ArticleApplied and environmental microbiology2000
Comparative characterization of complete and truncated forms of Lactobacillus amylovorus alpha-amylase and role of the C-terminal direct repeats in raw-starch binding.
Article in Applied and environmental microbiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 86 citations in OpenAlex.
- Production and application of α-amylase, native AmyJ33-ABC, from Bacillus siamensis JJC33M in gelatinized potato starch and its industrial potential.Biotechnology letters · 2025Article
- Long-read, multi-amplicon sequencing to explore genetic diversity associated with starch degrading phenotypes in amylolyticFrontiers in microbiology · 2025Article
- Identification of acacia gum fermenting bacteria from pooled human feces using anaerobic enrichment culture.Frontiers in microbiology · 2023Article
- Exploiting the Native Microorganisms from Different Food Matrices to Formulate Starter Cultures for Sourdough Bread Production.Microorganisms · 2022Review
- AmyJ33, a truncated amylase with improved catalytic properties.Biotechnology letters · 2022Article
- Characterization of a novel type of glycogen-degrading amylopullulanase from Lactobacillus crispatus.Applied microbiology and biotechnology · 2022Article
- Functional study of C-terminal domain of the thermoacidophilic raw starch-hydrolyzing α-amylase Gt-amy.Food science and biotechnology · 2020Article
- Article
- Aspergillus Oryzae S2 α-Amylase Domain C Involvement in Activity and Specificity: In Vivo Proteolysis, Molecular and Docking Studies.PloS one · 2016Article
- α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Cellular and molecular life sciences : CMLS · 2014Review
- Close relationship of a novel Flavobacteriaceae α-amylase with archaeal α-amylases and good potentials for industrial applications.Biotechnology for biofuels · 2014Article
- A single residue mutation abolishes attachment of the CBM26 starch-binding domain from Lactobacillus amylovorus alpha-amylase.Journal of industrial microbiology & biotechnology · 2009Article
- Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domains.Applied and environmental microbiology · 2007Article
- Starch-binding domain affects catalysis in two Lactobacillus alpha-amylases.Applied and environmental microbiology · 2005Article
- Direct production of ethanol from raw corn starch via fermentation by use of a novel surface-engineered yeast strain codisplaying glucoamylase and alpha-amylase.Applied and environmental microbiology · 2004Article
- Improving the thermostability of raw-starch-digesting amylase from a Cytophaga sp. by site-directed mutagenesis.Applied and environmental microbiology · 2003Article
- Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two constructs derived from the alpha-amylase gene (amyA) of Lactobacillus amylovorus were expressed in Lactobacillus plantarum, and their expression products were purified, characterized, and compared. These products correspond to the complete (AmyA) and truncated (AmyADelta) forms of alpha-amylase; AmyADelta lacks the 66-kDa carboxyl-terminal direct-repeating-unit region. AmyA and AmyADelta exhibit similar amylase activities towards a range of soluble substrates (amylose, amylopectin and alpha-cyclodextrin, and soluble starch). The specific activities of the enzymes towards soluble starch are similar, but the K(M) and V(max) values of AmyADelta were slightly higher than those of AmyA, whereas the thermal stability of AmyADelta was lower than that of AmyA. In contrast to AmyA, AmyADelta is unable to bind to beta-cyclodextrin and is only weakly active towards glycogen. More striking is the fact that AmyADelta cannot bind or hydrolyze raw starch, demonstrating that the carboxyl-terminal repeating-unit domain of AmyA is required for raw-starch binding activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.