ArticleApplied biochemistry and biotechnology2022
Homologous Expression and Characterization of α-L-rhamnosidase from Aspergillus niger for the Transformation of Flavonoids.
Article in Applied biochemistry and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 13 citations in OpenAlex.
- Screening of mutants, enzymatic properties, and scale-up fermentation for catalysis of naringin using recombinantFrontiers in microbiology · 2026Article
- An Organic Solvent-Tolerant α-L-Rhamnosidase fromMolecules (Basel, Switzerland) · 2025Article
- Homologous expression of Aspergillus niger α-L-rhamnosidase and its application in enzymatic debittering of Ougan juice.Biotechnology letters · 2024Article
- α-L-rhamnosidase: production, properties, and applications.World journal of microbiology & biotechnology · 2023Review
- Effects of several flavonoids on human gut microbiota and its metabolism byFrontiers in microbiology · 2023Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Aspergillus niger has been used for homologous and heterologous expressions of many protein products. In this study, the α-L-rhamnosidase from A. niger (Rha-N1, GenBank XP_001389086.1) was homologously expressed in A. niger 3.350 by Agrobacterium tumefaciens-mediated transformation. The enzyme activity of Rha-N1 was 0.658 U/mL, which was obtained by cultivation of engineered A. niger in a 5-L bioreactor. Rha-N1 was purified by affinity chromatography and characterized. The optimum temperature and optimum pH for Rha-N1 were 60 °C and 4.5, respectively. Enzyme activity was promoted by Al
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