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Literature DB >> 19763902

alpha-Amylase: an ideal representative of thermostable enzymes.

Abstract

The conditions prevailing in the industrial applications in which enzymes are used are rather extreme, especially with respect to temperature and pH. Therefore, there is a continuing demand to improve the stability of enzymes and to meet the requirements set by specific applications. In this respect, thermostable enzymes have been proposed to be industrially relevant. In this review, alpha-amylase, a well-established representative of thermostable enzymes, providing an attractive model for the investigation of the structural basis of thermostability of proteins, has been discussed.

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Year: 2009 PMID： 19763902 DOI： 10.1007/s12010-009-8735-4

Source DB: PubMed Journal: Appl Biochem Biotechnol ISSN： 0273-2289 Impact factor: 2.926

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Cited

24 in total

1. Distinct characteristics of single starch-binding domain SBD1 derived from tandem domains SBD1-SBD2 of halophilic Kocuria varians alpha-amylase.

Authors: Rui Yamaguchi; Tsutomu Arakawa; Hiroko Tokunaga; Matsujiro Ishibashi; Masao Tokunaga
Journal: Protein J Date: 2012-03 Impact factor: 2.371

2. Templating α-amylase peptide inhibitors with organotin compounds.

Authors: Fernando Porcelli; Cristina Olivieri; Larry R Masterson; Yi Wang; Gianluigi Veglia
Journal: J Biol Inorg Chem Date: 2011-07-07 Impact factor: 3.358

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. New insight in the structural features of haloadaptation in α-amylases from halophilic Archaea following homology modeling strategy: folded and stable conformation maintained through low hydrophobicity and highly negative charged surface.

Authors: Mohamed Amine Zorgani; Kevin Patron; Mickaël Desvaux
Journal: J Comput Aided Mol Des Date: 2014-05-28 Impact factor: 3.686

5. Structural investigation of the thermostability and product specificity of amylosucrase from the bacterium Deinococcus geothermalis.

Authors: Frédéric Guérin; Sophie Barbe; Sandra Pizzut-Serin; Gabrielle Potocki-Véronèse; David Guieysse; Valérie Guillet; Pierre Monsan; Lionel Mourey; Magali Remaud-Siméon; Isabelle André; Samuel Tranier
Journal: J Biol Chem Date: 2011-12-29 Impact factor: 5.157

6. Sorbitol counteracts temperature- and chemical-induced denaturation of a recombinant α-amylase from alkaliphilic Bacillus sp. TS-23.

Authors: Meng-Chun Chi; Tai-Jung Wu; Hsing-Ling Chen; Huei-Fen Lo; Long-Liu Lin
Journal: J Ind Microbiol Biotechnol Date: 2012-08-12 Impact factor: 3.346

alpha-Amylase: an ideal representative of thermostable enzymes.

1. Distinct characteristics of single starch-binding domain SBD1 derived from tandem domains SBD1-SBD2 of halophilic Kocuria varians alpha-amylase.

2. Templating α-amylase peptide inhibitors with organotin compounds.

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

4. New insight in the structural features of haloadaptation in α-amylases from halophilic Archaea following homology modeling strategy: folded and stable conformation maintained through low hydrophobicity and highly negative charged surface.

5. Structural investigation of the thermostability and product specificity of amylosucrase from the bacterium Deinococcus geothermalis.

6. Sorbitol counteracts temperature- and chemical-induced denaturation of a recombinant α-amylase from alkaliphilic Bacillus sp. TS-23.

7. Recombinant expression, purification, and characterization of an α-amylase from Massilia timonae.

8. Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis.

9. Structural position correlation analysis (SPCA) for protein family.

Review 10. Marine extremophiles: a source of hydrolases for biotechnological applications.