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Purification and Characterization of a Naringinase fromAspergillus aculeatusJMUdb058
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
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Characterization of an α-l-rhamnosidase from Aspergillus kawachii and its gene
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Naringinases: occurrence, characteristics, and applications
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Updates on naringinase: structural and biotechnological aspects
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Purification and characterization of naringinase from a newly isolated strain of Aspergillus niger 1344 for the transformation of flavonoids
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Molecular identification of Staphylococcus xylosus MAK2, a new α-l-rhamnosidase producer
inferredcites →https://doi.org/10.1007/s11274-011-0766-7openalex-snapshot
Identification and characterization of a new naringinase-producing strain, Williopsis californica Jmudeb007
inferredcites →https://doi.org/10.1016/0003-2697(83)90314-7openalex-snapshot
A rapid method for the determination of naringin, prunin, and naringenin applied to the assay of naringinase
inferredcites →https://doi.org/10.1016/0003-2697(85)90614-1openalex-snapshot
A method for assaying the rhamnosidase activity of naringinase
inferredcites →https://doi.org/10.1016/0008-6215(88)80012-0openalex-snapshot
Sequential enzymic hydrolysis of potentially aromatic glycosides from grape
inferredcites →https://doi.org/10.1016/0141-0229(94)90168-6openalex-snapshot
Kinetic and immobilization studies on fungal glycosidases for aroma enhancement in wine
inferredcites →https://doi.org/10.1016/0378-1119(96)00179-5openalex-snapshot
Cloning and sequencing of the cDNA encoding β-glucosidase 1 from Aspergillus aculeatus
inferredcites →https://doi.org/10.1016/j.foodchem.2007.01.033openalex-snapshot
Immobilization of naringinase from Aspergillus niger CECT 2088 in poly(vinyl alcohol) cryogels for the debittering of juices
inferredcites →https://doi.org/10.1016/j.foodchem.2010.06.024openalex-snapshot
Purification and characterisation of Aspergillus sojae naringinase: The production of prunin exhibiting markedly enhanced solubility with in vitro inhibition of HMG-CoA reductase
inferredcites →https://doi.org/10.1016/j.jmb.2007.09.003openalex-snapshot
Crystal Structure of Glycoside Hydrolase Family 78 α-L-Rhamnosidase from Bacillus sp. GL1
inferredcites →https://doi.org/10.1016/j.procbio.2010.02.004openalex-snapshot
An innovative sol–gel naringinase bioencapsulation process for glycosides hydrolysis
inferredcites →https://doi.org/10.1016/j.procbio.2010.05.025openalex-snapshot
α-l-Rhamnosidase: A review
inferredcites →https://doi.org/10.1016/s0378-1097(97)00487-4openalex-snapshot
Purification and characterization of an α-?-rhamnosidase from Aspergillus niger
inferredcites →https://doi.org/10.1016/s0734-9750(00)00034-3openalex-snapshot
Production, purification, and characterization of the debittering enzyme naringinase
inferredcites →https://doi.org/10.1021/ac60007a016openalex-snapshot
Determination of Flavanones in Citrus Fruits
inferredcites →https://doi.org/10.1021/jf000434dopenalex-snapshot
β-Glucosidases from Five Black Aspergillus Species: Study of Their Physico-Chemical and Biocatalytic Properties
inferredcites →https://doi.org/10.1023/a:1008962131271openalex-snapshot
Production and partial purification of naringinase by Penicillium decumbens PTCC 5248
inferredcites →https://doi.org/10.1023/b:bile.0000044870.99039.19openalex-snapshot
Fractionation of the naringinase complex from Aspergillus terreus by dye affinity chromatography
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1038/nature04300openalex-snapshot
Genome sequencing and analysis of Aspergillus oryzae
inferredcites →https://doi.org/10.1038/nbt.1498openalex-snapshot
Genome sequencing and analysis of the filamentous fungus Penicillium chrysogenum
inferredcites →https://doi.org/10.1038/nbt1282openalex-snapshot
Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88
inferredcites →https://doi.org/10.1093/nar/gkp751openalex-snapshot
The Aspergillus Genome Database, a curated comparative genomics resource for gene, protein and sequence information for the Aspergillus research community
inferredcites →https://doi.org/10.1111/j.1365-2621.2001.tb11317.xopenalex-snapshot
Purification and Characterization of an α‐L‐Rhamnosidase from Aspergillus terreus of Interest in Winemaking
inferredcites →https://doi.org/10.1111/j.1470-8744.1999.tb01163.xopenalex-snapshot
Purification and biochemical characteristics of β‐D‐glucosidase from a thermophilic fungus, Thermomyces lanuginosus–SSBP
inferredcites →https://doi.org/10.1111/j.1574-6968.1997.tb12785.xopenalex-snapshot
Purification and characterization of an α-l-rhamnosidase from Aspergillus niger
inferredcites →https://doi.org/10.1111/j.1750-3841.2011.02471.xopenalex-snapshot
Characterization and Preparation of Aspergillus niger Naringinase for Debittering Citrus Juice
inferredcites →https://doi.org/10.1128/aem.13.6.842-845.1965openalex-snapshot
Production of the Enzyme Naringinase by Aspergillus niger
inferredcites →https://doi.org/10.1128/aem.67.5.2230-2234.2001openalex-snapshot
Purification and Characterization of Two Different α- l -Rhamnosidases, RhaA and RhaB, from Aspergillus aculeatus
inferredcites →https://doi.org/10.1271/bbb.62.1615openalex-snapshot
Expression of Aspergillus aculeatus No. F-50 Cellobiohydrolase I ( cbhI ) and β-glucosidase 1 ( bgl1 ) genes by Saccharomyces cerevisiae
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Convenient Immobilization of α‐L‐Rhamnosidase on Cerium‐based Metal‐Organic Frameworks Nanoparticles for Enhanced Enzymatic Activity and Recyclability
inferred← citeshttps://doi.org/10.1002/ffj.3239openalex-snapshot
Comparative analyses of aromas of fresh, naringinase‐treated and resin‐absorbed juices of pummelo by GC‐MS and sensory evaluation
inferred← citeshttps://doi.org/10.1002/jctb.6762openalex-snapshot
Facile preparation of immobilized naringinase on polyethylenimine/dopamine‐coated hydrothermal carbon spheres with high performance
inferred← citeshttps://doi.org/10.1007/s10068-015-0159-zopenalex-snapshot
Development and evaluation of simultaneous quantification of naringin, prunin, naringenin, and limonin in citrus juice
inferred← citeshttps://doi.org/10.1007/s11756-025-01888-6openalex-snapshot
Microbial naringinase: from microbial source to its current applications in various fields
inferred← citeshttps://doi.org/10.1007/s12010-017-2593-2openalex-snapshot
Purification and Characterization of a Naringinase from Cryptococcus albidus
inferred← citeshttps://doi.org/10.1007/s13399-023-04159-zopenalex-snapshot
Fermentation optimization of naringinase from a screened strain of Serratia marcescens C10 through response surface methodology
inferred← citeshttps://doi.org/10.1016/b978-0-444-63501-3.00007-7openalex-snapshot
Beta-Glucosidase From Penicillium
inferred← citeshttps://doi.org/10.1016/j.bcab.2023.102853openalex-snapshot
Enzymatic debittering of citrus juices: Optimization, modeling, and characterization of naringinase production from marine Bacillus subtilis strain BSnari
inferred← citeshttps://doi.org/10.1016/j.bcab.2026.104109openalex-snapshot
Purification, characterization, and debittering potential of naringinase from Bacillus megaterium CP026736: A comparative study with commercial enzyme
inferred← citeshttps://doi.org/10.1016/j.bej.2021.108277openalex-snapshot
Artificial naringinase system for cooperative enzymatic synthesis of naringenin
inferred← citeshttps://doi.org/10.1016/j.bej.2024.109253openalex-snapshot
Engineering artificial fusion naringinase for enhancing naringenin biosynthesis
inferred← citeshttps://doi.org/10.1016/j.bioorg.2025.108121openalex-snapshot
Surface display and characterization of recombinant α-l-Rhamnosidase from Emiliania huxleyi on Pichia pastoris
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2021.109940openalex-snapshot
Screening and characterization of a GH78 α-l-rhamnosidase from Aspergillus terreus and its application in the bioconversion of icariin to icaritin with recombinant β-glucosidase
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2025.110808openalex-snapshot
Naringinase: A comprehensive review on its characteristics, production, and biotechnological applications
inferred← citeshttps://doi.org/10.1016/j.foodchem.2016.06.108openalex-snapshot
Purification and characterization of a naringinase from a newly isolated strain of Bacillus amyloliquefaciens 11568 suitable for the transformation of flavonoids
inferred← citeshttps://doi.org/10.1016/j.foodchem.2024.139600openalex-snapshot
Amination of naringinase to improve citrus juice debittering using a catalyst immobilized on glyoxyl-agarose
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2015.12.093openalex-snapshot
Expression and biochemical characterization of recombinant α-l-rhamnosidase r-Rha1 from Aspergillus niger JMU-TS528
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2018.08.005openalex-snapshot
Kinetic and thermodynamic features of nanomagnetic cross-linked enzyme aggregates of naringinase nanobiocatalyst in naringin hydrolysis
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2026.151208openalex-snapshot
A novel PVA/gelatin hydrogel hybrid integrated with polydopamine-modified microcrystalline cellulose particles for the application in naringinase immobilization
inferred← citeshttps://doi.org/10.1016/j.mimet.2025.107342openalex-snapshot
Bioconversion of naringin to naringenin by a characterized Naringinase from Aspergillus niger HO32: Toward the valorization of citrus flavonoids
inferred← citeshttps://doi.org/10.1016/j.procbio.2017.07.012openalex-snapshot
Characterization of a naringinase from Aspergillus oryzae 11250 and its application in the debitterization of orange juice
inferred← citeshttps://doi.org/10.1016/j.procbio.2020.03.014openalex-snapshot
Naringinase-catalyzed hydrolysis of naringin adsorbed on macroporous resin
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Production of Prunin and Naringenin by Using Naringinase from Aspergillus oryzae NYO-2 and Their Neuroprotective Properties and Debitterization
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A Hyperthermostable Archaeal GH78 Rhamnosidase Efficiently Hydrolyzes Flavonoid Glycosides for Juice Debittering
inferred← citeshttps://doi.org/10.1021/acs.jafc.8b06932openalex-snapshot
Heterologous Expression and Characterization of a New Clade of Aspergillus α-L-Rhamnosidase Suitable for Citrus Juice Processing
inferred← citeshttps://doi.org/10.1021/acsomega.0c05756openalex-snapshot
Novel Strategy of Mussel-Inspired Immobilization of Naringinase with High Activity Using a Polyethylenimine/Dopamine Co-deposition Method
inferred← citeshttps://doi.org/10.1021/jf402711hopenalex-snapshot
Development and Evaluation of an HPLC Method for Accurate Determinations of Enzyme Activities of Naringinase Complex
inferred← citeshttps://doi.org/10.1038/s41598-022-14855-xopenalex-snapshot
Simultaneous production and sustainable eutectic mixture based purification of narringinase with Bacillus amyloliquefaciens by valorization of tofu wastewater
inferred← citeshttps://doi.org/10.1080/07388551.2020.1753648openalex-snapshot
How do biocatalysis and biotransformation affect Citrus dietary flavonoids chemistry and bioactivity? A review
inferred← citeshttps://doi.org/10.1080/10408398.2020.1793726openalex-snapshot
Recent developments in enzyme immobilization technology for high-throughput processing in food industries
inferred← citeshttps://doi.org/10.1111/1541-4337.13129openalex-snapshot
A comprehensive review of the metabolism of citrus flavonoids and their binding to bitter taste receptors
inferred← citeshttps://doi.org/10.1111/ijfs.13796openalex-snapshot
Enzymatic production of natural sweetener trilobatin from citrus flavanone naringin using immobilised α‐ l ‐rhamnosidase as the catalyst
inferred← citeshttps://doi.org/10.1111/lam.13167openalex-snapshot
Comparison between irradiating and autoclaving citrus wastes as substrate for solid‐state fermentation by Aspergillus aculeatus
inferred← citeshttps://doi.org/10.1155/2020/8927858openalex-snapshot
Solid‐State Fermentation of Aspergillus niger to Optimize Extraction Process of Isoliquiritigenin from Glycyrrhiza uralensis
inferred← citeshttps://doi.org/10.13005/bbra/3302openalex-snapshot
Recent Updates on Microbial Naringinase for Debittering of Citrus Juices by Transformation of Flavonoid Naringin
inferred← citeshttps://doi.org/10.1556/066.2020.49.1.13openalex-snapshot
Changes in bitterness, antioxidant activity and total phenolic content of grapefruit juice fermented by Lactobacillus and Bifidobacterium strains
inferred← citeshttps://doi.org/10.15611/pn.2016.461.02openalex-snapshot
Produkcja naringinazy przez Aspergillus niger – optymalizacja składu podłoża / Production of naringinase by Aspergillus niger – culture medium optimization
inferred← citeshttps://doi.org/10.31031/rdms.2018.04.000599openalex-snapshot
Characterization of Nariginase Obtained from Aspergillus niger by Submerged Fermentation Using Naringin Extracted from Lemon Peels
inferred← citeshttps://doi.org/10.3390/ijms26199813openalex-snapshot
Characterization of α-L-Rhamnosidase and β-D-Glucosidase Subunits of Naringinase Immobilized on a Magnetic Polysaccharide Carrier
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