Method for preparing maltogenic alpha-amylase variants

Data processing: measuring – calibrating – or testing – Measurement system in a specific environment – Chemical analysis

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S069100, C435S183000, C435S202000, C530S350000, C536S023200, C702S019000

Reexamination Certificate

active

07908094

ABSTRACT:
The inventors have modified the amino acid sequence of a maltogenic alpha-amylase to obtain variants with improved properties, based on the three-dimensional structure of the maltogenic alpha-amylase Novamyl. The variants have altered physicochemical properties, e.g. an altered pH optimum, improved thermostability, increased specific activity, an altered cleavage pattern or an increased ability to reduce retrogradation of starch or staling of bread.

REFERENCES:
patent: 2320813 (1999-09-01), None
patent: 120693 (1989-05-01), None
patent: WO 89/03421 (1989-04-01), None
patent: WO 96/23874 (1996-08-01), None
patent: WO 96/33267 (1996-10-01), None
patent: WO 97/41213 (1997-11-01), None
patent: WO 97/41736 (1997-11-01), None
patent: WO 97/43424 (1997-11-01), None
patent: WO 99/43794 (1999-09-01), None
Chica et al. Curr Opin Biotechnol. Aug. 2005;16(4):378-84.
Sen et al. Appl Biochem Biotechnol. Dec. 2007;143(3):212-23.
Diderichsen B. et al, Cloning of a Maltogenic Alpha-Amylase FromBacillus stearothermophillus, FEMS Microbiology Letters, vol. 56, pp. 53-60 (1988).
Boel et al, Calcium Binding in Alpha Amylases an X-ray Diffraction Study At 2.1-Aresolution of Two Enzymes FromAspergillus, Biochemistry, vol. 29, No. 26, pp. 6244-6249 (1990).
Machius M et al, Crystal Structure of Calsium-DepletedBacillus, Journal of Molecular Biology, vol. 246, No. 4, pp. 545-559 (1995).
Changsoo Chang et al, Crystallization and Preliminary X-ray Crystallographic Analysis of Alpha-Amylase FromBacillus subtilis, J. Mol. Biol., vol. 229, pp. 235-238 (1993).
Svensson Birte, Protein Engineering in the Alpha-Amylase Family: Catalytic Mechanism Substrate Specificity and Stability, Plant Molecular Biology, vol. 25, pp. 141-157 (1994).
Knegtel Ronald M.A. et al, Crystal Structure At 2.3 Å Resolution and Revised Nucleotide Sequence of the Thermostable Cyclodextrin Glycosyltransferase From Thermoanaerobacterium Thermossulfurigenes EM1, Journal of Molecular Biology, vol. 256, pp. 611-622(1996).
Christophersen et al, Enzymatic Characterisation of Novamyl A Thermostable Alfa-Amylase, Starch/Starke, vol. 50, No. 1, pp. 39-45 (1998).
Kubota et al, Molecular Structure of B.stearothermophillusCyclodextrin Glucanotransferase and Analysis of Substrate Binding Site, Denpun Kagaku, vol. 38, No. 2, pp. 141-146 (1991).
Tachibana et al, Cloning and Expression of the 4-Alfa-Glucanotransferase Gene From the Hyperthermophillic ArchaeonPyrococcusSP. KOD1, and Characterization of the Enzyme, Journal of Fermentation and Bioengineering, vol. 83, No. 6, pp. 540-548 (1997).
Henrissat Bernard, A Classifaction of Glycosyl Hydrolases Based on Amino Acid Sequence Similarities, Biochemical Journal, vol. 280, pp. 309-316 (1991).
Strokopytov et al, X-ray Structure of Cyclodextrin, Biochemistry, vol. 34, pp. 2234-2240 (1995).
Klein et al, Structure of Cyclodextrin Glycosyl Transferase Refined At 2:0 Å Resolution, Journal of Molecular Biology, vol. 217, pp. 737-750 (1991).
Lawson et al, Nucleotide Sequence and X-ray Structure of Cyclodextrin Glycosyltransferase FromBacillus circulansStrain 251 In a Maltose-Dependent Cyrstal Aform, Journal of Molecular Biology, vol. 236, pp. 590-600 (1994).
Hofmann et al, Three—Dimensional Structure Off Cyclodextrin Glycoisyltransferase FromBacillus circuanjsAt 3:4 Å Resolution, Journal of Molecular Biology, vol. 209, pp. 793-800 (1989).
Norman et al, Thermoanaerobacter SP. CGTASE: Its Properties and Application, vol. 39, No. 2, pp. 101-108 (1992).
Kim, Y.H. et al, Biochemistry and Molecular Biology, vol. 41, No. 2, pp. 227-234 (1997).
Sin et al, Journal of Biotechnology, vol. 32, No. 3, pp. 283-288 (1994).
Penninga D., Biochemistry, vol. 34, No. 10, pp. 3368-3376 (1995).
Dauter et al, X-ray Structure of Novamyl, The Five-Domain Maltogenic Alpha-Amylase FromBacillus stearothermophillusMaltose and Acarbose Complexes At 1.7 Å Resolution, Biochemistry, vol. 38, pp. 8385-8392 (1999).
Holm et al, Random Mutagenesis Used to Probe the Structure, Protein Engineering, vol. 3, No. 3 pp. 181-191 (1990).
Janecek. et al, Alpha-Amylase and Approaches Leading to Their Enhanced Stability, Febs Letters, vol. 304, No. 1, pp. 1-3 (1992).
Wind et al, Engineering of Factors Determining Alfa-Amylase and Cyclodextringlycosyltransferase Specificity in the Cyclodextrin Glycosyl, European Journal of Biochemistry, vol. 253, No. 3, pp. 598-605 (1998).
Bipin K. Dalmia et al, Domain E ofBacillus maceransCyclodextrin Glucanotransferase: Anindependent Starch-Binding Domain, Biotechnology and Bioengineering, vol. 47, pp. 575-584 (1995).
Del-Rio, G. et al, DiD Cyclodextrin Glycosyltransferases Evolve From Alpha-Amylase?, Febs Letters, vol. 416, pp. 221-224 (1997).
Jespersen et al, Biochemical Journal, vol. 280, pp. 51-55 (1991).
Updating the Sequence-Based Classification of Glycosyl Hydrolases, Biochemical Journal, vol. 316, pp. 695-696 (1996).
Chica et al., Semi-Rational Approaches, Current Opinion in Biotechnology, vol. 16, No. 4, pp. 378-384 (2005).
Witkowski et al., Conversion of a B-Ketoacyl Synthase., Biochemistry, vol. 38, No. 36, pp. 11643-11650 (1999).
Sen et al., Developments in Directed Evolution for Improving Enzyme Functions, Appl. Biochem Biotechnol, vol. 143, No. 3, pp. 212-223 (2007).
Diderichsen, B. et al, Database UNIPROT:P19531, Sequence Listing (1991).
Seffernick et al., Melamine Deaminase and Atrazine Chlorohydrolase., Journal of Bacteriology, vol. 183, No. 8, pp. 2405-2410 (2001).
Jones et al, Journal Biotechnology, vol. 134, pp. 325-333 (2008).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Method for preparing maltogenic alpha-amylase variants does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Method for preparing maltogenic alpha-amylase variants, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Method for preparing maltogenic alpha-amylase variants will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2686448

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.