| Description |
1 online resource |
| Contents |
Front cover -- Half title -- Full title -- Copyright -- Contents -- Contributors -- Preface -- The journey in understanding interactions of salts and solvents with proteins continues! -- Chapter 1 -- Three phase partitioning: some reminiscences, some science -- 1.1 The origin of the tpp method -- 1.2 How does TPP work? -- 1.3 Inhibition of enzyme activity by t-BuOH -- 1.4 Enhanced activity -- 1.5 Other molecules -- 1.6 TPP doesn't work in all cases -- References -- Chapter 2 -- How and why we happen to use three phase partitioning in areas other than protein purification -- 2.1 TPP for purification of proteins/enzymes -- 2.2 TPP used for edible oil extraction -- 2.3 TPP of polysaccharides -- 2.4 TPP of microbial cells -- 2.5 Isolation and purification of low molecular weight compounds -- 2.6 Conclusion -- References -- Chapter 3 -- Fundamental aspects of protein isolation and purification -- 3.1 Introduction -- 3.2 Fusion tags and protein solubility -- 3.3 Cell lysis -- 3.3.1 Mechanical procedures -- 3.4 Non-mechanical procedures -- 3.4.1 Physical methods -- 3.4.2 Chemical methods -- 3.5 Protein precipitation -- 3.5.1 Salting-in and salting out -- 3.5.2 Trichloroacetic acid (TCA) and other procedures -- 3.5.3 Protein precipitation by organic solvents -- 3.5.4 Metal-chelate protein precipitation -- 3.6 Affinity precipitation and immunoprecipitation -- 3.7 Protein purification -- 3.7.1 Dialysis -- 3.7.2 Size exclusion chromatography (SEC) -- 3.7.3 Ion exchange (IEC) chromatography -- 3.7.4 Hydrophobic chromatography/ hydrophobic interaction chromatography (HIC) -- 3.7.5 Affinity interaction chromatography (AIC) -- 3.7.6 Metal chelate chromatography -- 3.8 Conclusions and outlooks -- References |
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Chapter 4 -- The multiple facets of three-phase partitioning in the purification, concentration, yield and activity of enzy ... -- 4.1 Introduction -- 4.2 TPP as a rapid single step procedure to isolate and concentrate proteins -- 4.3 TPP concentrates proteins by decreasing the volume of water -- 4.4 TPP concentrates individual proteins by removing unwanted proteins -- 4.5 TPP preserves and increases enzyme activity -- 4.6 Explanations for TPP preserving and increasing enzyme activity -- 4.7 Purification and/or refolding of denatured enzymes with TPP -- 4.8 TPP purification of recombinant HIS-Tag fusion proteins or metal binding proteins -- 4.9 TPP purification of proteins with affinity ligands -- 4.10 Ultrasound assisted TPP to isolate proteins, oils and polysaccharides -- 4.11 Microwave assisted TPP -- 4.12 Versatility of TPP. separating DNA, carbohydrates and oils and two-step TPP protocols -- 4.13 Conclusion -- References -- Chapter 5 -- Enzymes recovery by three phase partitioning -- 5.1 Introduction -- 5.2 Overview of the studies and conditions of use of three phase partitioning and its variants for the recovery of enzymes -- 5.3 Three phase partitioning for the recovery of glycosidases -- 5.4 Three phase partitioning for the recovery of proteases -- 5.5 Three phase partitioning for the recovery of oxidoreductases -- 5.6 Three phase partitioning for the recovery of lipases -- 5.7 Three phase partitioning for the recovery of other hydrolases -- 5.8 Conclusion -- References -- Chapter 6 -- Emulsion gel formation in three phase partitioning -- 6.1 Introduction -- 6.2 The mechanism of TPP -- 6.2.1 The effect of ammonium sulfate and tert -butanol -- 6.2.2 Protein adsorption at the interface -- 6.2.3 The shear rheological properties of interfacial protein layer |
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6.2.4 The role of emulsion stability in the formation of gel as the middle phase -- 6.3 Conclusion -- References -- Chapter 7 -- Three-phase partitioning (TPP) of proteases from parasites, plants, tissue and bacteria for enhanced activity -- 7.1 Why we are interested in proteases -- 7.2 Three-phase partitioning as a protease purification tool -- 7.3 Conditions considered during optimization of tpp -- 7.3.1 Choice of organic solvent and its ratio to crude extract -- 7.3.2 Choice of salt and concentration of salt used for tpp -- 7.3.3 Effect of pH and pI on tpp -- 7.3.4 Effect of temperature on tpp -- 7.3.5 Parasite proteases as drug and diagnostic targets -- 7.3.6 Plant proteases for milk-clotting in cheese making -- 7.3.7 Bacterial proteases for laundry detergents and anti-inflammatory agents -- 7.3.8 Fish and bacterial proteases in food biotechnology -- 7.3.9 Protease inhibitors -- 7.4 Effect of tpp on protease structure and activity -- 7.5 Conclusions -- References -- Chapter 8 -- Three phase partitioning of plant peroxidases -- 8.1 Peroxidases -- 8.2 Sources and functions of peroxidases -- 8.2.1 Mammalian peroxidases -- 8.2.2 Microbial peroxidases -- 8.2.3 Plant peroxidases -- 8.3 Biotechnological applications of plant peroxidases -- 8.3.1 Pulp and paper industry -- 8.3.2 Bioremediation of phenolic compounds -- 8.3.3 Decolourization of industrial dyes -- 8.3.4 Biosensor -- 8.3.5 Analysis and diagnostic kits -- 8.3.6 Hair dyeing -- 8.4 Three phase partitioning system -- 8.4.1 Effect of salt on TPP -- 8.4.2 Effect of t-butanol on TPP -- 8.4.3 Effect of temperature on TPP -- 8.4.4 Effect of pH on TPP -- 8.5 TPP as an emerging technique for plant peroxidase purification -- 8.6 Conclusion -- References |
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Chapter 9 -- Macro-(affinity ligand) facilitated three phase partitioning Converting TPP into an affinity based process -- 9.1 Introduction -- 9.1.1 Importance of affinity interactions in protein purification -- 9.2 Water soluble polymers and smart polymers -- 9.2.1 Carrageenans -- 9.2.2 Alginates -- 9.2.3 Chitosan -- 9.2.4 Eudragits -- 9.3 Smart biocatalysts -- 9.4 MLFTPP -- 9.5 Conclusion/future perspectives -- References -- Chapter 10 -- Applications of three phase partitioning and macro-(affinity ligand) facilitated three phase partitioning in ... -- 10.1 Introduction -- 10.1.1 Protein structure -- 10.1.2 General strategies for protein refolding -- 10.1.3 Smart polymers and protein refolding -- 10.1.4 Refolding by TPP -- 10.1.5 Refolding by MLFTPP -- 10.1.6 Structural changes in proteins due to TPP -- 10.1.7 Some other underexploited applications of TPP treatment of proteins/cells -- 10.2 Conclusion -- References -- Chapter 11 -- Three phase partitioning-based strategies for highly efficient separation of bioactive polysaccharides from n ... -- 11.1 Introduction -- 11.2 Factors affecting the TPP process for extraction of PSs -- 11.2.1 Ammonium sulfate -- 11.2.2 t -butanol -- 11.2.3 pH -- 11.2.4 Temperature -- 11.2.5 Time -- 11.3 Process intensification of TPP system for PSs extraction -- 11.3.1 Enzyme-assisted TPP -- 11.3.2 US-assisted TPP -- 11.3.3 US-synergized TPP -- 11.4 TPP combined with downstream techniques -- 11.5 TPP separation influencing the properties of PSs -- 11.6 Conclusions -- Acknowledgements -- References -- Chapter 12 -- Technologies for oil extraction from oilseeds and oleaginous microbes -- 12.1 Introduction -- 12.1.1 Oilseeds and nutritional security -- 12.2 Importance of oil and lipid extraction -- 12.3 Green solvents and techniques for oil and lipid extraction |
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12.3.1 Selection of extraction solvent -- 12.4 Green solvents for oil/ lipid extraction -- 12.4.1 Bio-derived solvents -- 12.4.2 Supercritical fluid technology -- 12.4.3 Ionic liquids and deep eutectic solvents -- 12.4.4 Switchable solvents -- 12.5 Conventional and green extraction techniques for oil/ lipid extraction -- 12.5.1 Oil/Expeller pressing -- 12.5.2 Bead milling -- 12.5.3 Enzyme assisted oil/lipid extraction from oilseeds/biomass -- 12.5.4 Microwave treatment -- 12.5.5 Ultrasound assisted extraction (UAE) -- 12.6 Conclusion -- Author's contributions -- Competing interest -- Acknowledgements -- References -- Chapter 13 -- Three phase partitioning (TPP) as an extraction technique for oleaginous materials -- 13.1 Introduction -- 13.2 Conventional extraction techniques for oleaginous material -- 13.3 Mechanism of extraction using TPP -- 13.4 Advantages of TPP -- 13.5 Factors affecting TPP -- 13.5.1 Salt -- 13.5.2 Extraction solvent -- 13.5.3 pH -- 13.5.4 Temperature -- 13.5.5 Extraction time -- 13.6 Hyphenated TPP-techniques -- 13.6.1 Enzyme assisted TPP (EATPP) -- 13.6.2 Ultrasound assisted TPP (UATPP) -- 13.6.3 Microwave assisted TPP (MATPP) -- 13.6.4 High-pressure homogenization assisted TPP (HPHTPP) -- 13.7 Challenges and future perspectives -- References -- Chapter 14 -- Intensification of extraction of biomolecules using three-phase partitioning -- 14.1 Introduction -- 14.1.1 History -- 14.1.2 TPP process and mechanism -- 14.2 Key factors affecting the TPP method -- 14.2.1 Salt concentration -- 14.2.2 Crude extract to alcohol ratio -- 14.2.3 pH -- 14.2.4 Temperature -- 14.3 Advanced TPP processes -- 14.3.1 Two-step TPP -- 14.3.2 Macro-affinity ligand-facilitated three-phase partitioning (MLFTPP) -- 14.3.3 Ionic liquid three-phase partitioning (ILTPP) |
| Notes |
Print version record |
| Subject |
Phase partition.
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Biomolecules -- Separation
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Biomolecules -- Separation
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Phase partition
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| Form |
Electronic book
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| Author |
Gupta, Munishwar Nath
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Roy, Ipsita
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| ISBN |
9780323859035 |
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0323859038 |
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