• Produktbild: Methods of Testing Protein Functionality
  • Produktbild: Methods of Testing Protein Functionality
  • Produktbild: Methods of Testing Protein Functionality

Methods of Testing Protein Functionality

Fr. 137.00

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Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

17.09.2011

Herausgeber

George M. Hall

Verlag

Springer Us

Seitenzahl

266

Maße (L/B/H)

23.5/15.5/1.6 cm

Gewicht

429 g

Auflage

Softcover reprint of the original 1st edition 1996

Sprache

Englisch

ISBN

978-1-4612-8517-5

Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

17.09.2011

Herausgeber

George M. Hall

Verlag

Springer Us

Seitenzahl

266

Maße (L/B/H)

23.5/15.5/1.6 cm

Gewicht

429 g

Auflage

Softcover reprint of the original 1st edition 1996

Sprache

Englisch

ISBN

978-1-4612-8517-5

Herstelleradresse

Springer-Verlag KG
Sachsenplatz 4-6
1201 Wien
AT

Email: GPSR Kontakt

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  • Produktbild: Methods of Testing Protein Functionality
  • Produktbild: Methods of Testing Protein Functionality
  • Produktbild: Methods of Testing Protein Functionality
  • 1 Basic concepts.- 1.1 Introduction.- 1.2 Sources of functional proteins.- 1.3 Factors affecting protein functional properties.- 1.3.1 Intrinsic factors.- 1.3.2 Processing treatments.- 1.3.3 Application conditions.- 1.4 Conclusions.- References.- 2 Solubility.- 2.1 Introduction.- 2.1.1 Solubility definition and theory.- 2.1.2 Factors that influence protein solubility.- 2.1.3 Definition of terms used for protein solubility.- 2.2 Review of methods for measuring solubility.- 2.2.1 Protein solubilization.- 2.2.2 Separating the undissolved protein (clarification).- 2.2.3 Methods for measuring protein concentration.- 2.3 Protocols for methods.- 2.3.1 Protein dispersion and solubilization.- 2.3.2 Clarification and phase separation.- 2.3.3 Determination of protein concentration.- Acknowledgement.- References.- 3 Viscosity.- 3.1 Introduction.- 3.2 What is viscosity?.- 3.2.1 Factors which affect viscosity.- 3.2.2 Non-linear viscosity.- 3.2.3 Viscosity of suspensions.- 3.3 Viscometers for measuring shear viscosity.- 3.3.1 Rotational viscometers.- 3.3.2 Other techniques.- 3.4 Protocols for measuring viscosity.- 3.4.1 Shear viscosity.- 3.5 Summary.- References.- List of manufacturers.- 4 Gelation.- 4.1 Introduction.- 4.2 Scientific basis of protein gelation.- 4.2.1 Definition of gelation and types of gels.- 4.2.2 Conformational change of proteins.- 4.2.3 Chemical forces involved in gelation phenomena.- 4.2.4 Rheological aspects.- 4.3 Methods of testing gel properties of proteins.- 4.3.1 Determination of heating temperature.- 4.3.2 Detection and analysis of the early stage of gelation.- 4.3.3 Detection of the sol-gel transition (determination of gelling points).- 4.3.4 Effects of pH and ionic strength.- 4.3.5 Spectroscopic analysis of protein structural change through the gelation process.- 4.3.6 Contribution of chemical bonding to the gelation process.- 4.3.7 Rheological properties of gels.- 4.3.8 Microscopic observation.- 4.4 Protocol for testing the gelling ability of proteins.- 4.4.1 Information on samples.- 4.4.2 Solubilization or dispersion.- 4.4.3 Determination of the denaturation temperature.- 4.4.4 Determination of the gellingpoint.- 4.4.5 The effects of pH, ionic strength and other conditions.- 4.4.6 Evaluation of gel properties.- Acknowledgement.- References.- 5 Foam formation and stability.- 5.1 Scientific background.- 5.1.1 Introduction.- 5.1.2 Principles of protein foam formation.- 5.1.3 Principles of protein foam stability.- 5.1.4 Improving protein foam production.- 5.2 Review.- 5.2.1 Methods of foam generation.- 5.2.2 Methods of protein foam measurement.- 5.2.3 Analysis.- 5.3 Protocols.- 5.3.1 Pure proteins.- 5.3.2 Crude protein extracts.- 5.3.3 Real systems.- References.- 6 Emulsions.- 6.1 Introduction.- 6.2 Emulsion definition.- 6.3 Forces involved with emulsions.- 6.3.1 Attractive forces.- 6.3.2 Repulsive forces.- 6.3.3 Steric forces.- 6.3.4 Depletion forces.- 6.4 Emulsion stability.- 6.4.1 Creaming and drainage.- 6.4.2 Flocculation.- 6.4.3 Coalescence.- 6.4.4 Phase inversion.- 6.5 Stabilizers and emulsifiers.- 6.5.1 Interfacial properties.- 6.5.2 Types of protein.- 6.5.3 Protein modification.- 6.5.4 Mixed biopolymers.- 6.6 Forming emulsions.- 6.6.1 Procedure for the laboratory scale production of an emulsion.- 6.7 Methods of measuring emulsification properties.- 6.7.1 Measurement of droplet size.- 6.7.2 Emulsifying activity (EA).- 6.7.3 Emulsion capacity (EC).- 6.7.4 Oil phase volume (OPV).- 6.7.5 Emulsion stability (ES).- 6.8 Other useful parameters when assessing emulsion properties.- 6.8.1 Surface hydrophobicity.- 6.8.2 Viscosity.- 6.9 Conclusions.- References.- 7 Determining water and fat holding.- 7.1 Introduction.- 7.2 Scientific basis.- 7.3 Waterholding.- 7.3.1 Press method.- 7.3.2 High-speed centrifugation.- 7.3.3 Low-speed centrifugation.- 7.3.4 Capillary suction methods.- 7.3.5 Absorption/rehydration methods.- 7.3.6 Optical methods.- 7.3.7 Microscopy.- 7.3.8 Special instruments (NMR, DSC, X-ray).- 7.4 Fat holding.- 7.4.1 Review of methods.- 7.4.2 Cooking/processing.- 7.4.3 High-speed centrifugation.- 7.4.4 Low-speed centrifugation.- 7.4.5 Emulsification test.- 7.4.6 Solvent extraction.- 7.4.7 Optical methods.- 7.4.8 Microscopy.- 7.4.9 Special instruments.- 7.5 Development of a test protocol.- 7.6 Conclusions.- References.- 8 Measurement of surface hydrophobicity.- 8.1 Introduction.- 8.1.1 Definition of hydrophobicity.- 8.1.2 Protein structure and surface hydrophobicity.- 8.1.3 Quantitative structure-activity relationships.- 8.2 Measurement of surface hydrophobicity.- 8.2.1 Hydrophobicity scales for proteins.- 8.2.2 Empirical scales.- 8.2.3 Comparison of relative hydrophobicity values of proteins.- 8.2.4 Prospect of measurement of protein surface hydrophobicity: exposure of hydrophobic side chains.- 8.3 Experimental protocols.- 8.3.1 Probe spectrofluorometry.- 8.3.2 Hydrophobic-interaction chromatography.- 8.3.3 Contact angle determination.- 8.3.4 SDS binding capacity.- 8.3.5 Triglyceride binding capacity.- 8.3.6 Hydrophobic partition.- References.