ArticleApplied and environmental microbiology2005
Starch-binding domain affects catalysis in two Lactobacillus alpha-amylases.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 50 citations in OpenAlex.
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- Exploiting the Native Microorganisms from Different Food Matrices to Formulate Starter Cultures for Sourdough Bread Production.Microorganisms · 2022Review
- Comparative analysis of genome-based CAZyme cassette in Antarctic Microbacterium sp. PAMC28756 with 31 other Microbacterium species.Genes & genomics · 2022Article
- Use of Hydrolyzed Chinese Gallnut Tannic Acid in Weaned Piglets as an Alternative to Zinc Oxide: Overview on the Gut Microbiota.Animals : an open access journal from MDPI · 2021Article
- Lactic Acid Fermentation of Cereals and Pseudocereals: Ancient Nutritional Biotechnologies with Modern Applications.Nutrients · 2020Review
- Complete genome sequence of3 Biotech · 2020Article
- Bioaugmentation byFrontiers in microbiology · 2020Article
- Effects of starch concentration on calcium-enhanced black bullhead catfish protein gels.Food science & nutrition · 2017Article
- The targeting of starch binding domains from starch synthase III to the cell wall alters cell wall composition and properties.Plant molecular biology · 2017Article
- A chimeric α-amylase engineered from Bacillus acidicola and Geobacillus thermoleovorans with improved thermostability and catalytic efficiency.Journal of industrial microbiology & biotechnology · 2016Article
- α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Cellular and molecular life sciences : CMLS · 2014Review
- The carbohydrate-binding module of Fragaria × ananassa expansin 2 (CBM-FaExp2) binds to cell wall polysaccharides and decreases cell wall enzyme activities "in vitro".Journal of plant research · 2013Article
- Metabolism of oligosaccharides and starch in lactobacilli: a review.Frontiers in microbiology · 2012Article
- Enzymatic degradation of granular potato starch by Microbacterium aurum strain B8.A.Applied microbiology and biotechnology · 2012Article
- Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domains.Applied and environmental microbiology · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new starch-binding domain (SBD) was recently described in alpha-amylases from three lactobacilli (Lactobacillus amylovorus, Lactobacillus plantarum, and Lactobacillus manihotivorans). Usually, the SBD is formed by 100 amino acids, but the SBD sequences of the mentioned lactobacillus alpha-amylases consist of almost 500 amino acids that are organized in tandem repeats. The three lactobacillus amylase genes share more than 98% sequence identity. In spite of this identity, the SBD structures seem to be quite different. To investigate whether the observed differences in the SBDs have an effect on the hydrolytic capability of the enzymes, a kinetic study of L. amylovorus and L. plantarum amylases was developed, with both enzymes acting on several starch sources in granular and gelatinized forms. Results showed that the amylolytic capacities of these enzymes are quite different; the L. amylovorus alpha-amylase is, on average, 10 times more efficient than the L. plantarum enzyme in hydrolyzing all the tested polymeric starches, with only a minor difference in the adsorption capacities.
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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.