| 序号 | 专利名 | 申请号 | 申请日 | 公开（公告）号 | 公开（公告）日 | 发明人 |
|---|---|---|---|---|---|---|
| 1 | 用于改善水生动物健康的组合物和方法 | CN201480019820.3 | 2014-04-09 | CN105120682A | 2015-12-02 | D·德拉霍斯; C·蒙克; L·V·科弗德 |
| 本发明涉及用于增加水生动物健康的组合物和方法，这些组合物和方法包括一种或多种选定的细菌菌株。 | ||||||
| 2 | 将C-7糖转化为C-7羟基紫杉烷类的酶催化水解方法 | CN95101242.8 | 1995-01-13 | CN1111229A | 1995-11-08 | R·L·汉森; R·N·帕特尔; L·J·施扎卡 |
| 一种酶催化水解方法，其中将一种或多种带有C-7糖，优选带有C-7木糖基的紫杉烷类化合物(taxanes)与一种能够将所述糖基水解为羟基的酶或微生物接触。 | ||||||
| 3 | 将C-7糖转化为C-7羟基紫杉烷类的酶催化水解方法 | CN95101242.8 | 1995-01-13 | CN1061097C | 2001-01-24 | R·L·汉森; R·N·帕特尔; L·J·施扎卡 |
| 一种酶催化水解方法，其中将一种或多种带有C-7糖，优选带有C-7木糖基的紫杉烷类化合物(taxanes)与一种能够将所述糖基水解为羟基的酶或微生物接触。 | ||||||
| 4 | Heparitinase, process for producing the same and bacteria producing the same | US154740 | 1993-11-18 | US5405759A | 1995-04-11 | Kiyoshi Morikawa; Hirofumi Miyazono; Hiroshi Maruyama; Keiichi Yoshida |
| Disclosed are novel enzymes, heparitinase T-I, heparitinase T-II, heparitinase T-III and heparitinase T-IV, which degrade heparan sulfate and/or heparin, a process for producing thereof by cultivating a novel Bacillus circulans HpT 298 having an ability of producing these enzymes and a novel Bacillus circulans HpT 298. | ||||||
| 5 | Heparitinase, process for producing the same and bacteria producing the same | US843812 | 1992-02-28 | US5290695A | 1994-03-01 | Kiyoshi Morikawa; Hirofumi Miyazono; Hiroshi Maruyama; Keiichi Yoshida |
| Disclosed are novel enzymes, heparitinase T-I, heparitinase T-II, heparitinase T-III and heparitinase T-IV, which degrade heparan sulfate and/or heparin, a process for producing thereof by cultivating a novel Bacillus circulans HpT 298 having an ability of producing these enzymes and a novel Bacillus circulans HpT 298. | ||||||
| 6 | Ring peptide antibiotics, Permetin A and a process for producing the same | US27029 | 1979-04-04 | US4294754A | 1981-10-13 | Yoshiyuki Takahara; Yoshiteru Hirose; Yoko Takeuchi; Asao Murai; Masatsune Kainosho; Sawao Murao |
| A purified ring peptide antibiotic of the following empirical formula:N.alpha.-(3-hydroxy-4-methyl-1-oxohexyl)-L-.alpha.,.gamma.-diaminobutyryl-L-isoleucyl-L-.alpha.,.gamma.-diaminobutyryl-D-phenylalanyl-L-leucyl-L-.alpha.,.gamma.-diaminobutyryl-D-valyl-L-leucyl-L-serine (9-1)-lactoneand which has the following structural formula: ##STR1## and wherein Dab represents 2,4-diamino butyric acid. | ||||||
| 7 | Enzymatic hydrolysis method for the conversion of C-7 sugar to C-7 hydroxyl taxanes | US421017 | 1995-04-12 | US5700669A | 1997-12-23 | Ronald L. Hanson; Ramesh N. Patel; Laszlo J. Szarka |
| An enzymatic hydrolysis method, wherein one or more C-7 sugar, preferably C-7 xylosyl-bearing taxanes are contacted with an enzyme or microorganism capable of hydrolyzing said sugar groups to hydroxyl groups. | ||||||
| 8 | Biological inoculant | US523302 | 1990-05-05 | US5061490A | 1991-10-29 | Alan S. Paau; Dennis E. McCabe; Steven G. Platt |
| A biological inoculant is disclosed for facilitating and fostering the growth of edible corn plants. The inoculant includes biologically pure cultures of bacterial strains, including Bacillus circulans, a yet unidentified bacterial strain, and Xanthomonas maltotphilia. | ||||||
| 9 | Process of producing a peptide antibiotic with Bacillus circulans | US346451 | 1982-02-08 | US4360593A | 1982-11-23 | Masataka Konishi; Takeo Miyaki; Hiroshi Tsukiura; Hiroshi Kawaguchi |
| A novel peptide antibiotic complex designated herein as Bu-2470 is produced by fermentation of Bacillus circulans strain G493-B6 (ATCC 31,805). Complex Bu-2470 may be separated into four bioactive peptide antibiotics designated as Bu-2470A, B.sub.1, B.sub.2a, and B.sub.2b. The complex and individual bioactive factors possess significant antimicrobial activity. | ||||||
| 10 | Antibiotic compounds | US250987 | 1981-04-03 | US4341768A | 1982-07-27 | Masataka Konishi; Takeo Miyaki; Hiroshi Tsukiura; Hiroshi Kawaguchi |
| A novel peptide antibiotic complex designated herein as Bu-2470 is produced by fermentation of Bacillus circulans strain G493-B6 (ATCC 31,805). Complex Bu-2470 may be separated into four bioactive peptide antibiotics designated as Bu-2470A, B.sub.1, B.sub.2a, and B.sub.2b. The complex and individual bioactive factors possess significant antimicrobial activity. | ||||||
| 11 | 分岐α−グルカン及びこれを生成するα−グルコシル転移酵素とそれらの製造方法並びに用途 | JP2014152415 | 2014-07-25 | JP2014230542A | 2014-12-11 | WATANABE HIKARU; YAMAMOTO TAKUO; NISHIMOTO TOMOYUKI; TSUZAKI KEIJI; OKU KAZUYUKI; CHAEN HIROTO; FUKUDA SHIGEHARU |
| 【課題】水溶性食物繊維として有用なグルカンとその製造方法並びにその用途を提供することを課題とする。【解決手段】グルコースを構成糖とするα−グルカンであって、メチル化分析において、(1)2,3,6−トリメチル−1,4,5−トリアセチルグルシトールと2,3,4−トリメチル−1,5,6−トリアセチルグルシトールの比が1:0.6乃至1:4の範囲にある;(2)2,3,6−トリメチル−1,4,5−トリアセチルグルシトールと2,3,4−トリメチル−1,5,6−トリアセチルグルシトールとの合計が部分メチル化グルシトールアセテートの60%以上を占める;(3)2,4,6−トリメチル−1,3,5−トリアセチルグルシトールが部分メチル化グルシトールアセテートの0.5%以上10%未満である;及び(4)2,4−ジメチル−1,3,5,6−テトラアセチルグルシトールが部分メチル化グルシトールアセテートの0.5%以上である;ことを特徴とする分岐α−グルカンと当該分岐α−グルカンを生成する新規なα−グルコシル転移酵素、それらの製造方法並びに用途を提供することによって、上記課題を解決する。【選択図】なし | ||||||
| 12 | BRANCHED α-GLUCAN, α-GLUCOSYL TRANSFERASE FOR PRODUCING THE SAME, AND MANUFACTURING METHOD AND USE THEREFOR | JP2010262148 | 2010-11-25 | JP2011078426A | 2011-04-21 | WATANABE HIKARU; YAMAMOTO TAKUO; NISHIMOTO TOMOYUKI; TSUZAKI KEIJI; OKU KAZUYUKI; CHAEN HIROTO; FUKUDA SHIGEHARU |
| <P>PROBLEM TO BE SOLVED: To provide a glucan useful as water-soluble dietary fiber, its preparation and uses. <P>SOLUTION: There is provided a branched α-glucan which is an α-glucan making glucose as a constitution sugar and has a branched structure with a glucose polymerization degree of 1 or more connected to at least non-reduction terminal glucose residue positioned at an end of a linear glucan with a glucose polymerization degree of 3 or more connected through an α-1,4 bond through a bond other than the α-1,4 bond. A new α-glucosyl transferase for producing the branched α-glucan, and a process and use of the same. <P>COPYRIGHT: (C)2011,JPO&INPIT | ||||||
| 13 | Enzymatic hydrolysis for conversion of c-7 sugar-containing taxane to c-7 hydroxyl-containing taxane | JP388095 | 1995-01-13 | JPH07203981A | 1995-08-08 | RONARUDO ERU HANSON; RAMESHIYU ENU PATERU; RAZURO JIEI ZARUKA |
| PURPOSE: To industrially advantageously obtain the subject compound for medicines, etc., by inoculating taxane containing sugar group directly binding to C-7 with an enzyme, etc., capable of catalyzing hydrolysis of the sugar group to hydroxyl group to hydrolyze the taxane. CONSTITUTION: At least one kind of C-7 sugar-containing taxane (salt) of formula I (R 1 and R 2 are each hydroxyl or an acyloxy; R 3 and R 4 are each H, an alkyl, an alkenyl, an alkynyl, a cycloalkyl, a cycloalkenyl, an aryl or a heterocycle) is brought into contact with an enzyme (e.g. xylosidase) or a microorganism (e.g. Bacillus macerans) capable of catalyzing hydrolysis of sugar group to hydroxyl group to provide the objective taxanes represented by formula II, etc., and useful as a pharmacologically active antitumor agent, etc., such as paclitaxel and containing hydroxyl group directly bound to C-7. COPYRIGHT: (C)1995,JPO | ||||||
| 14 | JPH0341477B2 - | JP2757282 | 1982-02-24 | JPH0341477B2 | 1991-06-24 | |
| A novel peptide antibiotic complex designated herein as Bu-2470 is produced by fermentation of Bacillus circulans strain G493-B6 (ATCC 31,805). Complex Bu-2470 may be separated into four bioactive peptide antibiotics designated as Bu-2470A, B1, B2a, and B2b. The complex and individual bioactive factors possess significant antimicrobial activity. | ||||||
| 15 | Production of novel lactase | JP6434777 | 1977-05-31 | JPS53148591A | 1978-12-25 | IIDA TAKAO; OZAKI AKIRA; ODAKA TOSHIHIKO |
| A novel lactase having a molecular weight of about 3x105, an optimum pH value of about 6.0, an optimum temperature of about 60 DEG C. and at least 1 of the ratio of the activity for hydrolyzing lactose to the activity for hydrolyzing a synthetic substrate: o-nitrophenyl- beta -D-galactopyranoside (Lact/ONPG ratio), which is produced by cultivating a microorganism of the genus Bacillus being capable of producing the enzyme, particularly Bacillus circulans LOB 377 (ATCC No. 31382) and isolating from the culture broth. This novel lactase is characteristic in the excellent thermostability and the high Lact/ONPG ratio and hence is useful for treating milk and milk products as well as for preventing diarrhea due to lactose intolerance, especially in babies and infants. | ||||||
| 16 | 分岐α−グルカン及びこれを生成するα−グルコシル転移酵素とそれらの製造方法並びに用途 | JP2014152414 | 2014-07-25 | JP2014218677A | 2014-11-20 | WATANABE HIKARU; YAMAMOTO TAKUO; NISHIMOTO TOMOYUKI; TSUZAKI KEIJI; OKU KAZUYUKI; CHAEN HIROTO; FUKUDA SHIGEHARU |
| 【課題】水溶性食物繊維として有用なグルカンとその製造方法並びにその用途を提供することを課題とする。【解決手段】グルコースを構成糖とするα−グルカンであって、メチル化分析において、(1)2,3,6−トリメチル−1,4,5−トリアセチルグルシトールと2,3,4−トリメチル−1,5,6−トリアセチルグルシトールの比が1:0.6乃至1:4の範囲にある;(2)2,3,6−トリメチル−1,4,5−トリアセチルグルシトールと2,3,4−トリメチル−1,5,6−トリアセチルグルシトールとの合計が部分メチル化グルシトールアセテートの60%以上を占める;(3)2,4,6−トリメチル−1,3,5−トリアセチルグルシトールが部分メチル化グルシトールアセテートの0.5%以上10%未満である;及び(4)2,4−ジメチル−1,3,5,6−テトラアセチルグルシトールが部分メチル化グルシトールアセテートの0.5%以上である;ことを特徴とする分岐α−グルカンと当該分岐α−グルカンを生成する新規なα−グルコシル転移酵素、それらの製造方法並びに用途を提供することによって、上記課題を解決する。【選択図】なし | ||||||
| 17 | Branch α- glucan and to generate this α- glucosyltransferase and their preparation and uses | JP2013151138 | 2013-07-19 | JP5449604B2 | 2014-03-19 | 光 渡邊; 拓生 山本; 友之 西本; 桂二 津▲崎▼; 和之 奥; 博人 茶圓; 恵温 福田 |
| 18 | BRANCHED α-GLUCAN, α-GLUCOSYL TRANSFERASE FOR PRODUCING THE SAME, AND MANUFACTURING METHOD AND USE THEREFOR | JP2010132649 | 2010-06-10 | JP2010202882A | 2010-09-16 | WATANABE HIKARU; YAMAMOTO TAKUO; NISHIMOTO TOMOYUKI; TSUZAKI KEIJI; OKU KAZUYUKI; CHAEN HIROTO; FUKUDA SHIGEHARU |
| <P>PROBLEM TO BE SOLVED: To provide glucan useful as a water-soluble dietary fiber, a manufacturing method and use therefor. <P>SOLUTION: The branched α-glucan is an α-glucan making glucose as a constitution sugar and has a branched structure with a glucose polymerization degree of 1 or more connected to at least a non-reduction terminal end in a linear glucan with a glucose polymerization degree of 3 or more connected through an α-1,4 bond through a bond other than the α-1,4 bond, specifically is the branched α-glucan having the following characteristic in methylation analysis. The branched α-glucan characterized in that (1) a ratio of 2,3,6-trimethyl-1,4,5-triacetylglucitol to 2,3,4-trimethyl-1,5,6-triacetylglucitol is in a range of 1:0.6 to 1:4, (2) a total of 2,3,6-trimethyl-1,4,5-triacetylglucitol and 2,3,4-trimethyl-1,5,6-triacetylglucitol occupies 60% or more of a partially methylated glucitolacetate, (3) 2,4,6-trimethyl-1,3,5-triacetylglucitol is ≥0.5% and <10% of the partially methylated glucitolacetate, and (4) 2,4-dimethyl-1,3,5,6-tetraacetylglucitol is 0.5% or more of the partially methylated glucitolacetate, the novel α-glucosyl transferase for producing the branched α-glucan, the manufacturing methods and use therefor are provided. <P>COPYRIGHT: (C)2010,JPO&INPIT | ||||||
| 19 | 分岐α−グルカン及びこれを生成するα−グルコシル転移酵素とそれらの製造方法並びに用途 | JP2009512944 | 2008-04-23 | JPWO2008136331A1 | 2010-07-29 | 光 渡邊; 山本 拓生; 拓生 山本; 西本 友之; 友之 西本; 津▲崎▼ 桂二; 桂二 津▲崎▼; 奥 和之; 和之 奥; 茶圓 博人; 博人 茶圓; 福田 恵温; 恵温 福田 |
| 水溶性食物繊維として有用なグルカンとその製造方法並びにその用途を提供することを課題とし、グルコースを構成糖とするα−グルカンであって、メチル化分析において、下記の特徴を有する分岐α−グルカン:(1)2,3,6−トリメチル−1,4,5−トリアセチルグルシトールと2,3,4−トリメチル−1,5,6−トリアセチルグルシトールの比が1:0.6乃至1:4の範囲にある;(2)2,3,6−トリメチル−1,4,5−トリアセチルグルシトールと2,3,4−トリメチル−1,5,6−トリアセチルグルシトールとの合計が部分メチル化グルシトールアセテートの60%以上を占める;(3)2,4,6−トリメチル−1,3,5−トリアセチルグルシトールが部分メチル化グルシトールアセテートの0.5%以上10%未満である;及び(4)2,4−ジメチル−1,3,5,6−テトラアセチルグルシトールが部分メチル化グルシトールアセテートの0.5%以上である;ことを特徴とする分岐α−グルカンと当該分岐α−グルカンを生成する新規なα−グルコシル転移酵素、それらの製造方法並びに用途を提供することによって上記課題を解決する。 | ||||||
| 20 | New heparitinases, their production and microorganism producing the same | JP6370791 | 1991-03-06 | JPH04278087A | 1992-10-02 | MORIKAWA KIYOSHI; MIYAZONO HIROBUMI; MARUYAMA HIROSHI; YOSHIDA KEIICHI |
| PURPOSE: To obtain the subject new enzymes useful as a low-molecular heparin- forming agent, etc., in preparing a low-molecular heparin such as an antithrombotic agent by culturing a bacterium, belonging to the genus Bacillus and having the ability to produce heparitinases T-I to T-IV and collecting the resultant product from a culture solution or a microbial cell extract solution. CONSTITUTION: A bacterium, belonging to the genus Bacillus and having the ability to produce heparitinase T-I, heparitinase T-II, heparitinase T-III and heparitinase T-IV is cultured and the resultant product is then collected from its culture solution or a microbial extract solution. Thereby, the objective new enzymes heparitinase T-I (optimum pH; 5.5-6.5, optimum temperature; 55°C), heparitinase T-II (optimum pH; 5.5-6.5, optimum temperature; 55°C), heparitinase T-III (optimum pH; 7.0-8.0, optimum temperature; 50°C) and heparitinase T-IV (optimum pH; 7.0-8.0, optimum temperature; 40°C) which are lyases, acting on glycosaminide bonds of heparin and heparan sulfate and forming double bonds between the 4- and 5-positions of glucuronic acid or iduronic acid at the cleaved site are obtained. COPYRIGHT: (C)1992,JPO&Japio | ||||||
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