Pseudomonas Lipase Research Articles

Effect of Tween Type Non-Ionic Detergent on the Activity of Lipase of Pseudomonas aeruginosa.

Pseudomonas aeruginosa is a Gram-negative and rod-shaped bacterium. It can use a variety of carbon sources and grow in different culture media. Its versatile extracellular enzymes give it the ability to grow on complex carbon sources. One of the most important enzymes of this bacterium is lipase, which is an extracellular enzyme. Lipases are one of the most useful enzymes in medicine and industry, especially in the detergent industry. In recent years, lipases have become an important component of detergent powders, so it is important to evaluate the performance of lipases in the presence of detergents. The aim of this study was to investigate the effect of non-ionic detergents Tween 20 and 80 on the activity of the Pseudomonas lipase. These detergents reduced Km and increased Vmax of the enzyme. The enzyme activity increased in the presence of these detergents at optimal pH and temperature. Conformational studies with the purified enzyme by fluorescence spectrophotometry showed that in the presence of Tween 20 and 80, there was a hypochromicity in emission peak of the enzyme, which indicated that the enzyme became less compact in vicinity of these detergents.

Co-expression of Pseudomonas alcaligenes lipase and its specific foldase in Pichia pastoris by a dual expression cassette strategy

Lipomax is a commercialized foldase-dependent Pseudomonas lipase that was previously expressed only in Pseudomonas strains. Here, using Pichia pastoris as the host, we report a new co-expression method that leads to the successful production of Lipomax. The active Lipomax is extracellularly co-expressed with its cognate foldase (LIM); and the purified enzyme mix has the optimum pH at pH 8.0 and an optimal temperature around 40 °C. N-glycosylation was observed for Pichia produced Lipomax, and its reduction was shown to increase the lipolytic activity. With different p-nitrophenyl esters as the substrates, the substrate profiling analyses further indicate that Lipomax prefers esters with middle-long chain fatty acids, showing the highest specific activity to p-nitrophenyl caprylate (C8). The extracellular co-expression of Lipomax and LIM in Pichia will not only increase our ability to investigate additional eukaryotic hosts for lipase expression, but also be of considerable value in analyzing other foldase-dependent lipases.

Enhanced Biocatalytic Activity of Recombinant Lipase Immobilized on Gold Nanoparticles.

Bacterial lipases especially Pseudomonas lipases are extensively used for different biotechnological applications. With the better understanding and progressive needs for improving its activity in accordance with the growing market demand, we aimed in this study to improve the recombinant production and biocatalytic activity of lipases via surface conjugation on gold nanoparticles. The full length coding sequences of lipase gene (lipA), lipase specific foldase gene (lipf) and dual cassette (lipAf) gene were amplified from the genomic DNA of Pseudomonas aeruginosa PA14 and cloned into the bacterial expression vector pRSET-B. Recombinant lipases were expressed in E. coli BL-21 (DE3) pLysS then purified using nickel affinity chromatography and the protein identity was confirmed using SDS-PAGE and Western blot analysis. The purified recombinant lipases were immobilized through surface conjugation with gold nanoparticles and enzymatic activity was colorimetrically quantified. Here, two single expression plasmid systems pRSET-B-lipA and pRSET-B-lipf and one dual cassette expression plasmid system pRSET-B-lipAf were successfully constructed. The lipolytic activities of recombinant lipases LipA, Lipf and LipAf were 4870, 426 and 6740 IUmg-1, respectively. However, upon immobilization of these recombinant lipases on prepared gold nanoparticles (GNPs), the activities were 7417, 822 and 13035 IUmg-1, for LipA-GNPs, Lipf-GNPs and LipAf-GNPs, respectively. The activities after immobilization have been increased 1.52 and 1.93 -fold for LipA and LipAf, respectively. The lipolytic activity of recombinant lipases in the bioconjugate was significantly increased relative to the free recombinant enzyme where immobilization had made the enzyme attain its optimum performance.

Site-Specific Addressing of Particles and Coatings via Enzyme-Mediated Destabilization

Enzyme mediated addressing (EMA) is a highly specific and easy-to-apply technology for direction and deposition of particles and coatings on surfaces. Key feature of this process is an enzymatic reaction in direct proximity to the surface, which induces the deposition. The technique has previously shown great success in the handling of biological particles. In this study, addressing of non-biological nanoparticles, in particular plastics and metals, is presented. The respective particles are stabilized by an amphiphilic, enzyme-degradable block copolymer, consisting of poly(ethylene glycol) and poly(caprolactone). After contact with the enzyme pseudomonas lipase, the particles are destabilized, due to the loss of the hydrophilic part of the block copolymer. The lipase is therefore immobilized on glass supports. Immobilization is performed via adsorption or covalent bonding to epoxide groups. All deposition experiments show that addressing of individual particles occurs precisely within the predefined areas of enzyme activity. Depending on the material and reaction conditions, intact nanoparticles or coatings from such can be gained. The quintessence of the study is the indifference of the EMA regarding particle materials. From this rationale, the technique offers near unlimited materials compatibility within a precise, easy-to-apply, and upscalable process.

Pseudomonas Infection Responsive Liquid Crystals for Glycoside Hydrolase and Antibiotic Combination.

Bacterial biofilms account for up to 80% of all community-acquired infections for which bacterial eradication is currently not achievable using conventional antimicrobial treatments. The protective matrix that engulfs biofilm-associated bacteria frequently renders antibiotics ineffective. Glycoside hydrolases are a class of enzymes that break down the biofilm matrix, thereby increasing the effectiveness of antibiotics. Herein, nanostructured liquid crystals composed of glyceryl monooleate (GMO) were investigated as an infection responsive delivery system for alginate lyase (glycoside hydrolase) and gentamicin (antibiotic) to treat Pseudomonas biofilms. The presence of Pseudomonas lipase triggered the release of alginate lyase and gentamicin from the GMO liquid crystals. Treatment with the liquid crystals containing alginate lyase and gentamicin resulted in a greater than 2-log reduction in mucoid Pseudomonas aeruginosa (clinical isolate) biofilm. The anti-biofilm activity of alginate lyase and gentamicin from the liquid crystals was sustained for 2 days and equivalent to the respective unformulated solution treatments. Accordingly, GMO based liquid crystals are a promising responsive delivery system for alginate lyase and gentamicin to combat topicalPseudomonas infections.

Effect of pseudomonas lipase enzyme on the degradation of polycaprolactone/polycaprolactone-polyglycolide fiber blended nanocomposites

ABSTRACTThis study describes the interaction resulting from adding pseudomonas lipase (PS) enzyme to polycaprolactone-based composites designed for orthopedic applications. The biopolymer composite evaluated in this study consists of electrospun polycaprolactone (PCL)/polyglycolide (PGA) blended fibers impregnated with double stranded deoxyribonucleic acid wrapped single-walled carbon nanotubes encapsulated by a PCL matrix. PS enzyme was used to catalyze the degradation of PCL-based biocomposites. PCL present in the biocomposites showed considerable degradation in 4 weeks in the presence of the enzyme, exhibiting a contrast to hydrolytic degradation which lasts several years. PGA-consisting fibers degraded completely within one week of exposure to the enzyme.

PmrA/PmrB Two-Component System Regulation of lipA Expression in Pseudomonas aeruginosa PAO1.

Pseudomonas lipases are well-studied, but few studies have examined the mechanisms of lipase expression regulation. As a global regulatory protein, PmrA controls the expression of multiple genes such as the Dot/Icm apparatus, eukaryotic-like proteins, and secreted effectors. In this study, the effect of PmrA on expression of the lipase lipA in Pseudomonas aeruginosa PAO1 was investigated by knocking out or overexpressing pmrA, rsmY, and rsmA. PmrA regulated the expression of lipA at both the transcriptional and translational level although translation was the pivotal regulatory mechanism for lipA expression. PmrA also regulated the expression of rsmY. Using gel mobility shift assay and pmrA/rsmY double gene knock-out model, we showed that PmrA directly bound to the promoter sequence of rsmY to regulate lipA expression. Translation of lipA was activated by the PmrA/PmrB system via RsmA. Specifically, the Shine-Dalgarno (SD) sequence located at lipA mRNA was overlapped through combination between RsmA and the AGAUGA sequence, subsequently blocking the 30S ribosomal subunit to the SD sequence, leading to translational inhibition of lipA. Transcriptional repression of RsmY initiated translation of lipA through negative translational regulation of rsmA. In conclusion, this study demonstrated that in P. aeruginosa PAO1, PmrA mainly regulated rsmY expression at a translational level to influence lipA expression. RsmY primarily activated lipA translation via negative translational regulation of rsmA.

Heterologous expression and characterization of a new lipase from Pseudomonas fluorescens Pf0\u20131 and used for biodiesel production

As a kind of important biocatalysts, Pseudomonas lipases are commonly applied in various industrial fields. Pflip1, a new extracellular lipase gene from Pseudomonas. fluorescens Pf0–1, was first cloned and respectively expressed in Escherichia coli BL21(DE3) and Pichia pastoris KM71, the recombinant proteins Pflip1a and Pflip1b were later purified separately. Then Pflip1a was further characterized. The optimum pH of Pflip1a was 8.0 and its optimal temperature was 70 °C. After incubation at 70 °C for 12 h, Pflip1a could retain over 95% of its original activity. It showed the highest activity towards p-nitrophenyl caprylate. Moreover, its activity was profoundly affected by metal ion, ionic surfactants and organic solvents. Furthermore, the two obtained recombinant lipases were immobilized on the magnetic nanoparticles for biodiesel preparation. The GC analysis showed that for the immobilized lipases Pflip1b and Pflip1a, the biodiesel yield within 24 h respectively attained 68.5% and 80.5% at 70 °C. The activities of the two immobilized lipases still remained 70% and 82% after 10 cycles of operations in non-solvent system. These characteristics and transesterification capacity of the recombinant protein indicated its great potential for organic synthesis, especially for biodiesel production.

One pot biocatalytic synthesis of a biodegradable electroactive macromonomer based on 3,4-ethylenedioxytiophene and poly(l-lactic acid)

A novel electroactive macromonomer based on poly(l-lactic acid) (PLLA) with (3,4-ethylenedioxythiophene) (EDOT) functional end groups, was prepared by a traditional approach of organometallic polymerization with stannous octanoate [Sn(oct2)] and enzymatic polymerization using immobilized Candida antarctica Lipase B (CAL-B) and Amano lipase Pseudomonas cepacia(PS-IM), as catalysts. In the synthetic strategy, (2,3-dihydrothieno[3,4-b] dioxin-2-yl)methanol (EDOT-OH) was used to initiate the ring opening polymerization of lactide to yield PLLA with EDOT end group. All macromonomers (EDOT-PLLA) were characterized by 1H and 13C RMN, MALDI-TOF, GPC and EDX. Moreover, ICP-OES analysis showed the presence of Sn traces in the material synthesized by the traditional approach, but that pathway led to macromonomers with higher molecular weight while the enzymatic route led to completely metal-free macromonomers with medium and lower molecular weights. Also, electrochemical and chemical polymerization of EDOT-PLLA were tested showing that it is possible to prepare degradable conducting polymers based on poly(3,4-ethylenedioxythiphene) (PEDOT). The biocatalytic synthesis is a very promising and environmental friendly pathway for the preparation of biodegradable materials for short time applications.

The role of Hfq in regulation of lipA expression in Pseudomonas protegens Pf-5

Pseudomonas lipase is a well-studied lipase. However, few studies have been conducted to examine the mechanisms underlying the regulation of the lipase expression. Hfq is a global regulatory protein that, among others, controls the expression of multiple genes, regulate bacterial peristalsis, and participates in the regulation of quorum-sensing (QS) system. In this study, the effects of Hfq on lipase expression were investigated by knocking out the hfq and rsmY genes or overexpressing of hfq and rsmY genes. We found that Hfq regulates the expression of lipA at both transcriptional and translational levels. The translational level was the main regulatory level of lipA. Hfq also regulates the expression and stability of rsmY. Additionally, using hfq/rsmY double gene knock-out, we showed that Hfq can directly bind to the rsmY to regulate lipA activity. In conclusion, our results indicate that Hfq regulates the expression of rsmY mainly at the translational level to influence the expression of lipA in Pseudomonas protegens Pf-5.

Alternative Oils Tested as Feedstocks for Enzymatic FAMEs Synthesis: Toward a More Sustainable Process.

Previously isolated and characterized Pseudomonas lipases were immobilized in a low-cost MP-1000 support by a re-loading procedure that allowed a high activity per weight of support. Immobilized LipA, LipC, and LipCmut lipases, and commercial Novozym® 435 were tested for fatty acid methyl ester (FAMEs) synthesis using conventional and alternative feedstocks. Triolein and degummed soybean oils were used as model substrates, whereas waste cooking oil and M. circinelloides oil were assayed as alternative, low cost feedstocks, whose free fatty acid (FFA), and acylglyceride profile was characterized. The reaction conditions for FAMEs synthesis were initially established using degummed soybean oil, setting up the best water and methanol concentrations for optimum conversion. These conditions were further applied to the alternative feedstocks and the four lipases. The results revealed that Pseudomonas lipases were unable to use the FFAs, displaying a moderate FAMEs synthesis, whereas a 44% FAMEs production was obtained when M. circinelloides oil was used as a substrate in the reaction catalysed by Novozym® 435, used under the conditions established for degummed soybean oil. However, when Novozym® 435 was tested under previously described optimal conditions for this lipase, promising values of 85 and 76% FAMEs synthesis were obtained for waste cooking oil and M. circinelloides oil, respectively, which might result in promising, nonfood, alternative feedstocks for enzymatic biodiesel production. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 33:1209-1217, 2017.

The Pseudomonas transcriptional regulator AlgR controls LipA expression via the noncoding RNA RsmZ in Pseudomonas protegens Pf-5

Pseudomonas lipases are well studied enzymes. However, few studies have been conducted to explore the mechanism underlying the regulation of lipases expression. AlgR, a global regulator, controls the expression of multiple genes, regulates bacterial peristalsis, and participates in the regulation of quorum-sensing (QS) system, and so on. In this study, the effect of AlgR on lipase expression was investigated by knocking out the algR and rsmZ genes or overexpressing them. It is found out that AlgR can regulate the expression of lipA at both transcriptional and translational levels, but the transcriptional level was dominant. AlgR is also able to regulate the expression of rsmX/rsmY/rsmZ. Additionally, using algR/rsmZ double gene knock-out, it showed that AlgR could directly bind to the promoter sequence of rsmZ to regulate lipA activity. In conclusion, this study for the first time indicates that AlgR directly binds to rsmZ to regulates the expression of lipA via regulating transcription of rsmZ, and mainly regulates the expression of lipA at transcriptional level in P. protegens Pf-5.

3D Printed Polycaprolactone Carbon Nanotube Composite Scaffolds for Cardiac Tissue Engineering.

Fabrication of tissue engineering scaffolds with the use of novel 3D printing has gained lot of attention, however systematic investigation of biomaterials for 3D printing have not been widely explored. In this report, well-defined structures of polycaprolactone (PCL) and PCL- carbon nanotube (PCL-CNT) composite scaffolds have been designed and fabricated using a 3D printer. Conditions for 3D printing has been optimized while the effects of varying CNT percentages with PCL matrix on the thermal, mechanical and biological properties of the printed scaffolds are studied. Raman spectroscopy is used to characterise the functionalized CNTs and its interactions with PCL matrix. Mechanical properties of the composites are characterised using nanoindentation. Maximum peak load, elastic modulus and hardness increases with increasing CNT content. Differential scanning calorimetry (DSC) studies reveal the thermal and crystalline behaviour of PCL and its CNT composites. Biodegradation studies are performed in Pseudomonas Lipase enzymatic media, showing its specificity and effect on degradation rate. Cell imaging and viability studies of H9c2 cells from rat origin on the scaffolds are performed using fluorescence imaging and MTT assay, respectively. PCL and its CNT composites are able to show cell proliferation and have the potential to be used in cardiac tissue engineering.

Purification and Application of Lipases from Pseudomonas Species

Lipases are important hydrolytic enzymes that hydrolyze long chain triacylglycerol intodiacylglycerol, monoacylglycerol, glycerol and fatty acids. Lipases are found in microorganisms, fungi,plants and animals. Commercially, useful extracellular lipases are isolated from different bacterial species,including Bacillus, Achromobacter, Alcaligenes, Arthrobacter, Pseudomonas, Staphylococcus andChromobacterium species. Among the Pseudomonas species, Pseudomonas aeruginosa, P. cepacia andP. fluorescence are the major producers of lipases. Bacterial lipases have great industrial applicationsbecause of their stability, selectivity and broad substrate specificity. Due to their large scale applicationin industrial sectors, attention is given to isolate Pseudomonas lipases. In this review, purification strategiesfor lipases isolated from Pseudomonas species have been focussed.

Lipase immobilization on hyroxypropyl methyl cellulose support and its applications for chemo-selective synthesis of β-amino ester compounds

The present study carried out the synthesis of β-amino ester compounds using lipase immobilized on hyroxypropyl methyl cellulose (HMC) support. Initially various lipases (biocatalysts) from different origin were immobilized and subsequently screened to obtain the robust biocatalyst. The lipase Pseudomonas fluorescence (PFL) immobilized on HMC was displayed highest lipase activity, protein content and retention of activity. The physical and biochemical characterization verified immobilization of lipase PFL on the HMC support. This immobilized biocatalyst HMC:PFL (3.5:1) was successfully applied for the practical biocatalytic applications to synthesize variety of β-amino esters. Various eight reaction parameters were optimized in details to achieve the maximum yield and chemo-selectively. The developed biocatalytic protocol was successfully applied to synthesize different industrially important β-amino esters compounds (21 substrates) with an excellent yield (>90%) and remarkable chemo selectivity (>94%). Interestingly, the immobilized HMC:PFL lipase showed 2.1–2.5 folds higher bio-catalytic activity and five times recyclability as compared to the free PFL. The plausible mechanism for lipase catalyzed synthesis of β-amino ester compounds was also proposed.

S‐endo‐2‐Norbornyl‐N‐n‐butylcarbamate as a Potential Pseudomonas Lipase Inhibitor to Probe the Enantioselectivity of the Enzyme by Kinetic and Molecular Docking Evaluation

AbstractObesity is a complex health issue and it can cause many health and social problems. Previous studies reported that lipase is a main target for obesity treatment. We synthesized R‐exo‐2‐norbornyl‐N‐n‐butylcarbamate and S‐exo‐2‐norbornyl‐N‐n‐butylcarbamate as potential pseudomonas lipase inhibitors to probe the enantioselectivity of the enzyme and demonstrated that R‐exo‐2‐norbornyl‐N‐n‐butylcarbamate had better enzyme enantioselectivity, ki and the docking model with Pseudomonas species lipase in our previous studies. In this article, we reported the property of the Pseudomonas species lipase inhibitors, R‐and S‐endo‐2‐norbornyl‐N‐n‐butylcarbamate and compared the docking models of these two compounds with R‐ and S‐exo‐2‐norbornyl‐N‐n‐butylcarbamates by AutoDock. We found that S‐endo‐2‐norbornyl‐N‐n‐butylcarbamate has the best enantioselectivity, ki and docking model and this study could provide useful information about enzyme enantioselectivity for the development of Pseudomonas species lipase inhibitors for obesity treatment.

Biodegradable Glycopolymeric Micelles Obtained by RAFT-controlled Radical Ring-Opening Polymerization

The design and synthesis of an entirely degradable glycopolymer micelle was presented. This design relies on the utilization of RAFT-controlled radical ring-opening polymerization (rROP) technique to afford multiple insertions of cleavable ester linkages onto the backbone of the corona. RAFT polymerization using a macroRAFT agent based on poly(ε-caprolactone) PCL was employed to control the polymerization of well-defined statistical glycopolymers of 1-O-acryloyl-2,3:4,5-di-O-isopropylidene-β-d-fructopyranose (1-O-AiPrFru) and 5,6-benzo-2-methylene-1,3-dioxepane (BMDO) monomer. Three block copolymers were synthesized to generate poly(ε-caprolactone)-b-poly[(1-O-acryloyl-2,3:4,5-di-O-isopropylidene-β-d-fructopyranose)-co-(5,6-benzo-2-methylene-1,3-dioxepane)] (PCL-b-P[(1-O-AiPrFru)-co-(BMDO)]) with varying block lengths. Self-assembly of the deprotected block copolymers generated nonspherical egg shaped micelles, where the shorter chains PCL106-b-P[(1-O-AFru)69-co-(BMDO)9] underwent self-assembly forming micelles with the hydrodynamic diameter (DH) of 106 nm. The biodegradation of these micelles were investigated via enzymatic degradation by Lipase Pseudomonas sp., indicating entirely degradable architectures, which are no longer visible via dynamic light scattering (DLS). SEC further confirmed the appearance of fragmented glycopolymeric units. In vitro cell proliferation assay of the micelles and their degradation products revealed no toxicity against healthy human fibroblast HS27 and breast cancer MDA-MB-231 cell lines. The polymer concentration range tested was up to 0.20 mg·mL–1 with the cell viabilities of ≥95%.

Characterization and enzymatic degradation study of poly(ε-caprolactone)-based biocomposites from almond agricultural by-products

Reinforced poly(ε-caprolactone) (PCL)/almond skin (AS) biocomposites were prepared by extrusion and injection moulding at different AS contents (0, 10, 20, 30 wt%) in order to revalorize this agricultural residue. AS particles were characterized by field emission scanning electron microscopy (FESEM), attenuated total reflectance infrared spectroscopy (ATR-FTIR) and thermogravimetric analysis (TGA). Hemicelluloses were the first compound thermally degraded (263 ± 2 °C) followed by cellulose (330 ± 5 °C) and lignin (401 ± 3 °C) with a remaining residue of 20% which was associated to the fibre content present in AS. Mechanical, morphological, thermal, and water absorption properties; and enzymatic degradation using Pseudomonas lipase were evaluated for the obtained biocomposites. A significant improvement in Young's modulus with a gain of 73% at 30 wt% AS loading was obtained compared to neat PCL. An increase in Shore D hardness and decrease in elongation at break and impact energy were also observed with increasing AS content caused by the reinforcement effect. Lower DSC thermal enthalpies and higher crystallinity were obtained for the biocomposites. Some decrease in thermal stability and higher water absorption values were also found with AS addition. Finally, the presence of AS retarded the enzymatic degradation of PCL, showing neat PCL higher weight loss after 25 days of study followed by PCL with 10 wt% AS.

Enhanced biocatalytic activity of immobilized Pseudomonas cepacia lipase under sonicated condition.

The present work reports the use of biocatalyst and ultrasound for greener synthesis of cinnamyl propionate. The lipase Pseudomonas cepacia was immobilized on a copolymer of hydroxypropyl methyl cellulose and polyvinyl alcohol. This biocatalyst was u sed for ultrasound-assisted synthesis of cinnamyl propionate with the detailed optimization of various reaction parameters. Besides this, protocol was extended to synthesize various industrially important propionate esters. In addition to this, different enzyme-kinetic parameters such as r max and K m(vinyl propionate), K m(cinnamyl alcohol) and K i(cinnamyl alcohol) were studied which presented ordered bi-bi mechanism with an inhibition by cinnamyl alcohol. The developed biocatalyst demonstrated enhancement in catalytic activity and recyclability up to five recycles. Moreover, the biocatalyst was tested to investigate the effects of sonication via various characterization techniques such as scanning electron microscopy, thermogravimetry, and water content analysis.

Rationally Separating the Corona and Membrane Functions of Polymer Vesicles for Enhanced T₂ MRI and Drug Delivery.

It is an important challenge to in situ grow ultrafine super-paramagnetic iron oxide nanoparticles (SPIONs) in drug carriers such as polymer vesicles (also called polymersomes) while keeping their biodegradability for enhanced T2-weighted magnetic resonance imaging (MRI) and drug delivery. Herein, we present a new strategy by rationally separating the corona and membrane functions of polymer vesicles to solve the above problem. We designed a poly(ethylene oxide)-block-poly(ε-caprolactone)-block-poly(acrylic acid) (PEO43-b-PCL98-b-PAA25) triblock copolymer and self-assembled it into polymer vesicle. The PAA chains in the vesicle coronas are responsible for the in situ nanoprecipitation of ultrafine SPIONs, while the vesicle membrane composed of PCL is biodegradable. The SPIONs-decorated vesicle is water-dispersible, biocompatible, and slightly cytotoxic to normal human cells. Dynamic light scattering, transmission electron microscopy, energy disperse spectroscopy, and vibrating sample magnetometer revealed the formation of ultrafine super-paramagnetic Fe3O4 nanoparticles (1.9 ± 0.3 nm) in the coronas of polymer vesicles. Furthermore, the CCK-8 assay revealed low cytotoxicity of vesicles against normal L02 liver cells without and with Fe3O4 nanoparticles. The in vitro and in vivo MRI experiments confirmed the enhanced T2-weighted MRI sensitivity and excellent metastasis in mice. The loading and release experiments of an anticancer drug, doxorubicin hydrochloride (DOX·HCl), indicated that the Fe3O4-decorated magnetic vesicles have potential applications as a nanocarrier for anticancer drug delivery. Moreover, the polymer vesicle is degradable in the presence of enzyme such as Pseudomonas lipases, and the ultrafine Fe3O4 nanoparticles in the vesicle coronas are confirmed to be degradable under weakly acidic conditions. Overall, this decoration-in-vesicle-coronas strategy provides us with a new insight for preparing water-dispersible ultrafine super-paramagnetic Fe3O4 nanoparticles with promising theranostic applications in biomedicine.