ArticleApplied biochemistry and biotechnology2024
Heterologous Expression and Characterization of a Novel Mesophilic Maltogenic α-Amylase AmyFlA from Flavobacterium sp. NAU1659.
Article in Applied biochemistry and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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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Who cites it
2 citing papers in PubMed, 1 citations in OpenAlex.
- Partial purification and characterization of an extracellular cold-active protease from Flavobacterium azizsancarii, a novel Antarctic isolate.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Functions ofJournal of fungi (Basel, Switzerland) · 2025Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
A novel amylase AmyFlA from Flavobacterium sp. NAU1659, AmyFlA, was cloned and expressed in Esherichia coli. Based on phylogenetic and functional analysis, it was identified as a novel member of the subfamily GH13_46, sharing high sequence identity. The protein was predicted to consist of 620 amino acids, with a putative signal peptide of 25 amino acids. The enzyme was able to hydrolyze soluble starch with a specific activity of 352.97 U/mg at 50 °C in 50 mM phosphate buffer (pH 6.0). The K
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