scholarly journals Protein separation and purification. Small and large scales.

1988 ◽  
Vol 46 (11) ◽  
pp. 1014-1024 ◽  
Author(s):  
Shojiro YAMAZAKI ◽  
Sigeyasu KOBAYASHI
Keyword(s):  
Protein Separation ◽  
Separation And Purification

scholarly journals Influence of Salts on the Adsorption of Lysozyme on a Mixed-Mode Resin

2021 ◽  
Vol 2021 ◽  
pp. 1-11
Author(s):  
Jannette Kreusser ◽  
Fabian Jirasek ◽  
Hans Hasse
Keyword(s):  
Sodium Chloride ◽  
Ionic Strength ◽  
Ammonium Sulfate ◽  
Protein Separation ◽  
Mixed Mode ◽  
Hydrophobic Interaction Chromatography ◽  
Exchange Chromatography ◽  
Separation And Purification ◽  
Adsorption Equilibria ◽  
Wide Range

Mixed-mode chromatography (MMC), which combines features of ion exchange chromatography (IEC) and hydrophobic interaction chromatography (HIC), is an interesting method for protein separation and purification. The design of MMC processes is challenging as adsorption equilibria are influenced by many parameters, including ionic strength and the presence of different salts in solution. Systematic studies on the influence of those parameters in MMC are rare. Therefore, in the present work, the influence of four salts, namely, sodium chloride, sodium sulfate, ammonium chloride, and ammonium sulfate, on the adsorption of lysozyme on the mixed-mode resin Toyopearl MX-Trp-650M at pH 7.0 and 25°C was studied systematically in equilibrium adsorption experiments for ionic strengths between 0 mM and 3000 mM. For all salts, a noticeable adsorption strength was observed over the entire range of studied ionic strengths. An exponential decay of the loading of the resin with increasing ionic strength was found until approx. 1000 mM. For higher ionic strengths, the loading was found to be practically independent of the ionic strength. At constant ionic strength, the highest lysozyme loadings were observed for ammonium sulfate, the lowest for sodium chloride. A mathematical model was developed that correctly describes the influence of the ionic strength as well as the influence of the studied salts. The model is the first that enables the prediction of adsorption isotherms of proteins on mixed-mode resins in a wide range of technically interesting conditions, accounting for the influence of the ionic strength and four salts of practical relevance.

Protein Separation and Purification

Biotechnology ◽  
2008 ◽  
pp. 617-642 ◽  
Author(s):  
Jan-Christer Janson ◽  
Lars Rydén
Keyword(s):  
Protein Separation ◽  
Separation And Purification

scholarly journals Specific purification of a single protein from a cell broth mixture using molecularly imprinted membranes for the biopharmaceutical industry

RSC Advances ◽  
2019 ◽  
Vol 9 (41) ◽  
pp. 23425-23434 ◽  
Author(s):  
Wenyuan Xie ◽  
Honglei Wang ◽  
Yen Wah Tong ◽  
Niranjani Sankarakumar ◽  
Ming Yin ◽  
...  
Keyword(s):  
Protein Separation ◽  
Biopharmaceutical Industry ◽  
Separation And Purification ◽  
Surface Imprinting ◽  
Molecularly Imprinted ◽  
Single Protein ◽  
A Cell ◽  
Molecularly Imprinted Membrane ◽  
Imprinted Membrane

A surface imprinting method is presented herein for the development of a highly selective yet highly permeable molecularly imprinted membrane for protein separation and purification.

scholarly journals Design and synthesis of a novel nanocomposite based on magnetic dopamine nanoparticles for purification of α-amylase from the bovine milk

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Reza Eivazzadeh-Keihan ◽  
Haniyeh Dogari ◽  
Farnoush Ahmadpour ◽  
Hooman Aghamirza Moghim Aliabadi ◽  
Fateme Radinekiyan ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Protein Separation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Bovine Milk ◽  
Diglycidyl Ether ◽  
Magnetic Nanocomposites ◽  
Separation And Purification ◽  
X Ray ◽  
Design And Synthesis

AbstractIn this paper, a novel nanocomposite based on magnetic nanoparticles decorated by dopamine were reported. Three modified magnetic nanocomposites by dopamine were offered with different type of linkers. The mentioned magnetic nanocomposites were applied to separate α-amylase protein from fresh bovine milk. All of the magnetic nanocomposites were characterized and investigated by using Fourier-transform infrared spectroscopy, energy-dispersive X-ray spectroscopy, field-emission scanning microscope, X-ray diffraction pattern, and vibrating-sample magnetometer analyses. To investigate the purifying application, sodium dodecyl sulfate polyacrylamide gel electrophoresis, one-dimensional isoelectric focusing gel electrophoresis, and alpha-amylase activity assay were employed. With paying attention to factors such as yield of purification and concentration of separated protein by each of magnetic nanocomposite, it could be concluded that the length of linkers played an important role in α-amylase protein separation. According to the results, the best separation and purification of α-amylase protein with 49.83% recovery and 40.11-fold purification efficiency was related to longest length linker, 1,4-butanediol diglycidyl ether, because of considerable conjugation with nanocomposite. Also, docking calculation has shown that the binding energy is − 1.697 kcal/mol and ΔG = − 6.844 kcal/mol which result that the interaction process between dopamine and α-amylase protein is spontaneous.

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