Inulin Hydrolysis by Immobilized Inulinase on Functionalized Magnetic Nanoparticles Using Soy Protein Isolate and Bovine Serum Albumin

2018 ◽  
Vol 65 (6) ◽  
pp. 771-779 ◽  
Author(s):  
Homa Torabizadeh ◽  
Mohaddeseh Mikani ◽  
Reza Rahmanian
Drug Research ◽  
2020 ◽  
Vol 70 (05) ◽  
pp. 183-187
Author(s):  
Mohammad Shariq ◽  
Saba Parveen ◽  
Arshiya Shamim ◽  
Farogh Ahsan ◽  
Poonam Kushwaha ◽  
...  

AbstractPast few decades have emerged as the era of nanotechnology worldwide leading to an extensive research in pharmaceutical science as well as other fields. Nanoformulations have shown a promising future in therapeutics and theronostics. Protein based nanoformulations attracting attention in research as it can be used as therapeutics as well as carrier. Carrier based protein nanoformulatios are capable of accommodating range of therapeutics such as dyes, drugs, contrast agents and inorganic nanoclusters makings its application vast. The nano size of formulation enables it to reach the desired places by some modification. This paper reviewed the various protein based nanoformulation. Human serum albumin, Bovine serum albumin, soy protein isolate, phycocyanin, casein, bromelein, collagen and sericin based nanoformulations are briefly discussed. Various limitations of these proteins can be diminished by developing it in nano form and emerged as promising candidate as carrier as well as therapeutics in drug delivery advancements.


2011 ◽  
Vol 10 (04n05) ◽  
pp. 919-923 ◽  
Author(s):  
S. CHANDRA ◽  
N. NITHYAMATHI ◽  
P. SELVAMANI ◽  
D. BAHADUR

Iron oxide nanoparticles were prepared and functionalized by succinamide based dendrimer. The resultant particles were characterized by XRD, VSM, and FTIR spectroscopy. The results indicate that the dendrimers has effectively functionalized the magnetite nanoparticles which remain dispersive and exhibited super-paramagnetism with a magnetization value of 33.2 emu/g in a field of 2T. Mean particle size as calculated from the AFM was found to be ~ 23 nm. Bovine serum albumin was immobilized on the magnetic nanoparticles as was confirmed by the FTIR results.


Molecules ◽  
2018 ◽  
Vol 23 (11) ◽  
pp. 2993 ◽  
Author(s):  
José Guimarães ◽  
Raquel Giordano ◽  
Roberto Fernandez-Lafuente ◽  
Paulo Tardioli

The preparation of highly porous magnetic crosslinked aggregates (pm-CLEA) of porcine pancreas lipase (PPL) is reported. Some strategies to improve the volumetric activity of the immobilized biocatalyst were evaluated, such as treatment of PPL with enzyme surface-modifying agents (polyethyleneimine or dodecyl aldehyde), co-aggregation with protein co-feeders (bovine serum albumin and/or soy protein), use of silica magnetic nanoparticles functionalized with amino groups (SMNPs) as separation aid, and starch as pore-making agent. The combination of enzyme surface modification with dodecyl aldehyde, co-aggregation with SMNPs and soy protein, in the presence of 0.8% starch (followed by hydrolysis of the starch with α-amylase), yielded CLEAs expressing high activity (immobilization yield around 100% and recovered activity around 80%), high effectiveness factor (approximately 65% of the equivalent free enzyme activity) and high stability at 40 °C and pH 8.0, i.e., PPL CLEAs co-aggregated with SMNPs/bovine serum albumin or SMNPs/soy protein retained 80% and 50% activity after 10 h incubation, respectively, while free PPL was fully inactivated after 2 h. Besides, highly porous magnetic CLEAs co-aggregated with soy protein and magnetic nanoparticles (pm-SP-CLEAs) showed good performance and reusability in the hydrolysis of tributyrin for five 4h-batches.


2017 ◽  
Vol 53 (54) ◽  
pp. 7635-7637 ◽  
Author(s):  
Daily Rodriguez-Padrón ◽  
Alain R. Puente-Santiago ◽  
Alina M. Balu ◽  
Antonio A. Romero ◽  
Rafael Luque

A solventless mechanochemical approach was employed to obtain a bioconjugate (BSA–DA–Fe2O3) based on bovine serum albumin (BSA) and dopamine (DA) coated iron oxide magnetic nanoparticles. BSA molecules retained their native-like structure after the mechanochemical synthesis.


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