JP2002517157A - スルホロブス由来の熱安定性イソアミラーゼを使用する澱粉転化法 - Google Patents
スルホロブス由来の熱安定性イソアミラーゼを使用する澱粉転化法Info
- Publication number
- JP2002517157A JP2002517157A JP50617399A JP50617399A JP2002517157A JP 2002517157 A JP2002517157 A JP 2002517157A JP 50617399 A JP50617399 A JP 50617399A JP 50617399 A JP50617399 A JP 50617399A JP 2002517157 A JP2002517157 A JP 2002517157A
- Authority
- JP
- Japan
- Prior art keywords
- isoamylase
- dna sequence
- enzyme
- strain
- rhodothermus
- 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
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- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01068—Isoamylase (3.2.1.68)
Abstract
Description
Claims (1)
- 【特許請求の範囲】 1.支配的なプロセス条件において活性であるイソアミラーゼを澱粉の脱分枝 鎖に使用することを特徴する、分枝鎖切断工程を含む型の澱粉転化法。 2.イソアミラーゼがα−アミラーゼと一緒に液化工程の間に活性であること を特徴とする、液化工程および糖化工程をを含む澱粉解重合法である、請求項1 に記載の澱粉転化法。 3.活性イソアミラーゼが熱安定性イソアミラーゼである、請求項1および2 に記載の方法。 4.熱安定性イソアミラーゼがスルホロブス(Sulfolobus)属、例えば、スル ホロブス・アシドカルダリウス(Sulfolobus acidocaldarius)、およびロドテル ムス(Rhodothermus)属、例えば、ロドテルムス・マリナス(Rhodothermus mar inus)の好熱性株に由来する、請求項1〜3のいずれか一項に記載の方法。 5.液化工程を4.5〜6.5、好ましくは約5.5のpH値、105〜110 ℃の温度において5〜10分間実施し、次いで90〜100℃において、1〜3 時間、好ましくは約2時間実施する、請求項2〜4のいずれか一項に記載の方法 。 6.液化工程を4.5〜6.5、好ましくは約5.5のpH値、70〜110℃ 、好ましくは約80℃の温度において30〜180分間、好ましくは約80分間 、α−アミラーゼ、必要に応じてイソアミラーゼの存在において実施する、請求 項2〜4のいずれか一項に記載の方法。 7.液化に引き続いて、糖化工程を50〜80℃の温度、pH4.5〜6.5、 好ましくは4.5の範囲のpHにおいて、24〜72時間、好ましくは48時間、 AMGおよび必要に応じてイソアミラー ゼの存在において実施する、請求項6に記載の方法。 8.カルシウムを0.75〜1.25mM、例えば、約1mMの量で添加する、請求項2〜 7のいずれか一項に記載の方法。 9.糖化工程後に、液化α−アミラーゼを不活性化する、請求項2〜8のいず れか一項に記載の方法。 10.α−アミラーゼがバシラス・リヘニフォルミス(Bacillus licheniform is)のα−アミラーゼまたはバシラス・ステアロサーモフィラス(Bacillus stea rothermophilus)のα−アミラーゼまたはピロコッカス・フリオスス(Pyrococcus furiosus)のα−アミラーゼである、請求項2〜9のいずれか一項に記載の方法 。 11.糖化工程に引き続いて、異性化工程を実施する、請求項2〜10のいず れか一項に記載の方法。 12.高フルクトースシロップを製造する、請求項2〜11のいずれか一項に 記載の方法。 13.脂肪代替物を製造する、請求項1、3および4に記載の方法。 14.澱粉の液化のためのα−アミラーゼと組み合わせた熱安定性イソアミラ ーゼの使用。 15.澱粉の糖化のためのAMGと組み合わせた熱安定性イソアミラーゼの使 用。 16.熱安定性イソアミラーゼがスルホロブス(Sulfolobus)属、例えば、ス ルホロブス・アシドカルダリウス(Sulfolobus acidocaldarius)、およびロドテ ルムス(Rhodothermus)属、例えば、ロドテルムス・マリナス(Rhodothermus m arinus)の好熱性株に由来する、請求項15に記載の使用。 17.高フルクトースシロップを製造する、請求項15または17に記載の使 用。 18.α−アミラーゼがバシラス(Bacillus)属、例えば、バシラス・リヘニ フォルミス(B.licheniformis)の株に由来する、請求項15〜17のいずれか 一項に記載の使用。 19.澱粉から脂肪代替物を製造するための、熱安定性イソアミラーゼの使用 。 20.熱安定性イソアミラーゼがスルホロブス(Sulfolobus)属、例えば、ス ルホロブス・アシドカルダリウス(Sulfolobus acidocaldarius)、およびロドテ ルムス(Rhodothermus)属、例えば、ロドテルムス・マリナス(Rhodothermus m arinus)の好熱性株に由来する、請求項19に記載の使用。 21.ロドテルムス(Rhodothermus)属の株から得られ、そして i)50℃ において測定して、3.5〜6.5のpH範囲、最適にはpH約5においてイソアミ ラーゼ活性; ii)SDS-PAGEにより測定して、約80kDaの分子量;および iii)5.2〜5.8の範囲の等電点(pI); を有する、イソアミラーゼ活性を有する単離されたポリペプチド。 22.イソアミラーゼ活性を示す酵素をコードし、 (a)大腸菌(E.coli)DSM11971の中に存在するプラスミドpUC19の中にクロ ーニングされたDNA配列のイソアミラーゼをコードする部分; (b)配列番号:3中の位置1〜2178に示すDNA配列またはその相補的スト ランド; (c)前記DNA配列と少なくとも70%相同性である、(a)または(b) において規定されるDNA配列のアナローグ; (d)配列番号:3中の位置1〜2178に示す配列からなる二本鎖DNAのプロ ーブに対して低いストリンジェンシイにおいてハイブリダイゼーションするDN A配列; (e)遺伝暗号のデジェネラシーのために、(b)または(d)の配列とハイ ブリダイゼーションしないが、これらのDNA配列のいずれかによりコードされ るポリペプチドと正確に同一のアミノ酸配列を有するポリペプチドをコードする DNA配列;または (f)(a)、(b)、(c)、(d)または(e)において特定したDNA 配列のフラグメントであるDNA配列; からなるクローニングされたDNA配列。 23.イソアミラーゼ活性を示し、 (a)大腸菌(E.coli)DSM11971の中に存在するプラスミドpUC19の中にクロ ーニングされたDNA配列のイソアミラーゼをコードする部分によりコードされ るポリペプチド; (b)配列番号:4中の位置1〜726に示すアミノ酸配列からなるポリペプ チド; (c)前記ポリペプチドと少なくとも70%相同性である(a)または(b) において規定されるポリペプチドのアナローグ;および (d)(a)、(b)または(c)のフラグメント; から成る群より選択される、単離された酵素。 24.前記株がロドテルムス・マリナス(Rhodothermus marinus)、特にロド テルムス・マリナス(Rhodothermus marinus)DMS4252である、請求項21に記 載の単離されたポリペプチド。 25.イソアミラーゼ活性を示す酵素をコードするDNA配列が、微生物、好 ましくは糸状菌、酵母、または細菌から得られる、請求項22に記載のクローニ ングされたDNA配列。 26.DNA配列がシトファガレス(Cytophagales)目の株、例えば、ロドテ ルムス(Rhodothermus)属の株、特にロドテルムス・マリナス(Rhodothermus m arinus)またはロドテルムス・オバメン シス(Rhodothermus obamensis)の株から得られる、請求項25に記載のクロー ニングされたDNA配列。 27.DNA配列がロドテルムス・マリナス(Rhodothermus marinus)DMS425 2株のDNAライブラリーからクローニングされるか、あるいは前記DNAライ ブラリーをベースとして産生される、請求項26に記載のクローニングされたD NA配列。 28.DNA配列が大腸菌(E.coli)DSM11971からクローニングされる、請求 項22に記載のクローニングされたDNA配列。 29.ポリペプチドが、微生物、好ましくは糸状菌、酵母、または細菌から得 られる、請求項23に記載の単離された酵素。 30.細菌の株がロドテルムス(Rhodothermus)属の株、ロドテルムス・マリ ナス(Rhodothermus marinus)の株である、請求項29に記載の単離された酵素 。 31.請求項22および25〜28〜のいずれか一項に記載のクローニングさ れたDNA配列からなる組換え発現ベクター。 32.請求項22および25〜28〜のいずれか一項に記載のクローニングさ れたDNA配列または請求項31に記載の組換え発現ベクターからなる宿主細胞 。 33.真核細胞、特に菌類細胞、例えば、酵母細胞または糸状菌細胞である、 請求項32に記載の宿主細胞。 34.フザリウム(Fusarium)、アスペルギルス(Aspergillus)、トリコデ ルマ(Trichoderma)、サッカロマイセス(Saccharomyces)、カンジダ(Candida)、 ピキア(Pichia)、ハンゼヌラ(Hansenula)の株、特にフザリウム(Fusarium)A TCC 20334の同定特性を有するフザリウム(Fusarium)種、アスペルギルス・ニ ガー(Aspergillus niger)、アスペルギルス・オリゼ(Aspergillus oryzae)、 トリコデルマ・ハルジアナム(Trichoderma harzianum)、トリコデ ルマ・リーシエ(Trichoderma reesie)、サッカロミセス・セレビシエ(Saccha romyces cerevisiae)、カンジダ・ウチリス(Candida utilis)、カンジダ・ボ イディニ(Candida boidini)、ピキア・メタノリカ(Pichia metanolica)、ピキア ・アングスタ(Pichia angusta)、ピキア・パストリス(Pichia pastoris)また はピキア・アノマラ(Pichia anomala)の株である、請求項33に記載の宿主細 胞。 35.原核細胞、特に細菌細胞である、請求項32に記載の宿主細胞。 36.バシラス(Bacillus)、ラクトバシラス(Lactobacillus)、ブレヴィ バシラス(Brevibacillus)、ストレプトマイセス(Streptomyces)、エシェリキ ア(Escherichia)、特にバシラス・サチリス(Bacillus subtilis)、バシラス・ス テアロサーモフィラス(Bacillus stearothermophilus)、バシラス・リヘニフォ ルミス(Bacillus licheniformis)、バシラス・レンツス(Bacillus lentus)ま たは大腸菌(Escherichia coli)の株である、請求項35に記載の宿主細胞。 37.酵素の産生を可能とする条件下に、請求項32〜36のいずれか一項に 記載の細胞を培養し、そして培養物から酵素を回収することからなる、イソアミ ラーゼ活性を示す酵素を生産する方法。 38.(i)相同的不純物を含有せず、そして(ii)酵素が請求項36に記 載の方法に従い、請求項32〜36のいずれか一項に記載の宿主細胞を使用して 生産されていること特徴とする、イソアミラーゼ活性を示す単離された酵素。 39.請求項38に記載の酵素、または請求項37に記載の方法に従い産物さ れた酵素を含んでなる組成物。 40.澱粉の転化のための請求項38に記載の酵素、または請求 項39に記載の酵素組成物の使用。 41.請求項1〜13のいずれか一項に記載の方法における請求項40に記載 の使用。 42.寄託された大腸菌(E.coli)DSM11971株の単離された実質的に純粋な生 物学的培養物。 43.スルホロブス(Sulfolobus)の株に由来するイソアミラーゼ活性を有す る酵素をコードするクローニングされたDNA配列。 44.DNA配列がスルホロブス・アシドカルダリウス(Sulfolobus acidocal darius)またはスルホロブス・ソルファタリカス(Sulfolobus solfataricus)の株 に由来する、請求項43に記載のクローニングされたDNA配列。 45.請求項43または44に記載のクローニングされたDNA配列からなる 組換え発現ベクター。 46.請求項43または44に記載のクローニングされたDNA配列または請 求項45に記載の組換え発現ベクターを含む宿主細胞。 47.真核細胞、特に菌類細胞、例えば、酵母細胞または糸状菌細胞である、 請求項46に記載の宿主細胞。 48.サッカロマイセス(Saccharomyces)、カンジダ(Candida)、ピキア(Pi chia)、ハンゼヌラ(Hansenula)、フザリウム(Fusarium)、アスペルギルス(As pergillus)、トリコデルマ(Trichoderma)の株、特にサッカロミセス・セレビシ エ(Saccharomyces cerevisiae)、カンジダ・ウチリス(Candida utilis)、カ ンジダ・ボイディニ(Candida boidini)、ピキア・メタノリカ(Pichia metanolic a)、ピキア・アングスタ(Pichia angusta)、ピキア・パストリス(Pichia past oris)、ピキア・アノマラ(Pichia anomala)、フザリウム(Fusarium)ATCC 20 334、アスペルギルス・ニガー(As pergillus niger)、アスペルギルス・オリゼ(Aspergillus oryzae)、トリコデ ルマ・ハルジアナム(Trichoderma harzianum)またはトリコデルマ・リーシエ(T richoderma reesie)の株である、請求項47に記載の宿主細胞。 49.酵素の産生を可能とする条件下に、請求項46〜49のいずれか一項に 記載の細胞を培養し、そして培養物から酵素を回収することからなる、請求項4 3に記載のクローニングされたDNA配列によりコードされるイソアミラーゼ活 性を示す酵素を生産する方法。
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DK0787/97 | 1997-07-02 | ||
DK78797 | 1997-07-02 | ||
US5586797P | 1997-08-13 | 1997-08-13 | |
PCT/DK1998/000304 WO1999001545A1 (en) | 1997-07-02 | 1998-07-02 | STARCH CONVERSION PROCESS USING THERMOSTABLE ISOAMYLASES FROM $i(SULFOLOBUS) |
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US (2) | US6087149A (ja) |
EP (1) | EP1002062B1 (ja) |
JP (1) | JP4087463B2 (ja) |
AT (1) | ATE325188T1 (ja) |
AU (1) | AU8102698A (ja) |
DE (1) | DE69834403T2 (ja) |
DK (1) | DK1002062T3 (ja) |
ES (1) | ES2263209T3 (ja) |
WO (1) | WO1999001545A1 (ja) |
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WO2017204317A1 (ja) * | 2016-05-27 | 2017-11-30 | 合同酒精株式会社 | 耐熱性イソアミラーゼ |
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US6265197B1 (en) | 1998-07-02 | 2001-07-24 | Novozymes A/S Krogshoejvej | Starch debranching enzymes |
WO2000058445A1 (en) * | 1999-03-29 | 2000-10-05 | Novozymes A/S | Polypeptides having branching enzyme activity and nucleic acids encoding same |
US20030134396A1 (en) * | 2001-12-19 | 2003-07-17 | Shetty Jayarama K. | Process for hydrolyzing starch without pH adjustment |
CN101193623A (zh) * | 2003-05-15 | 2008-06-04 | 柏尔迈瑞克斯公司 | 可植入的网状弹性基质的制造和应用 |
BRPI0416762A (pt) | 2003-11-21 | 2007-02-27 | Genencor Int | expressão de enzimas hidrolisantes de amido granular em trinchoderma e processo para produzir glicose a partir de substratos de amido granular |
US7763077B2 (en) | 2003-12-24 | 2010-07-27 | Biomerix Corporation | Repair of spinal annular defects and annulo-nucleoplasty regeneration |
JP2008517599A (ja) * | 2004-10-22 | 2008-05-29 | カーギル インコーポレイテッド | マルトデキストリンの作製のための工程およびマルトデキストリン |
EP2461702B1 (en) * | 2009-08-07 | 2018-11-21 | Danisco US Inc. | Alpha-amylase blend for starch processing and method of use thereof |
WO2011020910A1 (en) | 2009-08-21 | 2011-02-24 | Novozymes A/S | Polypeptides having isoamylase activity and polynucleotides encoding same |
US20110091938A1 (en) * | 2009-10-20 | 2011-04-21 | Grain Processing Corporation | Starch Hydrolysis |
EP2785746B1 (en) | 2012-08-09 | 2016-10-12 | Cargill, Incorporated | Process for starch liquefaction |
CR20160572A (es) | 2014-05-12 | 2017-04-24 | Valent Biosciences Corp | Métodos para incrementar el rendimientio del aceite de palma |
EP3835426B1 (en) * | 2019-12-13 | 2022-06-29 | Weissbiotech GmbH | Process for the preparation of a fermentable sugar composition and the fermentation thereof |
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US3730840A (en) * | 1968-04-01 | 1973-05-01 | Hayashibara Co | Process for preparing low molecular weight amyloses |
US3881991A (en) * | 1969-01-24 | 1975-05-06 | Hayashibara Co | Process for producing amylose powders having a mean degree of polymerization between 20{14 30 |
BE758661A (fr) * | 1969-11-09 | 1971-05-10 | Hayashibara Co | Compositions d'amyloses pour la production de pellicules |
AU630308B2 (en) * | 1990-11-19 | 1992-10-22 | National Starch And Chemical Investment Holding Corporation | Short chain amylose as a replacement for fats in foods |
EP0529893A1 (en) * | 1991-08-16 | 1993-03-03 | A.E. Staley Manufacturing Company | Debranched amylopectin-starch as fat replacer |
JP3173849B2 (ja) * | 1992-02-26 | 2001-06-04 | 天野エンザイム株式会社 | 新規な枝切り酵素及びその製造法 |
US5750876A (en) * | 1994-07-28 | 1998-05-12 | Monsanto Company | Isoamylase gene, compositions containing it, and methods of using isoamylases |
NL9500292A (nl) * | 1995-02-16 | 1996-10-01 | Stichting Nl Instituut Voor Ko | Werkwijze voor omzetting van een zetmeelmateriaal, en daarvoor bruikbaar enzympreparaat. |
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1998
- 1998-07-02 EP EP98930661A patent/EP1002062B1/en not_active Expired - Lifetime
- 1998-07-02 AU AU81026/98A patent/AU8102698A/en not_active Abandoned
- 1998-07-02 JP JP50617399A patent/JP4087463B2/ja not_active Expired - Fee Related
- 1998-07-02 DE DE69834403T patent/DE69834403T2/de not_active Expired - Lifetime
- 1998-07-02 ES ES98930661T patent/ES2263209T3/es not_active Expired - Lifetime
- 1998-07-02 WO PCT/DK1998/000304 patent/WO1999001545A1/en active IP Right Grant
- 1998-07-02 DK DK98930661T patent/DK1002062T3/da active
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WO2017204317A1 (ja) * | 2016-05-27 | 2017-11-30 | 合同酒精株式会社 | 耐熱性イソアミラーゼ |
US11136569B2 (en) | 2016-05-27 | 2021-10-05 | Godo Shusei Co., Ltd. | Heat resistant isoamylase |
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EP1002062B1 (en) | 2006-05-03 |
EP1002062A1 (en) | 2000-05-24 |
US6087149A (en) | 2000-07-11 |
ATE325188T1 (de) | 2006-06-15 |
DE69834403D1 (de) | 2006-06-08 |
US6448049B1 (en) | 2002-09-10 |
AU8102698A (en) | 1999-01-25 |
DK1002062T3 (da) | 2006-09-11 |
WO1999001545A1 (en) | 1999-01-14 |
ES2263209T3 (es) | 2006-12-01 |
DE69834403T2 (de) | 2007-04-19 |
JP4087463B2 (ja) | 2008-05-21 |
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