ArticleApplied and environmental microbiology2003
Improving the thermostability of raw-starch-digesting amylase from a Cytophaga sp. by site-directed mutagenesis.
Article in Applied and environmental microbiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 27 citations in OpenAlex.
- Molecular dynamics study to improve the substrate adsorption ofAdvances and applications in bioinformatics and chemistry : AABC · 2019Article
- Computational Model of the Effect of a Surface-Binding Site on theBioinformatics and biology insights · 2017Article
- The Importance of Surface-Binding Site towards Starch-Adsorptivity Level inEnzyme research · 2017Review
- Close relationship of a novel Flavobacteriaceae α-amylase with archaeal α-amylases and good potentials for industrial applications.Biotechnology for biofuels · 2014Article
- Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel.World journal of microbiology & biotechnology · 2012Article
- SORS: a universal one-round PCR-based method for site-directed mutagenesis.Molecular biotechnology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A heat-stable raw-starch-digesting amylase (RSDA) was generated through PCR-based site-directed mutagenesis. At 65 degrees C, the half-life of this mutant RSDA, which, compared with the wild-type RSDA, lacks amino acids R178 and G179, was increased 20-fold. While the wild type was inactivated completely at pH 3.0, the mutant RSDA still retained 41% of its enzymatic activity. The enhancement of RSDA thermostability was demonstrated to be via a Ca(2+)-independent mechanism.
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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.