02211nas a2200229 4500008004100000022001400041245011500055210006900170260007900239300001400318490000800332520136100340653002701701653002001728653001901748653002101767653002101788653001401809100002001823700001701843856012101860 2013 eng d a0273-228900aChemical modification of ethyl cellulose-based highly porous membrane for the purification of immunoglobulin G0 aChemical modification of ethyl cellulosebased highly porous memb a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcFEB a1026-10380 v1693 a

The chemical modification of developed ethyl cellulose-based membrane was carried out to make it suitable for bioseparation. The different reagents were used for the modification of membrane to couple protein A (PA) to study the purification of immunoglobulin G (IgG) from blood. The chemical modification was carried out using relatively simple and mild reaction conditions. The attenuated total reflectance Fourier transform infrared analysis of chemically modified membrane showed new peak at 1,596.06 and 1,716.49 cm(-1). The scanning electron microscopy of PA-coupled membrane, which was used for IgG purification showed open pores and 950 +/- 21.5 LMH (L m(-2) h(-1)) operational flux at 0.5-bar out pressure. The flux of unmodified membrane was 1,746 +/- 18.5 LMH at 0.5-bar out pressure. The equilibrium adsorption concentration (318.5 +/- 5.9 mu g cm(-2)) was obtained at 3 h. The adsorption character of PA-coupled membrane was consistent with the Langmuir adsorption model and the non-specific binding was 67.08 +/- 1.3 mu g cm(-2). The sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis showed similar purification pattern for purified IgG from human serum and commercial preparation of IgG. All the results have suggested a high potential of PA-coupled ethyl cellulose-based membrane for large-scale purification of IgG.

10aAffinity bioseparation10aEthyl cellulose10aGlutaraldehyde10aImmunoglobulin G10aPolyethylenimine10aProtein A1 aAdikane, H., V.1 aIyer, G., J. uhttps://library.ncl.res.in/content/chemical-modification-ethyl-cellulose-based-highly-porous-membrane-purification-002022nas a2200253 4500008004100000022001400041245010800055210006900163260000900232300001100241490000700252520118300259653002301442653002901465653001501494653002601509653001401535100002001549700001701569700001901586700002001605700002001625856012301645 2020 eng d a0734-975000aEngineering staphylococcal protein A for high-throughput affinity purification of monoclonal antibodies0 aEngineering staphylococcal protein A for highthroughput affinity cNOV  a1076320 v443 a

Protein A chromatography is one of the most widely used purification steps in the manufacturing of the various classes of recombinant and non-recombinant antibodies. Due to the higher cost, lower binding capacity, and limited life cycle of Protein A ligand, this affinity-based purification step is often one of the most significant contributors to the cost of manufacturing of monoclonal antibody (mAb) products. In the last decade, there has been significant progress in improving the Protein A chromatography throughput by designing new engineered Staphylococcal Protein A (SPA) variants with higher dynamic binding capacity, considerable alkaline tolerance, and mild acidic elution pH. This review aims at summarizing the various protein engineering approaches used for improving the throughput of the Protein A-based affinity purification of various immunoglobulins. With biopharmaceutical producers operating under ever-increasing pressure towards reducing the cost of manufacturing, these advances in engineered protein A variants will help in processing larger cell culture volumes with high throughput and thereby significantly lower the cost of raw materials.

10aAlkaline tolerance10aDynamic binding capacity10aElution pH10aMonoclonal antibodies10aProtein A1 aAmritkar, Vinod1 aAdat, Satish1 aTejwani, Vijay1 aRathore, Anurag1 aBhambure, Rahul uhttps://library.ncl.res.in/content/engineering-staphylococcal-protein-high-throughput-affinity-purification-monoclonal02210nas a2200265 4500008004100000022001400041245011100055210006900166260000800235300001400243490000700257520132700264653001501591653003001606653002601636653001401662653001501676100002601691700002001717700002501737700001801762700001901780700001701799856012801816 2022 eng d a0268-257500aMechanistic modeling of continuous capture step purification of biosimilar monoclonal antibody therapeutic0 aMechanistic modeling of continuous capture step purification of  cSEP a2404-24190 v973 a

{BACKGROUND Continuous multicolumn Protein A chromatography offers various advantages for capture stage purification of monoclonal antibody therapeutics, like higher productivity and resin capacity utilization, lower buffer consumption, small footprint, etc. Due to the complexity of the continuous process, experimental optimization is time-consuming and cost-intensive. This investigation proposes a hybrid process development approach integrating experimental and mechanistic modeling for time- and cost-effective development and optimization of continuous Protein A affinity chromatography. RESULTS Productivity and capacity utilization of the continuous CaptureSMB process under varying operating conditions were predicted using the Chromatography Analysis and Design Toolkit (CADET) framework and validated with experimental results. Effects of critical process parameters like feed concentration (c(0)), loading breakthrough (s) and residence time (RT) on productivity and capacity utilization were evaluated. Model predictions were validated using the experimental results proving the reliability and feasibility of the modeling approach. At 15.00 +/- 0.20 mg mL(-1) feed model mAb concentration, the model-based approach predicted the best performance giving 27.56 g L-1 h(-1) productivity (RT = 2 min

10aCaptureSMB10acontinuous chromatography10aMathematical modeling10aProtein A10asimulation1 aDeulgaonkar, Prashant1 aBhambure, Rahul1 aPrasad, Bhaskarjyoti1 aMishra, Ashok1 aTiwari, Sanjay1 aMody, Rustom uhttps://library.ncl.res.in/content/mechanistic-modeling-continuous-capture-step-purification-biosimilar-monoclonal-antibody