1990-08-02 | 1990-08-02 | Wool powder manufacturing method |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2205823A JPH0655829B2 (en) | 1990-08-02 | 1990-08-02 | Wool powder manufacturing method |
Publications (2)
Publication Number | Publication Date |
---|---|
JPH0489836A true JPH0489836A (en) | 1992-03-24 |
JPH0655829B2 JPH0655829B2 (en) | 1994-07-27 |
Family
ID=16513297
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2205823A Expired - Fee Related JPH0655829B2 (en) | 1990-08-02 | 1990-08-02 | Wool powder manufacturing method |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPH0655829B2 (en) |
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2000110083A (en) * | 1998-10-01 | 2000-04-18 | Suminoe Textile Co Ltd | Fabric for use in ink jet dyeing and dyeing method |
US7191596B2 (en) | 2003-10-01 | 2007-03-20 | Toyota Jidosha Kabushiki Kaisha | Stirling engine and hybrid system that uses the Stirling engine |
US7458216B2 (en) | 2003-10-01 | 2008-12-02 | Toyota Jidosha Kabushiki Kaisha | Exhaust heat recovery apparatus |
US7603857B2 (en) | 2005-06-29 | 2009-10-20 | Toyota Jidosha Kabushiki Kaisha | Exhaust heat recovery apparatus |
Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS62174231A (en) * | 1985-10-04 | 1987-07-31 | Nitta Zerachin Kk | Production of gelatin of improved solubility |
-
1990
- 1990-08-02 JP JP2205823A patent/JPH0655829B2/en not_active Expired - Fee Related
Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS62174231A (en) * | 1985-10-04 | 1987-07-31 | Nitta Zerachin Kk | Production of gelatin of improved solubility |
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2000110083A (en) * | 1998-10-01 | 2000-04-18 | Suminoe Textile Co Ltd | Fabric for use in ink jet dyeing and dyeing method |
US7191596B2 (en) | 2003-10-01 | 2007-03-20 | Toyota Jidosha Kabushiki Kaisha | Stirling engine and hybrid system that uses the Stirling engine |
US7458216B2 (en) | 2003-10-01 | 2008-12-02 | Toyota Jidosha Kabushiki Kaisha | Exhaust heat recovery apparatus |
US7603857B2 (en) | 2005-06-29 | 2009-10-20 | Toyota Jidosha Kabushiki Kaisha | Exhaust heat recovery apparatus |
Also Published As
Publication number | Publication date |
---|---|
JPH0655829B2 (en) | 1994-07-27 |
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