On the public citation graph

Enzymatic Synthesis of Phytosterol Esters Using Recombinant E. Coli Whole Cell Expressing Lipase from Burkholderia Sp

https://doi.org/10.2139/ssrn.5216344
0 signed · 44 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1097-0290(19960305)49:5<527::aid-bit5>3.0.co;2-lopenalex-snapshot
Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials
inferredcites →https://doi.org/10.1002/cbic.200300761openalex-snapshot
Lipase‐Specific Foldases
inferredcites →https://doi.org/10.1002/jsfa.13152openalex-snapshot
Ionic liquid modification reshapes the substrate pockets of lipase to boost its stability and activity in vitamin E succinate synthesis
inferredcites →https://doi.org/10.1002/ptr.7312openalex-snapshot
Biological and pharmacological effects and nutritional impact of phytosterols: A comprehensive review
inferredcites →https://doi.org/10.1007/978-1-0716-3385-4_15openalex-snapshot
Bioconversion of Phytosterols into Androstenedione by Mycolicibacterium
inferredcites →https://doi.org/10.1007/978-981-16-5214-1_12openalex-snapshot
Biotransformation of Industrially Important Steroid Drug Precursors
inferredcites →https://doi.org/10.1007/s00203-023-03541-9openalex-snapshot
Factors involved in heterologous expression of proteins in E. coli host
inferredcites →https://doi.org/10.1007/s00792-005-0494-8openalex-snapshot
Purification, characterization, and molecular cloning of organic-solvent-tolerant cholesterol esterase from cyclohexane-tolerant Burkholderia cepacia strain ST-200
inferredcites →https://doi.org/10.1007/s12010-020-03453-0openalex-snapshot
Co-Expression of a Thermally Stable and Methanol-Resistant Lipase and Its Chaperone from Burkholderia cepacia G63 in Escherichia coli
inferredcites →https://doi.org/10.1007/s12551-020-00754-wopenalex-snapshot
Mechanisms of action of ionic liquids on living cells: the state of the art
inferredcites →https://doi.org/10.1016/j.bej.2020.107695openalex-snapshot
Improving whole-cell biocatalysis for helicid benzoylation by the addition of ionic liquids
inferredcites →https://doi.org/10.1016/j.bej.2023.109023openalex-snapshot
Hydrocortisone production using whole-cell biocatalysts in recombinant Escherichia coli
inferredcites →https://doi.org/10.1016/j.biotechadv.2024.108422openalex-snapshot
Yeast surface display technology: Mechanisms, applications, and perspectives
inferredcites →https://doi.org/10.1016/j.fbio.2024.104023openalex-snapshot
Artificial preparation, biosynthetic, health effects, and applications of phytosterol and phytosterol ester: A review
inferredcites →https://doi.org/10.1016/j.foodchem.2019.125858openalex-snapshot
Synergistic effects of binary ionic liquid-solvent systems on enzymatic esterification of esculin
inferredcites →https://doi.org/10.1016/j.foodchem.2021.131256openalex-snapshot
An efficient and robust continuous-flow bioreactor for the enzymatic preparation of phytosterol esters based on hollow lipase microarray
inferredcites →https://doi.org/10.1016/j.foodchem.2024.139100openalex-snapshot
Preparation of functional oils rich in phytosterol esters and diacylglycerols by enzymatic transesterification
inferredcites →https://doi.org/10.1016/j.ijbiomac.2020.11.184openalex-snapshot
Bacterial triacylglycerol lipase is a potential cholesterol esterase: Identification of a key determinant for sterol-binding specificity
inferredcites →https://doi.org/10.1016/j.lwt.2023.114929openalex-snapshot
Ultrasound pretreatment for lipase-catalyzed synthesis of stigmasteryl oleate and evaluation of its physicochemical properties
inferredcites →https://doi.org/10.1016/j.lwt.2024.116598openalex-snapshot
Immobilized Burkholderia cepacia lipase and its application in selective enrichment of EPA by hydrolysis of fish oil
inferredcites →https://doi.org/10.1016/j.molcatb.2010.01.002openalex-snapshot
Lipases for use in industrial biocatalysis: Specificity of selected structural groups of lipases
inferredcites →https://doi.org/10.1016/j.molliq.2017.12.050openalex-snapshot
Ionic liquids as a potential solvent for lipase-catalysed reactions: A review
inferredcites →https://doi.org/10.1016/j.plipres.2018.04.001openalex-snapshot
Phytosterols and their derivatives: Structural diversity, distribution, metabolism, analysis, and health-promoting uses
inferredcites →https://doi.org/10.1016/s0969-2126(97)00177-9openalex-snapshot
The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor
inferredcites →https://doi.org/10.1021/acs.jafc.8b00059openalex-snapshot
Plant Sterols: Chemical and Enzymatic Structural Modifications and Effects on Their Cholesterol-Lowering Activity
inferredcites →https://doi.org/10.1021/acs.jcim.3c00194openalex-snapshot
The Conformational Transitions and Dynamics of Burkholderia cepacia Lipase Regulated by Water–Oil Interfaces
inferredcites →https://doi.org/10.1021/acsami.2c11500openalex-snapshot
Amphiphilic Nanointerface: Inducing the Interfacial Activation for Lipase
inferredcites →https://doi.org/10.1021/acscatal.0c05015openalex-snapshot
Computationally Driven Rational Design of Substrate Promiscuity on Serine Ester Hydrolases
inferredcites →https://doi.org/10.1021/acssuschemeng.0c05296openalex-snapshot
Effect of Cholinium Amino Acids Ionic Liquids As Cosolvents on the Bioconversion of Phytosterols by Mycobacterium sp. Resting Cells
inferredcites →https://doi.org/10.1021/acssuschemeng.1c07332openalex-snapshot
How Does Surface Charge Engineering of Bacillus subtilis Lipase A Improve Ionic Liquid Resistance? Lessons Learned from Molecular Dynamics Simulations
inferredcites →https://doi.org/10.1021/acssuschemeng.2c04216openalex-snapshot
Enzyme Hydration: How to Retain Resistance in Ionic Liquids
inferredcites →https://doi.org/10.1021/acssuschemeng.3c05735openalex-snapshot
CRISPR Tools in Bacterial Whole-Cell Biocatalysis
inferredcites →https://doi.org/10.1038/s41598-020-60093-4openalex-snapshot
Structural and dynamic insights revealing how lipase binding domain MD1 of Pseudomonas aeruginosa foldase affects lipase activation
inferredcites →https://doi.org/10.1080/10408398.2020.1764489openalex-snapshot
Immobilized microbial lipases in the food industry: a systematic literature review
inferredcites →https://doi.org/10.1080/10408398.2021.1888692openalex-snapshot
A review on chemical and physical modifications of phytosterols and their influence on bioavailability and safety
inferredcites →https://doi.org/10.1080/1040841x.2025.2461054openalex-snapshot
A multifarious bacterial surface display: potential platform for biotechnological applications
inferredcites →https://doi.org/10.1128/aem.65.2.787-794.1999openalex-snapshot
High-Level Formation of Active Pseudomonas cepacia Lipase after Heterologous Expression of the Encoding Gene and Its Modified Chaperone in Escherichia coli and Rapid In Vitro Refolding
inferredcites →https://doi.org/10.1128/jb.173.15.4836-4841.1991openalex-snapshot
Extracellular lipase of Pseudomonas sp. strain ATCC 21808: purification, characterization, crystallization, and preliminary X-ray diffraction data
inferredcites →https://doi.org/10.1186/s12896-016-0269-6openalex-snapshot
Cell-bound lipases from Burkholderia sp. ZYB002: gene sequence analysis, expression, enzymatic characterization, and 3D structural model
inferredcites →https://doi.org/10.1186/s12934-024-02385-2openalex-snapshot
Pregnenolone and progesterone production from natural sterols using recombinant strain of Mycolicibacterium smegmatis mc2 155 expressing mammalian steroidogenesis system
inferredcites →https://doi.org/10.18388/abp.2013_1999openalex-snapshot
A simple method for the determination of the cholesterol esterase activity.
inferredcites →https://doi.org/10.3390/catal12010088openalex-snapshot
Lipases as Effective Green Biocatalysts for Phytosterol Esters’ Production: A Review
inferredcites →https://doi.org/10.3390/ijms21113925openalex-snapshot
Functional Heterologous Expression of Mature Lipase LipA from Pseudomonas aeruginosa PSA01 in Escherichia coli SHuffle and BL21 (DE3): Effect of the Expression Host on Thermal Stability and Solvent Tolerance of the Enzyme Produced
inferredcites →https://doi.org/10.4103/1735-5362.288424openalex-snapshot
Evaluation of soluble expression of recombinant granulocyte macrophage stimulating factor (rGM-CSF) by three different E. coli strains
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.