Literature DB >> 10449318

Protein engineering of alpha-amylase for low pH performance.

A Shaw1, R Bott, A G Day.   

Abstract

Industrial-scale starch liquefaction is currently constrained to operating at pH 6.0 and above, as the enzyme used in the process, Bacillus licheniformis alpha-amylase, is unstable at lower pH under the conditions used. There is a need to develop an enzyme that can operate at lower pH. Recent progress has been made in engineering the B. licheniformis enzyme for improved industrial performance. The availability of crystal structures and subsequent analysis of improved variants, in a structural context, is revealing common factors and a rationale to make further improvements.

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Year:  1999        PMID: 10449318     DOI: 10.1016/S0958-1669(99)80063-9

Source DB:  PubMed          Journal:  Curr Opin Biotechnol        ISSN: 0958-1669            Impact factor:   9.740


  12 in total

1.  Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability.

Authors:  Mats Sandgren; Peter J Gualfetti; Andrew Shaw; Laurie S Gross; Mae Saldajeno; Anthony G Day; T Alwyn Jones; Colin Mitchinson
Journal:  Protein Sci       Date:  2003-04       Impact factor: 6.725

2.  Redesigning protein pKa values.

Authors:  Barbara Mary Tynan-Connolly; Jens Erik Nielsen
Journal:  Protein Sci       Date:  2006-12-22       Impact factor: 6.725

3.  Purification and biochemical characterization of an acidophilic amylase from a newly isolated Bacillus sp. DR90.

Authors:  Ahmad Asoodeh; Ashraf Alemi; Akbar Heydari; Jafar Akbari
Journal:  Extremophiles       Date:  2013-02-21       Impact factor: 2.395

4.  Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca²⁺ inhibition and Co²⁺ independent.

Authors:  Hajer Ben Hlima; Nushin Aghajari; Mamdouh Ben Ali; Richard Haser; Samir Bejar
Journal:  J Ind Microbiol Biotechnol       Date:  2011-12-04       Impact factor: 3.346

5.  Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum.

Authors:  Sang-Jae Lee; Dong-Woo Lee; Eun-Ah Choe; Young-Ho Hong; Seong-Bo Kim; Byoung-Chan Kim; Yu-Ryang Pyun
Journal:  Appl Environ Microbiol       Date:  2005-12       Impact factor: 4.792

6.  Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus α-amylase at 1.9 Å resolution.

Authors:  Wendy A Offen; Anders Viksoe-Nielsen; Torben V Borchert; Keith S Wilson; Gideon J Davies
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2015-01-01       Impact factor: 1.056

7.  One-step production of immobilized alpha-amylase in recombinant Escherichia coli.

Authors:  Indira A Rasiah; Bernd H A Rehm
Journal:  Appl Environ Microbiol       Date:  2009-02-05       Impact factor: 4.792

8.  Directed evolution of a bacterial alpha-amylase: toward enhanced pH-performance and higher specific activity.

Authors:  Cornelius Bessler; Jutta Schmitt; Karl-Heinz Maurer; Rolf D Schmid
Journal:  Protein Sci       Date:  2003-10       Impact factor: 6.725

9.  Improving the reversibility of thermal denaturation and catalytic efficiency of Bacillus licheniformis α-amylase through stabilizing a long loop in domain B.

Authors:  Zhu Li; Xuguo Duan; Sheng Chen; Jing Wu
Journal:  PLoS One       Date:  2017-03-02       Impact factor: 3.240

Review 10.  Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications.

Authors:  Deepika Mehta; Tulasi Satyanarayana
Journal:  Front Microbiol       Date:  2016-07-28       Impact factor: 5.640

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