AU3892397A - Protein engineering of glucoamylase to increase ph optimum, substrate specificity and thermostability - Google Patents

Protein engineering of glucoamylase to increase ph optimum, substrate specificity and thermostability

Info

Publication number
AU3892397A
AU3892397A AU38923/97A AU3892397A AU3892397A AU 3892397 A AU3892397 A AU 3892397A AU 38923/97 A AU38923/97 A AU 38923/97A AU 3892397 A AU3892397 A AU 3892397A AU 3892397 A AU3892397 A AU 3892397A
Authority
AU
Australia
Prior art keywords
glucoamylase
mutations
mutation
increased
mutant
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.)
Abandoned
Application number
AU38923/97A
Other languages
English (en)
Inventor
Martin Allen
Hsiu-Mei Chen
Pedro Coutinho
Tsuei-Yun Fang
Clark Ford
Richard Honzatko
Yuxing Li
Hsuan-Liang Liu
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Iowa State University Research Foundation ISURF
Original Assignee
University of Iowa Research Foundation UIRF
Iowa State University Research Foundation ISURF
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by University of Iowa Research Foundation UIRF, Iowa State University Research Foundation ISURF filed Critical University of Iowa Research Foundation UIRF
Publication of AU3892397A publication Critical patent/AU3892397A/en
Abandoned legal-status Critical Current

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405Glucanases
    • C12N9/2408Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411Amylases
    • C12N9/2428Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Wood Science & Technology (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Biomedical Technology (AREA)
  • Molecular Biology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Enzymes And Modification Thereof (AREA)
AU38923/97A 1996-07-24 1997-07-24 Protein engineering of glucoamylase to increase ph optimum, substrate specificity and thermostability Abandoned AU3892397A (en)

Applications Claiming Priority (5)

Application Number Priority Date Filing Date Title
US2257896P 1996-07-24 1996-07-24
US60022578 1996-07-24
US2307796P 1996-08-02 1996-08-02
US60023077 1996-08-02
PCT/US1997/012983 WO1998003639A1 (fr) 1996-07-24 1997-07-24 Fabrication par genie genetique et a l'aide de proteines d'une glucoamylase permettant d'obtenir un ph optimal et d'accroitre la specificite d'un substrat ainsi que la stabilite thermique

Related Child Applications (1)

Application Number Title Priority Date Filing Date
AU35130/01A Division AU3513001A (en) 1996-07-24 2001-04-12 Protein engineering of glucoamylase to increase pH optimum, ubstrate specificity and thermostability

Publications (1)

Publication Number Publication Date
AU3892397A true AU3892397A (en) 1998-02-10

Family

ID=26696092

Family Applications (1)

Application Number Title Priority Date Filing Date
AU38923/97A Abandoned AU3892397A (en) 1996-07-24 1997-07-24 Protein engineering of glucoamylase to increase ph optimum, substrate specificity and thermostability

Country Status (6)

Country Link
EP (1) EP0970193A1 (fr)
JP (1) JP2000515377A (fr)
CN (1) CN1238009A (fr)
AU (1) AU3892397A (fr)
CA (1) CA2259958A1 (fr)
WO (1) WO1998003639A1 (fr)

Families Citing this family (15)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6537792B1 (en) * 1996-07-24 2003-03-25 Iowa State University Protein engineering of glucoamylase to increase pH optimum, substrate specificity and thermostability
US6129788A (en) 1997-11-26 2000-10-10 Novo Nordisk A/S Method of producing saccharide preparations
US6352851B1 (en) 1998-07-15 2002-03-05 Novozymes A/S Glucoamylase variants
EP1914306A3 (fr) * 1998-07-15 2008-09-10 Novozymes A/S Variantes de la glucoamylase
WO2000004136A1 (fr) * 1998-07-15 2000-01-27 Novozymes A/S Variants de glucoamylase
WO2000075296A1 (fr) * 1999-06-02 2000-12-14 Novozymes A/S Nouvelle glucoamylase
EP1200566A2 (fr) 1999-07-09 2002-05-02 Novozymes A/S Variante de glucoamylase
WO2003029449A2 (fr) * 2001-10-01 2003-04-10 Novozymes A/S Variants de glucoamylase
BR112012003787A2 (pt) * 2009-08-19 2017-07-04 Danisco variantes de glicoamilase
CN102994474B (zh) * 2012-12-31 2015-04-15 江南大学 一种热稳定性提高的淀粉酶突变体及其应用
CN103409392B (zh) * 2013-07-25 2015-06-03 江南大学 一种热稳定的淀粉酶突变体及其制备方法和应用
BR112016018075B1 (pt) 2014-02-07 2022-01-18 Novozymes A/S Composição compreendendo uma alfa-amilase, uma pululanase e uma enzima glicoamilase e método de fabricação de xarope de glicose a partir de amido liquefeito
US20220220454A1 (en) * 2019-05-31 2022-07-14 Nanjing Bestzyme Bio-Engineering Co., Ltd. Thermostable glucose oxidase
CN114381448B (zh) * 2022-01-10 2024-02-20 鑫缘茧丝绸集团股份有限公司 一种葡聚糖酶突变体及其应用
WO2023225459A2 (fr) 2022-05-14 2023-11-23 Novozymes A/S Compositions et procédés de prévention, de traitement, de suppression et/ou d'élimination d'infestations et d'infections phytopathogènes

Also Published As

Publication number Publication date
JP2000515377A (ja) 2000-11-21
CN1238009A (zh) 1999-12-08
CA2259958A1 (fr) 1998-01-29
WO1998003639A1 (fr) 1998-01-29
EP0970193A1 (fr) 2000-01-12

Similar Documents

Publication Publication Date Title
Demirkan et al. α-Amylase from B. amyloliquefaciens: purification, characterization, raw starch degradation and expression in E. coli
Dong et al. Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
Yamamoto et al. Steric hindrance by 2 amino acid residues determines the substrate specificity of isomaltase from Saccharomyces cerevisiae
Brown et al. Characterization of amylolytic enzymes, having both α-1, 4 and α-1, 6 hydrolytic activity, from the thermophilic archaea Pyrococcus furiosus and Thermococcus litoralis
US5763385A (en) Modified α-amylases having altered calcium binding properties
US5162210A (en) Process for enzymatic hydrolysis of starch to glucose
AU3892397A (en) Protein engineering of glucoamylase to increase ph optimum, substrate specificity and thermostability
US20060134266A1 (en) Enzyme
Li et al. Effect on thermostability and catalytic activity of introducing disulfide bonds into Aspergillus awamori glucoamylase.
JP2000197491A (ja) 枯草菌/大腸菌シャトルベクター
Allen et al. Stabilization of Aspergillus awamori glucoamylase by proline substitution and combining stabilizing mutations.
Shinohara et al. A novel thermostable branching enzyme from an extremely thermophilic bacterial species, Rhodothermus obamensis
Nagasaka et al. Purification and properties of the raw-starch-digesting glucoamylases from Corticium rolfsii
Malle et al. Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168
US6537792B1 (en) Protein engineering of glucoamylase to increase pH optimum, substrate specificity and thermostability
Juge et al. Isozyme hybrids within the protruding third loop domain of the barley α‐amylase (β/α) 8‐barrel implication for BASI sensitivity and substrate affinity
Totsuka et al. Residues essential for catalytic activity of soybean β‐amylase
Rodenburg et al. Specific inhibition of barley α‐amylase 2 by barley α‐amylase/subtilisin inhibitor depends on charge interactions and can be conferred to isozyme 1 by mutation
Nielsen et al. Cloning, heterologous expression, and enzymatic characterization of a thermostable glucoamylase from Talaromyces emersonii
Flory et al. Thermosensitive mutants of Aspergillus awamori glucoamylase by random mutagenesis: inactivation kinetics and structural interpretation
WO1998045417A1 (fr) ENZYME α-AMYLASE HYPERTHERMOSTABLE
Wang et al. Improvement of Aspergillus niger glucoamylase thermostability by directed evolution
AU3513001A (en) Protein engineering of glucoamylase to increase pH optimum, ubstrate specificity and thermostability
MXPA99000786A (en) Glucoamylase protein engineering to increase thermostability and substrate specificity with ph opt
KR100674133B1 (ko) 폴리펩티드

Legal Events

Date Code Title Description
MK5 Application lapsed section 142(2)(e) - patent request and compl. specification not accepted