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https://doi.org/10.2139/ssrn.4654627

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inferredcites →https://doi.org/10.1002/cbic.201800421openalex-extracted
Design of Artificial Alcohol Oxidases: Alcohol Dehydrogenase–NADPH Oxidase Fusions for Continuous Oxidations
inferredcites →https://doi.org/10.1002/cbic.201800814openalex-extracted
Convergent Cascade Catalyzed by Monooxygenase–Alcohol Dehydrogenase Fusion Applied in Organic Media
inferredcites →https://doi.org/10.1002/prot.20244openalex-extracted
Conformations of variably linked chimeric proteins evaluated by synchrotron X‐ray small‐angle scattering
inferredcites →https://doi.org/10.1007/978-1-61779-433-9_5openalex-extracted
Heat-Shock Protein Fusion Vectors for Improved Expression of Soluble Recombinant Proteins in Escherichia coli
inferredcites →https://doi.org/10.1007/bf00339139openalex-extracted
Heat-stable enzymes from extremely thermophilic and hyperthermophilic microorganisms
inferredcites →https://doi.org/10.1007/s00217-006-0288-yopenalex-extracted
Immobilization and characterization of naringinase for the hydrolysis of naringin
inferredcites →https://doi.org/10.1007/s00239-017-9824-6openalex-extracted
From Molecules to Life: Quantifying the Complexity of Chemical and Biological Systems in the Universe
inferredcites →https://doi.org/10.1007/s00253-016-8011-9openalex-extracted
Fusion of agarase and neoagarobiose hydrolase for mono-sugar production from agar
inferredcites →https://doi.org/10.1007/s00253-017-8501-4openalex-extracted
Coupled reactions by coupled enzymes: alcohol to lactone cascade with alcohol dehydrogenase–cyclohexanone monooxygenase fusions
inferredcites →https://doi.org/10.1007/s10295-018-02134-6openalex-extracted
Modulating heterologous pathways and optimizing fermentation conditions for biosynthesis of kaempferol and astragalin from naringenin in Escherichia coli
inferredcites →https://doi.org/10.1007/s10529-020-02845-wopenalex-extracted
Biotransformation of cladribine by a magnetic immobilizated biocatalyst of Lactobacillus animalis
inferredcites →https://doi.org/10.1016/j.bej.2021.108277openalex-extracted
Artificial naringinase system for cooperative enzymatic synthesis of naringenin
inferredcites →https://doi.org/10.1016/j.bej.2022.108524openalex-extracted
Levan-type fructooligosaccharides synthesis by novel levansucrase-inulosucrase fusion enzyme
inferredcites →https://doi.org/10.1016/j.biortech.2017.06.002openalex-extracted
An efficient production of high-pure xylooligosaccharides from corncob with affinity adsorption-enzymatic reaction integrated approach
inferredcites →https://doi.org/10.1016/j.biotechadv.2011.05.020openalex-extracted
Substrate channeling and enzyme complexes for biotechnological applications
inferredcites →https://doi.org/10.1016/j.biotechadv.2014.11.005openalex-extracted
Synthetic fusion protein design and applications
inferredcites →https://doi.org/10.1016/j.enzmictec.2008.10.007openalex-extracted
Construction of a fusion enzyme of dextransucrase and dextranase: Application for one-step synthesis of isomalto-oligosaccharides
inferredcites →https://doi.org/10.1016/j.enzmictec.2017.07.004openalex-extracted
Impact of orientation of carbohydrate binding modules family 22 and 6 on the catalytic activity of Thermotoga maritima xylanase XynB
inferredcites →https://doi.org/10.1016/j.enzmictec.2020.109692openalex-extracted
Production of indigo through the use of a dual-function substrate and a bifunctional fusion enzyme
inferredcites →https://doi.org/10.1016/j.foodchem.2006.01.032openalex-extracted
Determination of flavonoids in a Citrus fruit extract by LC–DAD and LC–MS
inferredcites →https://doi.org/10.1016/j.foodchem.2010.06.024openalex-extracted
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.foodchem.2016.06.108openalex-extracted
Purification and characterization of a naringinase from a newly isolated strain of Bacillus amyloliquefaciens 11568 suitable for the transformation of flavonoids
inferredcites →https://doi.org/10.1016/j.foodres.2009.04.016openalex-extracted
Anti-inflammatory activity of naringin and the biosynthesised naringenin by naringinase immobilized in microstructured materials in a model of DSS-induced colitis in mice
inferredcites →https://doi.org/10.1016/j.ifset.2021.102790openalex-extracted
Immobilization of naringinase on asymmetric organic membranes: Application for debittering of grapefruit juice
inferredcites →https://doi.org/10.1016/j.ijbiomac.2015.06.057openalex-extracted
Biochemical characterization of three phase partitioned naringinase from Aspergillus brasiliensis MTCC 1344
inferredcites →https://doi.org/10.1016/j.ijbiomac.2018.01.080openalex-extracted
Bi-functional fusion enzyme EG-M-Xyn displaying endoglucanase and xylanase activities and its utility in improving lignocellulose degradation
inferredcites →https://doi.org/10.1016/j.ijbiomac.2022.09.222openalex-extracted
Fusion enzyme design based on the “channelization” cascade theory and homogenous dextran product improvement
inferredcites →https://doi.org/10.1016/j.indcrop.2021.114106openalex-extracted
Enhancing the enzymatic hydrolysis efficiency of lignocellulose assisted by artificial fusion enzyme of swollenin-xylanase
inferredcites →https://doi.org/10.1016/j.jbiotec.2010.07.007openalex-extracted
An efficient bioprocess for enzymatic production of l-menthol with high ratio of substrate to catalyst using whole cells of recombinant E. coli
inferredcites →https://doi.org/10.1016/j.jbiotec.2012.09.016openalex-extracted
Rational design of a tripartite fusion protein of heparinase I enables one-step affinity purification and real-time activity detection
inferredcites →https://doi.org/10.1016/j.jbiotec.2014.11.025openalex-extracted
Escherichia coli EDA is a novel fusion expression partner to improve solubility of aggregation-prone heterologous proteins
inferredcites →https://doi.org/10.1016/j.jbiotec.2016.03.045openalex-extracted
Human xanthine oxidase recombinant in E. coli: A whole cell catalyst for preparative drug metabolite synthesis
inferredcites →https://doi.org/10.1016/j.jnutbio.2022.108967openalex-extracted
Beneficial effects of citrus flavanones naringin and naringenin and their food sources on lipid metabolism: An update on bioavailability, pharmacokinetics, and mechanisms
inferredcites →https://doi.org/10.1016/j.lwt.2022.113390openalex-extracted
Enhancement of the performance of the GH75 family chitosanases by fusing a carbohydrate binding module and insights into their substrate binding mechanisms
inferredcites →https://doi.org/10.1016/j.procbio.2017.07.012openalex-extracted
Characterization of a naringinase from Aspergillus oryzae 11250 and its application in the debitterization of orange juice
inferredcites →https://doi.org/10.1016/j.procbio.2020.03.014openalex-extracted
Naringinase-catalyzed hydrolysis of naringin adsorbed on macroporous resin
inferredcites →https://doi.org/10.1016/j.tox.2008.11.012openalex-extracted
Naringenin protects against cadmium-induced oxidative renal dysfunction in rats
inferredcites →https://doi.org/10.1016/j.ymben.2005.11.001openalex-extracted
Functional expression of a P450 flavonoid hydroxylase for the biosynthesis of plant-specific hydroxylated flavonols in Escherichia coli
inferredcites →https://doi.org/10.1021/jf303512qopenalex-extracted
Purification and Characterization of a Naringinase fromAspergillus aculeatusJMUdb058
inferredcites →https://doi.org/10.1038/nchem.2459openalex-extracted
Substrate channelling as an approach to cascade reactions
inferredcites →https://doi.org/10.1039/c4ra05891gopenalex-extracted
A fusion enzyme consisting of bacterial expansin and endoglucanase for the degradation of highly crystalline cellulose
inferredcites →https://doi.org/10.1039/c6fo00633gopenalex-extracted
Absorption and disposition of naringenin and quercetin after simultaneous administration via intestinal perfusion in mice
inferredcites →https://doi.org/10.1107/s1399004713032276openalex-extracted
Structural analysis of β-glucosidase mutants derived from a hyperthermophilic tetrameric structure
inferredcites →https://doi.org/10.1107/s1744309111035238openalex-extracted
Structure of hyperthermophilic β-glucosidase from Pyrococcus furiosus
inferredcites →https://doi.org/10.1128/aem.62.8.2875-2882.1996openalex-extracted
Keratin Degradation by Fervidobacterium pennavorans, a Novel Thermophilic Anaerobic Species of the Order Thermotogales
inferredcites →https://doi.org/10.1128/aem.71.7.3617-3623.2005openalex-extracted
Metabolic Engineering of Anthocyanin Biosynthesis in Escherichia coli
inferredcites →https://doi.org/10.1128/jb.01023-10openalex-extracted
Genome Sequence of the Polysaccharide-Degrading, Thermophilic AnaerobeSpirochaeta thermophilaDSM 6192
inferredcites →https://doi.org/10.1155/2019/9752826openalex-extracted
Preventive Effect of Naringin on Metabolic Syndrome and Its Mechanism of Action: A Systematic Review
inferredcites →https://doi.org/10.1186/s12934-017-0724-7openalex-extracted
Whole-cell biocatalysts by design
inferredcites →https://doi.org/10.1186/s12934-020-01501-2openalex-extracted
Construction and characterization of a novel glucose dehydrogenase-leucine dehydrogenase fusion enzyme for the biosynthesis of l-tert-leucine
inferredcites →https://doi.org/10.1186/s13068-018-1301-yopenalex-extracted
Expression of an endoglucanase–cellobiohydrolase fusion protein in Saccharomyces cerevisiae, Yarrowia lipolytica, and Lipomyces starkeyi
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