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序号 专利名 申请号 申请日 公开(公告)号 公开(公告)日 发明人
461 Non-reducing saccharide-forming enzyme, trehalose-releasing enzyme, and process for producing saccharides using the enzymes EP99307220.6 1999-09-13 EP0990704A2 2000-04-05 Yamamoto, Takuo; Maruta, Kazuhiko; Kubota, Michio; Fukuda, Shigeharu; Miyake, Toshio

A non-reducing saccharide-forming enzyme and a trehalose-releasing enzyme, which have an optimum temperature in a medium temperature range, i.e., a temperature of over 40 or 45°C but below 60°C; and an optimum pH in an acid pH range, i.e., a pH of less than 7. The two-types of enzymes can be obtained in a desired amount, for example, by culturing in a nutrient culture medium microorganisms capable of producing the enzymes or by recombinant DNA technology.

462 Polynucleotides encoding trehalose-6-phosphate phosphatase and methods of use thereof US13549794 2012-07-16 US09121033B2 2015-09-01 Kateri Duncan; Michael L. Nuccio; Weining Gu
The present invention relates generally to the field of molecular biology and regards various polynucleotides, polypeptides and methods that may be employed to enhance yield in transgenic plants. Specifically the transgenic plants may exhibit any one of the traits consisting of increased yield, increased tolerance to abiotic stress, increased cell growth and increased nutrient use efficiency.
463 Recombinant thermostable enzyme for converting maltose into trehalose from Thermus aquaticus US537002 1995-09-29 US5773282A 1998-06-30 Keiji Tsusaki; Michio Kubota; Toshiyuki Sugimoto
Disclosed are a recombinant thermostable enzyme, which converts maltose into trehalose and is stable up to a temperature of about 80.degree. C. even when incubated at pH 7.0 for 60 min, a preparation of the enzyme, a DNA encoding the enzyme, a recombinant DNA containing the DNA, a transformant, and an enzymatic conversion method of maltose by using the enzyme.
464 Recombinant enzyme for converting maltose into trehalose from pimelobacter sp. US528199 1995-09-14 US5763228A 1998-06-09 Michio Kubota; Keiji Tsusaki; Toshiyuki Sugimoto
A recombinant enzyme, having a molecular weight of about 57,000-67,000 daltons on SDS-PAGE and a pI of about 4.1-5.1 on isoelectrophoresis, which converts maltose into trehalose and vice versa. Depending on the enzymatic conditions, the enzyme forms about 70 w/w % of trehalose when acts on maltose, while about 20 w/w % of maltose when acts on trehalose. The culture of a transformant, prepared by introducing into a host a recombinant DNA containing a DNA coding for the enzyme and a self-replicable vector, facilitates the industrial-scale production of trehalose.
465 "Alga species lobsphaera TM-33 (ATCC 75630) which is useful for preparing trehalase" US231318 1994-04-22 US5529927A 1996-06-25 Sumio Kitahata; Hirofumi Nakano; Tsutomu Washino; Masamitsu Moriwaki
Novel trehalase having the properties that it hydrolyzes .alpha.,.alpha.'-trehalose, 2,2'-dideoxy-.alpha.,.alpha.'-trehalose and 2-deoxy-.alpha.,.alpha.'-trehalose into the respective constituting sugars while it does not act on neotrehalose, lactose, maltose, celobiose and sucrose; its optimum pH is 5 to 6; its optimum temperature is 65.degree. C.; it is stable against heating up to 65.degree. C.; its molecular weight as measured by a gel filtration is 400,000 to 500,000 while the molecular weight of the subunit as measured by a sodium dodecylsulfate--polyacrylamide gel electrophoresis is 180,000 to 250,000; its isoelectric point as measured by an isoelectricfocusing is 2.7; and it is a glycoprotein.
466 PROCESS FOR PRODUCING ETHANOL FROM A HYDROLYSATE OF THE HEMICELLULOSE FRACTION OF SUGARCANE BAGASSE IN A PRESS REACTOR US12667369 2007-07-03 US20100273228A1 2010-10-28 Lidia Maria Melo Sant'Anna; Nei Pereira; Gabriel Jamie Vargas Bitancur; Juliana Vaz Bevilaqua; Absai da Conceicao Gomes; Emerson Pires Menezes
The invention is a process for producing ethanol from sugarcane bagasse, the principal steps of which are mild sulphuric acid hydrolysis of the hemicellulose fraction of the sugarcane bagasse, followed by extraction of the hydrolysate and then fermentation thereof with the yeast Pichia stipitis. The process can be carried out with different solid : liquid ratios, and provides a step of acclimatizing the Pichia stipitis yeast, which results in a greater rate of ethanol production. The process takes place in a press reactor specially designed for this purpose, which allows more efficient extraction of the hydrolysate and, as a consequence, better process performance.
467 Methods for the identification of inhibitors of Trehalose-6-Phosphate Synthase as antibiotics US10703292 2003-11-07 US20040146960A1 2004-07-29 Blaise Darveaux; Sanjoy Mahanty; Ryan Heiniger; Amy Covington; Huaqin Pan; Rex Tarpey; Jeffrey Shuster; Matthew M. Tanzer; Lisbeth Hamer; Kiichi Adachi; Todd DeZwaan; Sze-Chung Lo; Maria Victoria Montenegro-Chamorro; Sheryl Frank
The present inventors have discovered that Trehalose-6-Phosphate Synthase is essential for normal fungal pathogenicity. Specifically, the inhibition of Trehalose-6-Phosphate Synthase gene expression in fungi results in reduced pathogenicity (i.e. smaller, non-viable lesions). Thus, Trehalose-6-Phosphate Synthase can be used as a target for the identification of antibiotics, preferably antifungals. Accordingly, the present invention provides methods for the identification of compounds that inhibit Trehalose-6-Phosphate Synthase expression or activity. The methods of the invention are useful for the identification of antibiotics, preferably antifungals.
468 USE OF SEA CUCUMBER GLYCOSAMINOGLYCAN IN PREPARING MEDICINE FOR PREVENTION AND TREATMENT OF THROMBOEMBOLIC DISEASE US14890854 2014-05-07 US20160082051A1 2016-03-24 Zhiguo Wang; Quanhai Liu; Xuehai Wu
The present invention discloses use of sea cucumber glycosaminoglycan in the preparation of drugs. In particular, the present invention relates to use of medical use of sea cucumber glycosaminoglycan, and more particularly to use of depolymerized sea cucumber glycosaminoglycan or natural molecular segments of sea cucumber glycosaminoglycan with a weight average molecular weight greater than 54,500 Da in the preparation of a drug for the prevention and treatment of thromboembolic diseases. Thromboembolic diseases include atherosclerotic thrombotic diseases, venous thromboembolic diseases, hypercoagulable states and postoperative thrombosis or treatment of postoperative thrombi. The present invention has a wide treatment window for thromboembolic diseases, has a higher level of safety, and has good development and research value.
469 Sequence-determined DNA fragments encoding trehalose-6P phosphatase proteins US14301826 2014-06-11 US09068173B2 2015-06-30 Nickolai Alexandrov; Vyacheslav Brover; Kenneth Feldmann
The present invention provides DNA molecules that constitute fragments of the genome of a plant, and polypeptides encoded thereby. The DNA molecules are useful for specifying a gene product in cells, either as a promoter or as a protein coding sequence or as an UTR or as a 3′ termination sequence, and are also useful in controlling the behavior of a gene in the chromosome, in controlling the expression of a gene or as tools for genetic mapping, recognizing or isolating identical or related DNA fragments, or identification of a particular individual organism, or for clustering of a group of organisms with a common trait.
470 OtsA gene encoding trehalose-6-phosphate synthase from a coryneform bacterium US10637551 2003-08-11 US07307160B1 2007-12-11 Hiromi Ohtaki; Jun Nakamura; Hiroshi Izui; Tsuyoshi Nakamatsu
L-Glutamic acid is produced by culturing a coryneform bacterium having L-glutamic acid producing ability, in which trehalose synthesis ability is decreased or deleted by, for example, disrupting the otsA gene derived from a coryneform bacterium source, coding for trehalose-6-phosphate synthase, to produce and accumulate L-glutamic acid in the medium, and collecting the L-glutamic acid from the medium.
471 Immobilized acetylcholinesterase stabilized by a film of gelatin or albumin containing trehalose US405816 1995-03-16 US5624831A 1997-04-29 Nguyen Vu Khue; Phillippe Poindron; Roland Maes
Acetylcholinesterase and/or a receptor of acetylcholinesterase is immobilized on a solid support and stabilized by covering with a protective film of gelatin and/or albumin containing trehalose. The film is applied by covering the immobilized acetylcholinesterase and/or receptor of acetylcholinesterase with a layer of a gel-forming solution of gelatin or albumin in an evaporable solvent containing dissolved trehalose, and evaporating the solvent to leave the film. The film provides stability against dry heat, organic solvents, proteases and changes in pH. Other additives such as polyhydric alcohols, organic solvents, polymers and/or ionic and non-ionic components may be present to increase stabilization. A diagnostic kit or chromatography column may be formed containing the stabilized immobilized acetylcholinesterase and/or receptor of acetylcholinesterase.
472 Trehalase and a method of manufacturing sugars by said enzyme EP94105701.0 1994-04-13 EP0661381A3 1995-11-29 Kitahata, Sumio; Nakano, Hirofumi; Washino, Tsutomu; Moriwaki, Masamitsu

Novel trehalase having the properties that it hydrolyzes α,α'-trehalose, 2,2'-dideoxy-α,α'-trehalose and 2-deoxy-α,α'-trehalose into the respective constituting sugars while it does not act on neotrehalose, lactose, maltose, celobiose and sucrose; its optimum pH is 5 to 6; its optimum temperature is 65°C; it is stable against heating up to 65°C; its molecular weight as measured by a gel filtration is 400,000 to 500,000 while the molecular weight of the subunit as measured by a sodium dodecylsulfate - polyacrylamide gel electrophoresis is 180,000 to 250,000; its isoelectric point as measured by an isoelectricfocusing is 2.7; and it is a glycoprotein.

473 Trehalase and a method of manufacturing sugars by said enzyme EP94105701.0 1994-04-13 EP0661381A2 1995-07-05 Kitahata, Sumio; Nakano, Hirofumi; Washino, Tsutomu; Moriwaki, Masamitsu

Novel trehalase having the properties that it hydrolyzes α,α'-trehalose, 2,2'-dideoxy-α,α'-trehalose and 2-deoxy-α,α'-trehalose into the respective constituting sugars while it does not act on neotrehalose, lactose, maltose, celobiose and sucrose; its optimum pH is 5 to 6; its optimum temperature is 65°C; it is stable against heating up to 65°C; its molecular weight as measured by a gel filtration is 400,000 to 500,000 while the molecular weight of the subunit as measured by a sodium dodecylsulfate - polyacrylamide gel electrophoresis is 180,000 to 250,000; its isoelectric point as measured by an isoelectricfocusing is 2.7; and it is a glycoprotein.

474 Non-reducing saccharide-forming enzyme, trehalose-releasing enzyme, and process for producing saccharides using the enzymes US11564493 2006-11-29 US07575900B2 2009-08-18 Takuo Yamamoto; Kazuhiko Maruta; Michio Kubota; Shigeharu Fukuda; Toshio Miyake
A non-reducing saccharide-forming enzyme and a trehalose-releasing enzyme, which have an optimum temperature in a medium temperature range, i.e., a temperature of over 40 or 45° C. but below 60° C.; and an optimum pH in an acid pH range, i.e., a pH of less than 7. The two-types of enzymes can be obtained in a desired amount, for example, by culturing in a nutrient culture medium microorganisms capable of producing the enzymes or by recombinant DNA technology.
475 USE OF TREHALOSE-6-PHOSPHATE SYNTHASE TO MODULATE PLANT GROWTH EP07703096.3 2007-01-29 EP1989312A1 2008-11-12 LEYMAN, Barbara; RAMON, Matthew; ROLLAND, Filip; THEVELEIN, Johan; VAN DIJCK, Patrick; VANDESTEENE, Lies
The present invention relates to the use of trehalose-6-phosphate synthase to modulate plant growth. More specifically, it relates to the use of a class Il trehalose-6-phosphate synthase, comprising both a synthase and a phosphatase-like part to modulate plant growth. Preferably, the activity of trehalose-6-phosphate synthase is downregulated to obtain an increased plant biomass yield.
476 USE OF TREHALOSE-6-PHOSPHATE SYNTHASE TO MODULATE PLANT GROWTH EP07703096.3 2007-01-29 EP1989312B1 2011-10-19 LEYMAN, Barbara; RAMON, Matthew; ROLLAND, Filip; THEVELEIN, Johan; VAN DIJCK, Patrick; VANDESTEENE, Lies
The present invention relates to the use of trehalose-6-phosphate synthase to modulate plant growth. More specifically, it relates to the use of a class Il trehalose-6-phosphate synthase, comprising both a synthase and a phosphatase-like part to modulate plant growth. Preferably, the activity of trehalose-6-phosphate synthase is downregulated to obtain an increased plant biomass yield.
477 Trehalose releasing enzyme, DNA encoding therefor, their preparation and uses EP95301474.3 1995-03-07 EP0671470B9 2004-11-03 Kubota, Michio; Tsusaki, Keiji; Hattori, Kazuko; Sugimoto, Toshiyuki
478 POLYPEPTIDES HAVING TREHALASE ACTIVITY AND THE USE THEREOF IN PROCESS OF PRODUCING FERMENTATION PRODUCTS EP16734780.6 2016-06-13 EP3310910A1 2018-04-25 KANG, Zhengfang; SCHNORR, Kirk Matthew; SKOV, Lars Kobberøe
The present invention relates to polypeptides having trehalase activity. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using a trehalase of the invention, in particular a process of producing a fermentation product, such as ethanol.
479 USE OF TREHALASE GENES TO CONFER NEMATODE RESISTANCE TO PLANTS EP08708688.0 2008-02-05 EP2111456A1 2009-10-28 WIIG, Aaron; HUANG, Xiang; CHAUDHURI, Sumita
The invention provides transgenic plants that exhibit increased resistance to nematode infection by virtue of overexpression of a gene that encodes trehalase in nematode-induced syncytia. Expression vectors comprising trehalase-encoding polynucleotides and methods of employing such vectors to increase nematode resistance of plants are also provided.
480 Maltose-trehalose converting enzyme, and preparation and uses thereof EP94305342.1 1994-07-20 EP0636693B1 2005-12-28 Nishimoto, Tomoyuki; Chaen, Hiroto; Sugimoto, Toshiyuki; Miyake, Toshio
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