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

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411—Amylases
    • C12N9/2428—Glucan 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 (en) 1996-07-24 1997-07-24 PROTEIN ENGINEERING OF GLUCOAMYLASE TO INCREASE pH OPTIMUM, SUBSTRATE SPECIFICITY AND THERMOSTABILITY

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 (zh)
JP (1) JP2000515377A (zh)
CN (1) CN1238009A (zh)
AU (1) AU3892397A (zh)
CA (1) CA2259958A1 (zh)
WO (1) WO1998003639A1 (zh)

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
KR20010032497A (ko) * 1997-11-26 2001-04-25 에이.이. 스테일리 매니팩츄어링 컴파니 막 분리 단계를 포함하는 효소성 전분 당화
US6352851B1 (en) 1998-07-15 2002-03-05 Novozymes A/S Glucoamylase variants
EP1914306A3 (en) * 1998-07-15 2008-09-10 Novozymes A/S Glucoamylase Variants
EP1097196B2 (en) * 1998-07-15 2011-04-20 Novozymes A/S Glucoamylase variants
WO2000075296A1 (en) * 1999-06-02 2000-12-14 Novozymes A/S Novel glucoamylase
CA2374009A1 (en) 1999-07-09 2001-01-18 Novozymes A/S Glucoamylase variant
WO2003029449A2 (en) 2001-10-01 2003-04-10 Novozymes A/S Glucoamylase variants
AR077942A1 (es) * 2009-08-19 2011-10-05 Danisco Variantes de glucoamilasa
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
CN105960176A (zh) 2014-02-07 2016-09-21 诺维信公司 用于生产葡萄糖糖浆的组合物
WO2020239064A1 (zh) * 2019-05-31 2020-12-03 南京百斯杰生物工程有限公司 一种热稳定性葡萄糖氧化酶
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 (en) 2022-05-14 2023-11-23 Novozymes A/S Compositions and methods for preventing, treating, supressing and/or eliminating phytopathogenic infestations and infections

Also Published As

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

Similar Documents

Publication Publication Date Title
Tews et al. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay–Sachs disease
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
US5763385A (en) Modified α-amylases having altered calcium binding properties
AU3892397A (en) Protein engineering of glucoamylase to increase ph optimum, substrate specificity and thermostability
US20060134266A1 (en) Enzyme
EP0536270A1 (en) Enzymatic hydrolysis of starch to glucose, using a genetically engineered enzyme
Li et al. Effect on thermostability and catalytic activity of introducing disulfide bonds into Aspergillus awamori glucoamylase.
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
Chen et al. Identification and elimination by site-directed mutagenesis of thermolabile aspartyl bonds in Aspergillus awamori glucoamylase
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
Nielsen et al. Cloning, heterologous expression, and enzymatic characterization of a thermostable glucoamylase from Talaromyces emersonii
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
Flory et al. Thermosensitive mutants of Aspergillus awamori glucoamylase by random mutagenesis: inactivation kinetics and structural interpretation
WO1998045417A1 (en) HYPERTHERMOSTABLE α-AMYLASE
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