ArticleMolecules (Basel, Switzerland)2019
Immobilization of Naringinase from
Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.
- Use of Naringinase to Modify the Sensory Quality of Foods and Increase the Bioavailability of Flavonoids: A Systematic Review.Molecules (Basel, Switzerland) · 2025Pooled it
- A Hyperthermostable Archaeal GH78 Rhamnosidase Efficiently Hydrolyzes Flavonoid Glycosides for Juice Debittering.Journal of agricultural and food chemistry · 2026Article
- Anti-inflammatory effects of naringinase treated ethanol extracts ofFood science and biotechnology · 2025Article
- A novel chitosan microsphere as food processing enzyme immobilization carrier and its application in nucleotide production.Food chemistry: X · 2025Article
- Immobilization of Naringinase onto Polydopamine-Coated Magnetic Iron Oxide Nanoparticles for Juice Debittering Applications.Polymers · 2024Article
- Recent Advances and Perspectives on Food-Grade Immobilisation Systems for Enzymes.Foods (Basel, Switzerland) · 2024Review
- Green nanobiocatalysts: enhancing enzyme immobilization for industrial and biomedical applications.PeerJ · 2024Review
- Enhancement of debitterness, water-solubility, and neuroprotective effects of naringin by transglucosylation.Applied microbiology and biotechnology · 2023Article
- α-L-rhamnosidase: production, properties, and applications.World journal of microbiology & biotechnology · 2023Review
- Grapefruit Debittering by Simultaneous Naringin Hydrolysis and Limonin Adsorption Using Naringinase Immobilized in Agarose Supports.Molecules (Basel, Switzerland) · 2022Article
- Novel Strategy of Mussel-Inspired Immobilization of Naringinase with High Activity Using a Polyethylenimine/Dopamine Co-deposition Method.ACS omega · 2021Article
- Chitosan-Grafted Halloysite Nanotubes-FePolymers · 2020Article
- Immobilization of Naringinase fromMolecules (Basel, Switzerland) · 2020Article
- Editorial for Special Issue: Enzyme Immobilization and Its Applications.Molecules (Basel, Switzerland) · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Naringinase is an enzyme complex which exhibits α-l-rhamnosidase and β-d-glucosidase activity. This enzymatic complex catalyzes the hydrolysis of naringin (4',5,7-trihydroxy flavanone 7-rhamnoglucoside), the main bittering component in grapefruit. Reduction of the level of this substance during the processing of juice has been the focus of many studies. The aim of the study was the immobilization of naringinase on chitosan microspheres activated with glutaraldehyde and, finally, the use of such immobilized enzyme for debittering grapefruit juice. The effect of naringinase concentration and characterization of the immobilized enzyme compared to the soluble enzyme were investigated. The maximum activity was observed at optimum pH 4.0 for both free and immobilized naringinase. However, the optimum temperature was shifted from 70 to 40 °C upon immobilization. The K
Indexed as
Identifiers
What OpenQuestion holds
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.