Reverse Micelle Liquid-Liquid Extraction of Bovine Serum Albumin and Lysozyme

2012 ◽  
pp. 07-11 ◽  
Author(s):  
Siti Hamidah Mohd Setapar ◽  
Siti Norazimah Mohamad Aziz ◽  
Constantine Joanne
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Reverse Micelle ◽  
Bovine Serum ◽  
Surfactant Concentration ◽  
Extraction Process ◽  
Factors Affecting ◽  
Forward Transfer ◽  
Protein Bovine Serum Albumin ◽  
Reverse Micelle Extraction

Reverse micelle extraction by using Sodium bis (2-ethylhexyl) Suffoccinate (AOT) of protein bovine serum albumin (BSA) and lysozyme was investigated in this research. Study of factors affecting the surfactant concentration and pH of aqueous for both forward and backward extraction process was performed in the research. The BSA concentrations were characterized by using the UV- spectrophotometer at wavelength, λ = 280 nm. The result indicated that the extraction percentage of lysozyme was higher than BSA in forward transfer for both parameters; however BSA demonstrated a better extraction performance in backward extraction process. The maximum lysozyme extracted in the forward extraction process was at 60 mM of surfactant concentration while for BSA was 100 mM since BSA is a bulky molecule and the size is larger than of lysozyme. Pengekstrakan misel terbalik dengan menggunakan Sodium bis (2-ethylhexyl) Suffoccinate (AOT) untuk protein bovine serum albumin (BSA) dan lysozyme disiasat dalam penyelidikan ini. Kajian tentang faktor-faktor yang mempengaruhi kepekatan surfaktan dan pH akueus untuk proses pengekstrakan hadapan dan ke belakang telah dijalankan. Kepekatan BSA telah dicirikan dengan menggunakan spektrofotometer UV pada panjang gelombang, λ = 280 nm. Hasil kajian telah menunjukkan bahawa peratusan pengekstrakan lysozyme adalah lebih tinggi daripada BSA bagi pemindahan ke hadapan untuk kedua-dua parameter, namun begitu BSA menunjukkan prestasi pengekstrakan yang lebih baik di dalam proses pengekstrakan kebelakang. Jumlah maksimum lysozyme yang diekstrak di dalam proses pengekstrakan ke hadapan adalah 60 mM kepekatan surfaktan manakala bagi BSA adalah 100 mM disebabkan BSA adalah molekul yang sangat besar dan ia mempunyai saiz yang lebih besar berbanding daripada lysozyme.

Effect of H-bonding effect on reverse micelle extraction of bovine serum albumin

2019 ◽  
Vol 41 (14) ◽  
pp. 2169-2175 ◽  
Author(s):  
Mengyuan Ma ◽  
Jian Song ◽  
Lichen Bai ◽  
Guan Wei ◽  
Jianfeng Dai ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Reverse Micelle ◽  
Bovine Serum ◽  
Bonding Effect ◽  
Reverse Micelle Extraction

scholarly journals Reverse Micelle Liquid-Liquid Extraction of a Pharmaceutical Product

2012 ◽  
Vol 545 ◽  
pp. 240-244 ◽  
Author(s):  
Siti Hamidah Mohd-Setapar ◽  
Siti Norazimah Mohamad-Aziz ◽  
N.H. Harun ◽  
S.H. Hussin
Keyword(s):  
Aqueous Solution ◽  
Aqueous Phase ◽  
Reverse Micelle ◽  
Surfactant Concentration ◽  
Protein Extraction ◽  
Biological Activities ◽  
Extraction Process ◽  
Pharmaceutical Product ◽  
Penicillin G ◽  
Reverse Micelle Extraction

Reverse micelle extraction has received considerable attention in recent years due to its ability to selectively solubilise solutes from an aqueous phase, and in the case of biomolecules to maintain their biological activities. The apparent success of research on protein extraction from the aqueous phase using reverse micelle provides motivation to study the solubilisation of antibiotic. The objective of this study is to investigate the extraction of antibiotic (penicillin G is chosen as model antibiotic) from aqueous solution (forward extraction) and from the reverse micelle to a new aqueous solution (backward extraction). Sodium di(2-ethylhexyl)sulfosuccinate (AOT) is chosen as the surfactant and isooctane as the organic solvent. The UV-Vis spectrophotometer is used to determine the mass of penicillin G in solution after the extraction process. The extraction is expected to be influenced by the initial penicillin G concentration, the salt type and concentration in the aqueous phase, pH, and surfactant concentration. It is expected that as penicillin is an interfacially active compound that will interacts with AOT surfactant, the interfacial association will be dependent on both pH and surfactant concentration.

Influence of Terahertz Radiation of Various Ranges on Molecule Conformation of Bovine Serum Albumin

2010 ◽  
Vol 5 (4) ◽  
pp. 182-185
Author(s):  
Angelina V. Kapralova ◽  
Aleksandr S. Pogodin
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Radiation Power ◽  
Uv Spectrophotometry ◽  
Absorption Bands ◽  
Conformation Changes ◽  
Protein Molecules ◽  
Molecule Conformation ◽  
Protein Bovine Serum Albumin

We investigated the influence of THz laser radiation of frequencies of 1.15 THz and 3.68 THz and radiation power of about 10 Mw on protein (bovine serum albumin). Using UV spectrophotometry, we revealed increase in the optical density of irradiated samples of bovine serum albumin at the characteristic absorption bands, which is evidence of conformation changes in protein molecules

scholarly journals The Glass Transition Behavior of the Globular Protein Bovine Serum Albumin

2003 ◽  
Vol 85 (6) ◽  
pp. 3943-3950 ◽  
Author(s):  
Geoffrey J. Brownsey ◽  
Timothy R. Noel ◽  
Roger Parker ◽  
Stephen G. Ring
Keyword(s):  
Glass Transition ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Globular Protein ◽  
Transition Behavior ◽  
Protein Bovine Serum Albumin

scholarly journals Anomalous protein kinetics on low-fouling surfaces

2020 ◽  
Vol 22 (9) ◽  
pp. 5264-5271
Author(s):  
Mohammadhasan Hedayati ◽  
Matt J. Kipper ◽  
Diego Krapf
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Single Molecule ◽  
Bovine Serum ◽  
Time Distribution ◽  
Dwell Time ◽  
Protein Kinetics ◽  
Single Molecule Tracking ◽  
Heavy Tailed ◽  
Protein Bovine Serum Albumin

Single-molecule tracking reveals the protein bovine serum albumin exhibits anomalous kinetics with a heavy-tailed dwell time distribution on PEG surfaces. This effect is shown to be caused by the ability of the protein to oligomerize in solution.

scholarly journals KONJUGASI ANHIDRAT KlORAMFENIKOL-PROTEIN (CAP-BSA DAN CAP-KLH) UNTUK PRODUKSI IgG DARI SERUM KELINCI

2011 ◽  
Vol 1 (2) ◽  
pp. 23-31
Author(s):  
Musyirna Rahmah Nst ◽  
Tri Budhi Murdiati
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Immunosorbent Assay ◽  
Bovine Serum ◽  
Keyhole Limpet Hemocyanin ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein Bovine Serum Albumin

 Dalam pengembangan metoda analisis residu antibiotik pada produk pangan hewani secara immunokimia telah dilakukan sintesis imunogen kloramfenikol (CAP) dengan protein Bovine Serum Albumin (BSA) dan Keyhole Limpet Hemocyanin (KLH) dengan metoda konjugasi mixed anhidrad. Hasil sintesis digunakan untuk produksi antibodi.Antigen dan antibodi yang dihasilkan dijadikan prangkat analisis residu antibiotik dengan Competitive Enzyme Linked Immunosorbent Assay (ELISA kompetitif). Hasil penelitian menunjukkan bahwa metoda konjugasi mixed anhidrad pada preparasi imunogen dengan jumlah CAP yang terkonjugasi ke grup amino bebas dari molekul protein BSA (CAP-BSA) adalah 18 unit dan ke protein KLH (CAP-KLH) adalah 782 unit. Antibodi poliklonal CAP-BSA dan CAP-KLH yang diproduksi dengan rata-rata kandungan IgG CAP-BSA 2,07 mg/ml dan IgG CAP-KLH 2,21 mg/ml.

scholarly journals Doxorubicin hinders DNA condensation promoted by the protein bovine serum albumin (BSA)

Biopolymers ◽  
2017 ◽  
Vol 107 (12) ◽  
pp. e23071
Author(s):  
C. H. M. Lima ◽  
H. M. C. de Paula ◽  
L. H. M. da Silva ◽  
M. S. Rocha
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Dna Condensation ◽  
Protein Bovine Serum Albumin
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