Article3 Biotech2019
A spectrophotometric method for high-throughput screening of α-l-rhamnosidase activity on rutin coupled with a β-d-glucosidase assay.
Article in 3 Biotech, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- A Metabolism-Guided Framework for Selecting Structural Modification or Nano-Delivery Strategies for Oral Rutin.International journal of molecular sciences · 2026Review
- Substrate Selectivities of GH78 α-L-Rhamnosidases from Human Gut Bacteria on Dietary Flavonoid Glycosides.Molecules (Basel, Switzerland) · 2025Article
- Rutin of Moringa oleifera as a potential inhibitor to Agaricus bisporus tyrosinase as revealed from the molecular dynamics of inhibition.Scientific reports · 2024Article
- Quercetin Derivatives as Potential Therapeutic Agents: An Updated Perspective on the Treatment of Nicotine-Induced Non-Small Cell Lung Cancer.International journal of molecular sciences · 2023Review
- Insights into glycosidic bond specificity of an engineered selective α-L-rhamnosidase N12-Rha via activity assays and molecular modelling.AMB Express · 2022Article
- Computer-Aided Design of α-L-Rhamnosidase to Increase the Synthesis Efficiency of Icariside I.Frontiers in bioengineering and biotechnology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-l-Rhamnosidase may biotransform rutin into isoquercetin with better bioavailability and bioactivity. To date, the high-throughput screening for the activity of α-l-rhamnosidases on rutin could not be achieved. Herein, based on the spectral differences between rutin and its aglycone quercetin in alkaline pH 10.0, we have developed a novel and simple spectrophotometric method for high-throughput screening of α-l-rhamnosidase activity on rutin by combining with a highly active β-d-glucosidase. Quercetin showed the maximum absorbance at 320 nm in alkaline pH 10.0, and could be considered as the characteristic peak of quercetin because rutin had low absorption at 320 nm. Meanwhile, rutin exhibited the maximum absorption at 400 nm and quercetin showed low absorption at 400 nm in pH 10.0. With this novel spectrophotometric method, the relative abilities of nine different α-l-rhamnosidases on rutin had been evaluated by monitoring the absorption values of the reaction mixture in alkaline pH 10.0 at 320 nm and 400 nm, and the trend in the activity on rutin was consistent with that obtained by HPLC. Moreover, the library from site-directed saturation mutagenesis at the residue Val338 in the α-l-rhamnosidase BtRha78A from
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