Laboratory 5: Purification of Alkaline Phosphatase from E. coli
Introduction to Alkaline Phosphatase
Enzyme Overview: Alkaline phosphatases are non-specific enzymes that catalyze hydrolysis of phosphate monoesters to release inorganic phosphate.
Reaction: R-O-PO3H- + H2O → R-OH + H2PO4.
Classification: Orthophosphoric monoester phosphohydrolases (EC 3.1.3.1), active at basic pH.
Sources: Present in bacteria, fungi, and higher animals but absent in plants.
E. coli Specifics: Major alkaline phosphatase from E. coli is a bipartite enzyme (86,000 Da, composed of two subunits), requiring both for activity.
Physical Parameters:
pH Optimum: 8.0
Isoelectric Point (pI): 4.5
Cofactors: Contains two zinc atoms per enzyme.
Function: Extracts inorganic phosphate (Pi) from phosphorylated compounds
Hydrolysis occurs in the periplasmic space, where it is bound by Pi-binding protein and transferred to the Pst system for cytoplasmic transport.
Purification Strategy:
Exploits heat stability of alkaline phosphatase to selectively denature and remove other soluble proteins.
Utilizes ammonium sulfate precipitation and ion-exchange chromatography on DEAE-cellulose for further purification.
Week 1 - Preparation and Enzyme Extraction
Materials Needed:
Hydrated E. coli K-12 cells, lysozyme, DNase I, EDTA, MgSO4, dialysis tubing, and buffers.
Protocol:
- Prepare E. coli Cells:
- Hydrate cells in sucrose for 48-72 hours at 4°C after washing and pelleting.
- Cell Lysis (all steps at room temperature except post-lysis):
- Add lysozyme to hydrolyze cell wall.
- Add DNase to prevent viscosity from liberated DNA.
- Use EDTA for chelation of divalent cations (Ca2+, Mg2+) aiding in cell lysis.
- Add MgSO4 to prevent prolonged EDTA exposure to alkaline phosphatase.
- Centrifugation (4°C):
- Centrifuge at 9,500 x g to separate supernatant from pellet (Stage 1 Enzyme).
- Dialysis:
- Prepare dialysis bag with ice-cold retentate to remove impurities and small molecules.
Week 2 - Heat Denaturation and Ammonium Sulfate Precipitation
Materials Needed:
Ammonium sulfate, 1N NaOH, dialysis buffer, and others as required.
Heat Treatment:
- Remove dialysis bag and squeeze out retentate into test tube.
- Heat at 80°C for 15 min and cool rapidly.
- Centrifuge and collect supernatant (Stage 2 Enzyme).
- Ammonium Sulfate Precipitation:
- Calculate ammonium sulfate: 0.603 g/mL for 90% saturation.
- Add crystals slowly while stirring gently to avoid denaturation.
- Correct acidity with NaOH, allow precipitation.
- Centrifuge and discard supernatant, resuspend pellet in dialysis buffer.
Week 3 - Ion-Exchange Chromatography
Anion-Exchange Setup:
Pack DEAE cellulose, equilibrated with low-ionic-strength buffer (Buffer A).
Chromatography Steps:
- Apply Stage 3 Enzyme to column.
- Rinse with Buffer A and elute with Buffer B (higher NaCl) to collect enzyme fractions.
- Assay fractions for alkaline phosphatase activity (yellow color indicates presence).
- Pool active fractions for Stage 4 Enzyme.
Activity Assays and Protein Determination
Alkaline Phosphatase Activity Assay:
Monitor breakdown of pNPP to pNP spectrophotometrically at 410 nm.
Set up reaction mixtures and measure absorbance.
Perform enzyme blanks to correct for substrate degradation.
Protein Determination (Bradford Method):
- Prepare BSA standards of known concentration.
- Mix samples with Bradford reagent and measure at 595 nm.
- Construct standard curve for protein quantification.
Calculations and Data Analysis
- Calculate absorptivity from pNP solution absorption.
- Determine enzyme activity rate, specific activity, recovery percentages, and fold purification.
- Present findings in a purification summary table and appropriate graphs comparing enzyme activity across purification stages.
References
- Garen, A. & Levinthal, C. (1960) Alkaline Phosphatase Purification Study.
- Neu, H.C. & Heppel, L.A. (1965) Enzyme Release Techniques.
- Schlesinger, M.J. & Barrett, K. (1965) Alkaline Phosphatase in E. coli Study.