DNA directed immobilization enzyme on polyamidoamine tethered magnetic composites with high reusability and stability

2016 ◽  
Vol 4 (35) ◽  
pp. 5873-5882 ◽  
Author(s):  
Jiayi Song ◽  
Ping Su ◽  
Ye Yang ◽  
Ting Wang ◽  
Yi Yang
Keyword(s):  
Enzyme Immobilization ◽  
Immobilized Enzyme ◽  
Magnetic Composites ◽  
Immobilization Enzyme

A novel enzyme immobilization procedure was developed. The immobilized enzyme composites exhibited significantly improved digestion performance, excellent reusability, stability and dynamic reversible reproducibility.

Environmentally Friendly Preparation of Magnetic Composites Featuring Proteolytic Properties

INEOS OPEN ◽  
2020 ◽  
Author(s):  
N. A. Samoilova ◽  
Keyword(s):  
Enzyme Immobilization ◽  
Maleic Acid ◽  
Environmentally Friendly ◽  
Synthetic Polymer ◽  
Magnetic Composites ◽  
Interpolyelectrolyte Complex ◽  
Hydrolysis Rates ◽  
Poly Ethylene ◽  
Noncovalent Binding

The enzyme-containing magnetic composites are presented. The magnetic matrix for enzyme immobilization is obtained by sequential application of an amine-containing polysaccharide—chitosan and a synthetic polymer—poly(ethylene-alt-maleic acid) to the magnetite microparticles to form the interpolyelectrolyte complex shell. Then, the enzyme (trypsin) is immobilized by covalent or noncovalent binding. Thus, the suggested composites can be readily obtained in the environmentally friendly manner. The enzyme capacity of the resulting composites reaches 28.0–32.6 mg/g. The maximum hydrolysis rates of the H-Val-Leu-Lys-pNA substrate provided by these composites range within 0.60·10–7–0.77·10–7 M/min.

scholarly journals Peptide-Mediated Immobilization on Magnetoferritin for Enzyme Recycling

Nanomaterials ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 1558 ◽  
Author(s):  
Zhang ◽  
Dong ◽  
Zhou ◽  
Hu ◽  
Li ◽  
...  
Keyword(s):  
Enzyme Immobilization ◽  
Immobilized Enzyme ◽  
Coiled Coil ◽  
Retention Rates ◽  
Generate Functional ◽  
Retention Efficiency ◽  
Enzyme Recycling ◽  
Lysine Residues ◽  
Target Molecules ◽  
Good Retention

Ferritin possess favorable properties because its exterior and interior surface can be applied to generate functional nanomaterials, which make them possible for enzyme immobilization and recycling. Here, we report the noncovalent immobilization of a genetically modified β-glucosidase onto the outer surface of synthetic magnetoferritin through the electrostatic interaction of a heterodimeric coiled-coil protein formed by coils containing lysine residues (K-coils) and coils containing glutamic acid (E-coils). The immobilized enzyme was characterized, and its enzymatic properties were evaluated. Furthermore, reusability of immobilized enzyme was demonstrated in aqueous solution under an applied magnetic field. The results showed that magnetoferritin was successfully prepared and it was an excellent support for enzyme immobilization. After three times usages, the retention rates were 93.75%, 82.5%, and 56.25%, respectively, demonstrating that immobilized enzyme possessed good retention efficiency and could be used as potential carrier for other biomolecules. The strategy of enzyme immobilization developed in this work can be applied, in general, to many other target molecules.

scholarly journals PEMANFAATAN ZEOLIT ALAM SEBAGAI MEDIA PENDUKUNG AMOBILISASI ENZIM α-AMILASE

2015 ◽  
Vol 5 (1) ◽  
pp. 79
Author(s):  
Upita Septiani ◽  
Agrina Lisma
Keyword(s):  
Surface Morphology ◽  
Unit Activity ◽  
Incubation Time ◽  
Natural Zeolite ◽  
Immobilized Enzyme ◽  
Natural Zeolites ◽  
Optimum Temperature ◽  
Optimal Activity ◽  
Immobilization Enzyme ◽  
The Stability

 ABSTRACT The utilization of natural zeolite as supporting media of α-amylase enzyme has been done. Natural zeolite which is activated with 3M HCl can remove impurities in the surface natural zeolite, uncover and widen the pores of the zeolite and activate functional groups to interact with α-amylase enzyme in the process of immobilization enzyme process. The mass of activated natural zeolite which is used as a material immobilized to get the optimal activity of α-amylase enzyme was 0.3 gram. Based on the measurement result of optimization of α-amylase enzyme were obtained optimum temperature of 35 oC, pH 5.6 and incubation time of 35 minutes with 0.04845 units/mL of the unit activity. And for α-amylase immobilized enzyme will be stable at the optimum temperature of 50 oC, pH 5.6 and incubation time of 45 minutes with 0.030 units/mL of the unit activity. SEM-EDX pattern shows the differences in surface morphology between natural zeolite and activated natural zeolites which contain α-amylase enzyme. A mobilization technique can increase the stability utilized in a α-amylase enzyme. Keywords : Zeolite, amobilization, α-amylase enzyme

EFFECT OF REACTION CONDITIONS ON THE SYNTHESIS OF CYCLODEXTRIN (CD) BY USING IMMOBILIZED ENZYME

2018 ◽  
Vol 80 (3) ◽  
Author(s):  
Suhaily Suhaimi ◽  
Rohaida Che Man ◽  
Natassha Jamil ◽  
Zatul Iffah Mohd Arshad ◽  
Shalyda Md Shaarani ◽  
...  
Keyword(s):  
Enzyme Immobilization ◽  
Hollow Fiber ◽  
Immobilized Enzyme ◽  
Hollow Fiber Membrane ◽  
Potato Starch ◽  
Enzymatic Reaction ◽  
Cyclodextrin Glucanotransferase ◽  
Fiber Membrane ◽  
Reaction Conditions ◽  
Agricultural Industries

The production of cyclodextrin (CD) over the years has been increasing due to the numerous applications in industries such as in food, cosmetic, pharmaceutical and agricultural industries. However, cyclodextrin glucanotransferase (CGTase) which involved in the enzymatic reaction on the production of CD is unstable and easily denatured at extreme conditions resulted in low CD production. Hence, the enzyme immobilization technique is introduced to overcome these problems and subsequently increase the production of CD. In the present study, the CGTase was immobilized on hollow fiber membrane to increase the production of CD during the reaction. The effect of reaction conditions (types of starch, concentration of starch, temperature and pH) of the immobilized enzyme on the production of CD were investigated. Among the three types of starch tested, the soluble potato starch was the most suitable substrate for the production of CD with 4.13 mg/mL. In addition, by using 3% (w/v) of the soluble potato starch, the production of CD was 5.22 mg/mL . The optimal reaction temperature and pH were found to be at 40°C and pH 6 with 5.21 mg/mL and 4.62 mg/ml of CD, respectively. The immobilized enzyme exhibited a 1.3-3-fold increase in CD production compared to the free enzyme. Therefore, the hollow fiber membrane is suitable to be used as a support for enzyme immobilization with the high production of CD.

scholarly journals Rapid protein immobilization for thin film continuous flow biocatalysis

2016 ◽  
Vol 52 (66) ◽  
pp. 10159-10162 ◽  
Author(s):  
Joshua Britton ◽  
Colin L. Raston ◽  
Gregory A. Weiss
Keyword(s):  
Thin Film ◽  
Enzyme Activity ◽  
Enzyme Immobilization ◽  
Continuous Flow ◽  
Immobilized Enzyme ◽  
Protein Immobilization

Continuous flow biocatalysis gets a new spin. An efficient and general enzyme immobilization technique for vortex fluidic processing has been developed. The immobilized enzyme demonstrated no decrease in enzyme activity over 10 h in continuous flow with a >95% reduction in quantities of required reagents and enzymes.

scholarly journals Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

Catalysts ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 83 ◽  
Author(s):  
Gregory A. Ellis ◽  
Scott N. Dean ◽  
Scott A. Walper ◽  
Igor L. Medintz
Keyword(s):  
Quantum Dots ◽  
Gold Nanoparticles ◽  
Enzyme Immobilization ◽  
Large Scale ◽  
Immobilized Enzyme ◽  
Recent Literature ◽  
Immobilized Enzymes ◽  
Factors Affecting ◽  
Enzyme Conjugate ◽  
Underlying Mechanisms

Nanoparticle scaffolds can impart multiple benefits onto immobilized enzymes including enhanced stability, activity, and recoverability. The magnitude of these benefits is modulated by features inherent to the scaffold–enzyme conjugate, amongst which the size of the nanoscaffold itself can be critically important. In this review, we highlight the benefits of enzyme immobilization on nanoparticles and the factors affecting these benefits using quantum dots and gold nanoparticles as representative materials due to their maturity. We then review recent literature on the use of these scaffolds for enzyme immobilization and as a means to dissect the underlying mechanisms. Detailed analysis of the literature suggests that there is a “sweet-spot” for scaffold size and the ratio of immobilized enzyme to scaffold, with smaller scaffolds and lower enzyme:scaffold ratios generally providing higher enzymatic activities. We anticipate that ongoing studies of enzyme immobilization onto nanoscale scaffolds will continue to sharpen our understanding of what gives rise to beneficial characteristics and allow for the next important step, namely, that of translation to large-scale processes that exploit these properties.

scholarly journals Application of Immobilized Cholest-4-en-3-one Δ1-Dehydrogenase from Sterolibacterium denitrificans for Dehydrogenation of Steroids

2020 ◽  
Author(s):  
Mateusz Tataruch ◽  
Patrycja Wójcik ◽  
Agnieszka M. Wojtkiewicz ◽  
Katarzyna Zaczyk ◽  
Katarzyna Szymańska ◽  
...  
Keyword(s):  
Enzyme Immobilization ◽  
Electron Acceptor ◽  
Immobilized Enzyme ◽  
Specific Activity ◽  
Batch Reactor ◽  
Fed Batch ◽  
Immobilized Catalyst ◽  
Silica Supports ◽  
Dehydrogenase Enzyme ◽  
Final Yield

Cholest-4-en-3-one Δ1-dehydrogenase (AcmB) from Sterolibacterium denitrificans is successfully immobilized on 3-aminopropyltrimethoysilane functionalized MCF and SBA-15 silica supports using adsorption or covalently with glutaraldehyde or divinyl sulfone linkers. The best catalyst, AcmB on MCF linked covalently with glutaraldehyde, retains the specific activity of the homogenous enzyme while exhibiting a substantial increase of the operational stability. The immobilized enzyme was used continuously in the fed-batch reactor for 27 days, catalyzing 1,2-dehydrogenation of androst-4-en-3-one to androst-1,4-dien-3-one with a final yield of 29.9 mM (8.56 g/L) and 99% conversion. The possibility of reuse of the immobilized catalyst was also demonstrated and resulted with a doubling of the product amount compared to that in the reference homogenous reactor. Finally, it was shown that molecular oxygen from the air can efficiently be used as an electron acceptor either reoxidizing directly the enzyme or the reduced DCPIPH2. Keywords: 3-ketosteroid D1-dehydrogenase; KSTD; KSDH; AcmB; 1,2-dehydrogenation; cholest-4-en-3-one Δ1-dehydrogenase; enzyme immobilization, FAD-dependent enzymes; enzyme immobilization;

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