scholarly journals Magnetic Biocatalysts of Pectinase: Synthesis by Macromolecular Cross-Linker for Application in Apple Juice Clarification

2020 ◽  
Vol 58 (4) ◽  
Author(s):  
Marjan Nouri ◽  
Faramarz Khodaiyan
Keyword(s):  
Enzyme Immobilization ◽  
Apple Juice ◽  
Magnetic Particles ◽  
Industrial Applications ◽  
Biochemical Properties ◽  
Free Form ◽  
Kinetics Parameters ◽  
Cross Linker ◽  
Pectinase Enzyme ◽  
Excellent Stability

Research background. Pectinase enzyme has become a valuable compound in beverage industry. One of the most significant concepts to overcome the drawbacks of using industrial enzymes is the immobilization of enzymes. In the present study, magnetic chitosan microparticles were utilized as a substrate for pectinase enzyme immobilization. New methods of enzyme immobilization involve the use of non-chemical cross-linkers between the enzyme and the substrate. The aim of this study was to immobilize the pectinase enzyme using polyaldehyde kefiran as a macromolecular crosslinker on magnetic particles. Experimental approach. Pectinase enzyme was immobilized in four steps: relative oxidation of kefiran and its application as a crosslinker; production of magnetic iron (II, III) oxide (Fe3O4) microparticles; coating of magnetic Fe3O4 microparticles with chitosan; and immobilization of enzyme on the substrate, prepared by the use of oxidized kefiran crosslinker. Parameters, such as crosslinking concentration, time, and ratio of chitosan magnetic microparticles to enzyme, were optimized. Fourier-transform infrared spectroscopy (FTIR), dynamic light scattering (DLS), transmission electron microscopy (TEM), and vibrating sample magnetometer (VSM) were used to identify the groups and investigate the structures. The biochemical properties (stability of enzyme activity at different pH, temperature and time), enzyme reusability, kinetics parameters (Km and Vmax) and apple juice turbidity, using free and immobilized pectinase enzymes, were also measured. Results and conclusions. Cross-linker concentration, crosslinking time and ratio of CMMP to enzyme were important factors in activity recovery of pectinase enzyme. FTIR analysis correctly identified functional groups in the structures. The results showed that after enzyme stabilization, the particle size and molecular mass increased and decreased the magnetic saturation strength, respectively. According to the thermal kinetic study, the immobilized pectinase was higher than its free form. In the present study, findings indicate the excellent stability and durability of the immobilized pectinase. Findings indicate the excellent stability and durability of the immobilized pectinase in present study. Finally, a magnetic pectinase micro-biocatalyst was used to clarify apple juice, which reduced turbidity of processing. Novelty and scientific contribution. This study investigates the usage of kefiran oxidized as a new cross linker for the immobilization of pectinase enzyme. Magnetic pectinase micro-biocatalyst has a good potential for industrial applications in the food industry, with high thermal stability.

scholarly journals Enhanced Performance of Immobilized Xylanase/Filter Paper-ase on a Magnetic Chitosan Support

Catalysts ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 966
Author(s):  
Aldo Amaro-Reyes ◽  
Azariel Díaz-Hernández ◽  
Jorge Gracida ◽  
Blanca E. García-Almendárez ◽  
Monserrat Escamilla-García ◽  
...  
Keyword(s):  
Filter Paper ◽  
Catalytic Efficiency ◽  
Cost Effective ◽  
Immobilized Enzymes ◽  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Biochemical Properties ◽  
Free Form ◽  
Cross Linking ◽  
Magnetic Chitosan

Enzyme immobilization on different supports has emerged as an efficient and cost-effective tool to improve their stability and reuse capacity. This work aimed to produce a stable immobilized multienzymatic system of xylanase and filter paper-ase (FPase) onto magnetic chitosan using genipin as a cross-linking agent and to evaluate its biochemical properties and reuse capacity. A mixture of chitosan magnetic nanoparticles, xylanase, and FPase was covalently bonded using genipin. Immobilization yield and efficiency were quantified. The activity of free and immobilized enzymes was quantified at different values of pH, temperature, substrate concentration (Km and Vmax), and reuse cycles. The immobilization yield, immobilization efficiency, and activity recovery were 145.3% ± 3.06%, 14.8% ± 0.81%, and 21.5% ± 0.72%, respectively, measured as the total hydrolytic activity. Immobilization confers resistance to acidic/basic conditions and thermal stability compared to the free form. Immobilization improved 3.5-fold and 78-fold the catalytic efficiency (Kcat/Km) of the xylanase and filter paper-ase activities, while immobilized xylanase and FPase could be reused for 34 min and 43 min, respectively. Cross-linking significantly improved the biochemical properties of immobilized enzymes, combined with their simplicity of reuse due to the paramagnetic property of the support. Multienzyme immobilization technology is an important issue for industrial applications.

Synthesis and Properties of Fe3O4 Ferrofluids with Narrow Particle Size Distribution

2011 ◽  
Vol 694 ◽  
pp. 575-579
Author(s):  
Jian Hui Zhang ◽  
Hai Bo Sun
Keyword(s):  
Magnetic Particles ◽  
Particle Diameter ◽  
Free Form ◽  
Narrow Particle Size Distribution ◽  
Particle Sizes ◽  
Bingham Plastic ◽  
Plastic Fluid ◽  
Form Model ◽  
The Mean ◽  
Inference Theory

Fe3O4 ferrofluids with uniform magnetic particles were prepared via improved chemical coprecipation technique. A narrow distribution of 8.6-10.8 nm particle sizes was obtained from the magnetization curve using the free-form-model based on Bayesian inference theory. The mean particle diameter about 9.8 nm is consistent with the XRD and SEM results. The hydrodynamic properties of ferrofluids were investigated with different applied magnetic field and shear rate. The experimental results show that diluted ferrofluid and concentrated ferrofluid are Newtonian-fluid and Bingham-plastic fluid, respectively.

Lyapunov Control Strategy for Thermoelectric Cooler Activating an Ice-Clamping System

2018 ◽  
Vol 10 (4) ◽  
Author(s):  
Alexandra Mironova ◽  
Paolo Mercorelli ◽  
Andreas Zedler
Keyword(s):  
Manufacturing Systems ◽  
Control Strategies ◽  
Industrial Applications ◽  
Machining Process ◽  
Free Form ◽  
Cooling Power ◽  
Machining Processes ◽  
Clamping System ◽  
Ice Strength ◽  
Free Form Surfaces

Deformation-free clamping plays an important role in manufacturing systems helping to ensure zero-defect production. The fixture of workpieces during machining processes poses challenges not only for microparts but also for thin-walled pieces or free-form surfaces in macromanufacturing. To address this challenge, a nontraditional adhesive technique, using frozen water to clamp, is introduced in this paper. By increasing the cooling power and thus reducing the temperature of the clamping plate, higher adhesive ice strength and, therefore, a safer clamping system during machining process, can be achieved. The objective of this investigation is to ensure a stable low temperature and to compensate for thermal disturbances. Thanks to their structural robustness, Lyapunov-based control strategies demonstrate an appropriate capability to achieve these results in real industrial applications. Model design of the clamping system as well as simulation and experimental results are shown and discussed.

scholarly journals Molecular Properties and New Potentials of Plant Nepenthesins

Plants ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 570
Author(s):  
Zelalem Eshetu Bekalu ◽  
Giuseppe Dionisio ◽  
Henrik Brinch-Pedersen
Keyword(s):  
Current Knowledge ◽  
Industrial Applications ◽  
Biochemical Properties ◽  
Carnivorous Plant ◽  
Current Data ◽  
Fungal Resistance ◽  
Limited Attention ◽  
Specific Sequence ◽  
Aspartic Proteases ◽  
Trait Improvement

Nepenthesins are aspartic proteases (APs) categorized under the A1B subfamily. Due to nepenthesin-specific sequence features, the A1B subfamily is also named nepenthesin-type aspartic proteases (NEPs). Nepenthesins are mostly known from the pitcher fluid of the carnivorous plant Nepenthes, where they are availed for the hydrolyzation of insect protein required for the assimilation of insect nitrogen resources. However, nepenthesins are widely distributed within the plant kingdom and play significant roles in plant species other than Nepenthes. Although they have received limited attention when compared to other members of the subfamily, current data indicates that they have exceptional molecular and biochemical properties and new potentials as fungal-resistance genes. In the current review, we provide insights into the current knowledge on the molecular and biochemical properties of plant nepenthesins and highlights that future focus on them may have strong potentials for industrial applications and crop trait improvement.

scholarly journals Highly efficient novel recombinant L-asparaginase with no glutaminase activity from a new halo-thermotolerant Bacillus strain

Bioimpacts ◽  
2018 ◽  
Vol 9 (1) ◽  
pp. 15-23 ◽  
Author(s):  
Azam Safary ◽  
Rezvan Moniri ◽  
Maryam Hamzeh-Mivehroud ◽  
Siavoush Dastmalchi
Keyword(s):  
Lymphoblastic Leukemia ◽  
Industrial Applications ◽  
Biochemical Properties ◽  
Substrate Affinity ◽  
Bacillus Sp ◽  
Recombinant Enzymes ◽  
E Coli ◽  
Bacillus Strain ◽  
Antineoplastic Effect ◽  
Wide Range

Introduction: The bacterial enzyme has gained more attention in therapeutic application because of the higher substrate specificity and longer half-life. L-asparaginase is an important enzyme with known antineoplastic effect against acute lymphoblastic leukemia (ALL). Methods: Novel L-asparaginase genes were identified from a locally isolated halo-thermotolerant Bacillus strain and the recombinant enzymes were overexpressed in modified E. coli strains, OrigamiTM B and BL21. In addition, the biochemical properties of the purified enzymes were characterized, and the enzyme activity was evaluated at different temperatures, pH, and substrate concentrations. Results: The concentration of pure soluble enzyme obtained from Origami strain was ~30 mg/L of bacterial culture, which indicates the significant improvement compared to L-asparaginase produced by E. coli BL21 strain. The catalytic activity assay on the identified L-asparaginases (ansA1 and ansA3 genes) from Bacillus sp. SL-1 demonstrated that only ansA1 gene codes an active and stable homologue (ASPase A1) with high substrate affinity toward L-asparagine. The Kcat and Km values for the purified ASPase A1 enzyme were 23.96s-1 and 10.66 µM, respectively. In addition, the recombinant ASPase A1 enzyme from Bacillus sp. SL-1 possessed higher specificity to L-asparagine than L-glutamine. The ASPase A1 enzyme was highly thermostable and resistant to the wide range of pH 4.5–10. Conclusion: The biochemical properties of the novel ASPase A1 derived from Bacillus sp. SL-l indicated a great potential for the identified enzyme in pharmaceutical and industrial applications.

scholarly journals Jet cutter as tool to immobilize lipase for biodiesel production

2019 ◽  
Author(s):  
Marcelo D'Elia Feliciano ◽  
Ana Silvia Prata Soares ◽  
Marcus Bruno Soares Forte ◽  
Beatriz Travalia
Keyword(s):  
Mass Transfer ◽  
Environmental Impacts ◽  
Enzyme Immobilization ◽  
Contact Area ◽  
Industrial Applications ◽  
Biodiesel Production ◽  
Immobilize Lipase ◽  
Technical Aspects ◽  
Size Of Particles ◽  
Low Rate

The use of lipases as a biocatalyst for industrial applications is an interesting route due to technical aspects but also to reduce environmental impacts caused by the use of chemical catalysts. Gel immobilization of the enzyme allows its reuse and avoids contamination of the product with residual portions of free enzyme. However, a typical technique available for enzyme immobilization is based on dripping driven by gravity which produces big particles and low rate of production. The reduction of size can improve the mass transfer by increasing the contact area. Thus, aiming to increase the rate of particles production and reduce the size of particles, the objective of this work was to encapsulate lipase, using a tool designed to cut the jet produced by pumping, called as Jet Cutter.

scholarly journals A Novel Neoagarotriose-Producing Agarase from the Marine Bacterium Gilvimarinus Agarilyticus JEA5

2020 ◽  
Author(s):  
Youngdeuk Lee ◽  
Eunyoung Jo ◽  
Yeon-Ju Lee ◽  
Hansol Choi ◽  
Tae-Yang Eom ◽  
...  
Keyword(s):  
Marine Bacterium ◽  
Industrial Applications ◽  
Biochemical Properties ◽  
Carbohydrate Binding ◽  
Ionization Mass ◽  
Coding Region ◽  
Protein Activity ◽  
Amino Acid Similarity ◽  
Chromatography Analysis ◽  
Layer Chromatography

Abstract Background The degradation of agar by bacterial agarases has many commercial and academic applications. We recently identified a novel neoagarotriose-producing β-agarase, Gaa16B, in the marine bacterium Gilvimarinus agarilyticus JEA5. This is the first report to describe neoagarotriose production from β-agarase.Results The Gaa16B agarase, which belongs to the glycoside hydrolase 16 (GH16) family of β-agarases, shows less than 70.9% amino acid similarity with previously characterized agarases. The coding region of Gaa16B is 1800 bp long, encoding 600 amino acids, and exhibits features typical of agarases belonging to the GH16 family. A recombinant Gaa16B lacking the carbohydrate binding region (rGaa16Bc) was overexpressed in Escherichia coli and purified as a maltose-binding protein (MBP) fusion protein. Activity assays revealed the optimal temperature and pH of rGaa16Bc to be 55 °C and pH 6–7, respectively, and the protein was highly stable at 55 °C for 90 min. Additionally, rGaa16Bc activity was strongly enhanced (2.3-fold) in the presence of 2.5 mM MnCl2. The Km and Vmax of rGaa16Bc for agarose were 6.4 mg/ml and 953 U/mg, respectively. Thin layer chromatography analysis revealed that rGaa16Bc can hydrolyze agarose into neoagarotetraose, neoagarotriose, and neoagarobiose, and the production of neoagarotriose by rGaa16Bc was successfully validated by high-resolution electrospray ionization mass spectrometry.Conclusion The biochemical properties of Gaa16B and the results of the hydrolytic pattern analysis suggest that Gaa16B could be useful to produce functional neoagaro-oligosaccharides for industrial applications.

Magnetic particles for enzyme immobilization: a versatile support for ligand screening

2021 ◽  
pp. 114286
Author(s):  
Isabela Abreu Trindade Ximenes ◽  
Pamella Christina Ortega de Oliveira ◽  
Camila Anchau Wegermann ◽  
Marcela Cristina de Moraes
Keyword(s):  
Enzyme Immobilization ◽  
Magnetic Particles ◽  
Ligand Screening

scholarly journals DEVELOPMENT STATUS IN THE MEADOW OF NANOSTRUCTURE MAGNETIC DRUG DELIVERY SYSTEM AND ITS PROMISING APPLICATIONS

2017 ◽  
Vol 9 (12) ◽  
pp. 10
Author(s):  
Priyatama V. Powar
Keyword(s):  
Drug Delivery ◽  
Magnetic Nanoparticles ◽  
Magnetic Particles ◽  
Cell Function ◽  
Drug Loading ◽  
Control Cell ◽  
Chemical Properties ◽  
Biochemical Properties ◽  
Local Drug Delivery ◽  
Magnetic Drug Targeting

This article discusses about magnetic nanoparticles, their physico-chemical properties various applications in medicinal sectors and technology advancements. Superparamagnetic, high magnetic susceptibility, non-toxicity, biocompatibility and less Curie temperature are critical characteristics of magnetic nanoparticles which make them suitable for assorted medical applications. Now a day’s magnetic particles play significant role in diverse technological areas with potential applications in fields such as electronics, energy biomedicine and diagnosis. Magnetic nanoparticles have been a vivacious topic of extreme research for the last fifty years due to its top-down approaches. The prospective of magnetic nanoparticles stems from the fundamental characteristics of their magnetic cores collective with their drug loading capability, biochemical properties. This article review the modern advancement of magnetic nanoparticles for drug delivery, focusing chiefly on the impending applications like targeted drug delivery, bioseparation, ,magnetic resonance and cancer diagnosis, induction of hyperthermia, induction of hyperthermia, nanorobotic agents ,tissue engineering ,artificial muscle  ,magnetically activated polymers, controlled tissue assembly, control cell function, bone regeneration scaffold ,destruction of blood clots ,labeling stem cells with magnetic nanoparticles, implant-assisted intrathecal magnetic drug targeting, biodegradable magnetic nanocomposite stent, local drug delivery etc.

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