Antoine Bouchoux, Pierre-Emerson Cayemitte, Julien Jardin, Geneviève Gésan-Guiziou, and Bernard Cabane

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1 Biophysical Journal, Volume 96 Supplementary Material Casein Micelle Dispersions under Osmotic Stress Antoine Bouchoux, Pierre-Emerson Cayemitte, Julien Jardin, Geneviève Gésan-Guiziou, and Bernard Cabane

2 Supporting Information Casein Micelle Dispersions under Osmotic Stress Antoine Bouchoux*,#, Pierre-Emerson Cayemitte*,#, Julien Jardin*,#, Geneviève Gésan- Guiziou*,#, and Bernard Cabane * INRA, UMR1253, STLO, F Rennes, France # Agrocampus Rennes, UMR1253, F Rennes, France PMMH, CNRS UMR 7636, ESPCI, 10 rue Vauquelin, F Paris cedex 05, France 1. Materials Urea-polyacrylamide gel electrophoresis Samples were analysed by urea-polyacrylamide gel electrophoresis (urea-page) using 18% (w/v) acrylamide gels comprising 4.33 M urea and M Tris-HCl buffer, ph 8.8, according to the method of Andrews et al. (1). A Mini Protean II gel system (BioRad, Ivry-sur Seine, France) was used. NPC dispersions were diluted between 1/5 and 1/20 in distilled water and 1 ml of the diluted dispersions were denatured with 0.5 ml M Tris-HCl buffer, ph 6.8, containing, 3.3 M urea, 5% (v/v) b-mercaptoethanol, 10% (v/v) glycerol and 0.05% (w/v) bromophenol blue for 1 h at 37 C. 20 L of sample were loaded into each lane. Electrophoresis was continued for 2.5 h at 20 C and 200 V constant voltage, using 0.5 M Tris-HCl, ph 8.3, containing M glycine as the electrode buffer. The bands were revealed with R250 Coomassie blue staining. Liquid chromatography-mass spectrometry (LC-MS) Before chromatographic separation and analysis by MS, peptide enrichment and partial elimination of trichloroacetic acid (TCA), salts and lactose from the samples were carried out using Waters Sep-Pack Vac cartridges (Waters, Mildford, MA, USA) containing 200 mg of trifunctional C18 in 3 ml volume as packing material. The cartridge was conditioned with 10 volumes of deionised water, rinsed with 3 volumes of acetonitrile and with 10 volumes of deionised water containing 0.1% (w/w) TFA. Then 2 ml of sample was loaded on to the cartridge. The loaded cartridge was washed with 20 ml of deionised water and peptides were eluted with 3 volumes of pure acetonitrile. Deionised water was added to samples (1:1) and mixtures were lyophilized. The freeze-dried powder was dissolved in 1 ml of deionised water. Analytical reverse phase high-performance liquid chromatography (RP-HPLC) was carried out using an Agilent HP1100 chromatographic system (Agilent Technologies, Massy, France). Separation was performed on a Vydac 214TP5215 C4 column (5 µm particle size, 2.1 mm i.d 150 mm length). The elution was carried out at 40 C and at a flow rate of 0.25 ml/min by a binary gradient with acetonitrile as an organic modifier. Solvent A contained 0.106% (v/v) trifluoroacetic acid (TFA) in deionised water and solvent B contained 80% (v/v) acetonitrile and 0.1% (v/v) TFA in deionised water. Samples were analyzed through on-line LC-MS. The column was initially equilibrated with 3% of solvent B. 50µL of samples were injected into the system and eluted by a linear gradient from 3% to 80% of solvent B in 46 minutes. Fragments were detected both by UV 1

3 absorbance at 214nm and mass spectrometry. Throughout on-line coupling, splitting of chromatographic flow was achieved by a low dead volume T-junction with 85% of the flow directed to the UV detector and 15% to the mass spectrometer. This split yielded a perfect superposition between UV and Total Ion Current (TIC) detections. The mass spectrometer (API III+ SCIEX, Thornhill, Ontario, Canada) comprises a triple quadrupole equipped with an atmospheric pressure electrospray ionisation source. Analysis was carried out in positive detection mode. A 75 m sprayer was set at 4800 V to generate multiply-charged ions and orifice voltage (OR) was set to 100V. The nebulizer gas (Air) pressure was set around 0.5 MPa and the curtain gas (N 2 ) flow was set to 1.2 L/min. The instrument mass-to-charge (m/z) scale was calibrated with polypropylene glycols. Each scan was acquired over the range of m/z values from 500 to 2400 using a step size of 0.3 Da and a dwell time of 0.5 ms. Masses of fragments observed were calculated from multiply charged ions using the software BioMultiview (MDS Sciex). 2. Results Extent of casein degradation during osmotic stress experiments Fig. 1 gives an overall view of casein degradation with time during osmotic stress experiments at osmotic pressures below 5000 Pa Pa 5000 Pa c 1d 7d 14d 7d -caseins -casein s1 -casein FIGURE 1 Urea-PAGE electrophoretograms for NPC dispersions in UF permeate after 1 day (1d); 7 days (7d); 14 days (14d) of osmotic compression at 20 C. As a control (c), the initial NPC dispersion before compression, at 25 g/l of caseins, is also shown. The osmotic pressures applied by the stressing solutions are indicated at the top. -caseins are casein fragments from Da to Da that are formed by the proteolysis of -casein (by plasmin for instance, see (2)). These fragments were already present in fresh NPC dispersions in small relative proportion as compared to "intact" -casein and s1 -casein. As incubation time increases, the relative proportion of -casein over -casein increases so that the degradation is significant after 14 days of dialysis at 1500 Pa. However, after 7 days, the extent of proteolysis is still low for 1500 Pa and 5000 Pa. Based on these qualitative observations, osmotic compression were limited to 7 days at low osmotic pressures ( < 5000 Pa), i.e. for casein concentrations at equilibrium below 150 g/l. This duration is a good 2

4 compromise between a relatively low degradation and a sufficient time for the thermodynamic equilibrium to be reached. At higher pressures ( 8000 Pa), virtually no degradation occurred at dialysis times comprised between 10 and 49 days and identical results (same casein concentrations) were obtained from dispersions at thermodynamic equilibrium but with different ages. Low molar mass peptides identified in NPC dispersions Following a protocol developed by Gaucheron et al. (3), the low molar mass peptides present in a NPC dispersion after 7 days of incubation at 20 C was identified by LC-MS. As casein degradation was significant only for osmotic pressures below 5000 Pa (previous section), a 25 g/l casein dispersion ( 00 Pa) was chosen for these experiments. After 7 days of incubation at 20 C, the casein micelles were removed by ultracentrifugation at g for 2 h at 20 C in a Sorvall Discovery 90 SE ultracentrifuge (Hitachi, USA). Remaining proteins was then removed by precipitation in 12% (w/w) TCA and filtration on Whatman No. 40 filter paper. Fig. 2 gives the RP-HPLC profile obtained from this sample. 100 s Relative Absorbance (%) Time (min) FIGURE 2 RP-HPLC profiles of the peptide fraction present in a 25 g/l casein dispersion of NPC in UF permeate after 7 days of incubation at 20 C. Eluted peaks were detected by UV absorbance at 214 nm. Peak numbers refer to Table 1. The peak labelled "s" is the signal of the solvent, i.e. UF permeate (the RP-HPLC profile of UF permeate alone gave a unique peak of the same intensity at this elution time). It includes different species (small organics, modified serum proteins, etc.) that were not identified by MS due to their low ionisation efficiency. The heights of all other peaks are measured as percentages of peak "s" absorbance. Fig. 2 shows a group of sharp peaks located at elution 3

5 times between 27 and 32 minutes. These peaks are from small peptides in the range of Da. The exact molar masses of the main contributors to the total signal are given in Table 1. The amount of each species relative to the total peptide content was estimated from the RP-HPLC profile in Fig. 2. TABLE 1 Identification of the major peptides present in a 25 g/l casein dispersion of NPC in UF permeate after 7 days of incubation at 20 C. Identification numbers are indicated in Fig. 2. Identification number Molar mass (Da) Estimated relative amount (%) and or The same type of analysis was done with PEG stressing solutions after 7 days of dialysis equilibrium with the NPC dispersions. An example is given in Fig. 3 for a 2000 Pa stressing solution. 100 s Relative Absorbance (%) Time (min) FIGURE 3 RP-HPLC profiles of a 2000 Pa stressing solution after 7 days of dialysis against a NPC dispersion at 20 C. 4

6 This spectrum only shows peak "s", that is the signal of UF permeate. The relative absence of any peptide peaks in this spectrum indicates that the peptides that are released by the NPC dispersion are retained within the dialysis bag, and therefore contribute to the osmotic pressure of the dispersion. 3. References 1. Andrews, A. T Proteinases in normal bovine milk and their action on caseins. J. Dairy Res. 50: Eigel, W. N., C. J. Hofmann, B. A. Chibber, J. M. Tomich, T. W. Keenan, and E. T. Mertz Plasmin-mediated proteolysis of casein in bovine milk. Proc. Nat. Acad. Sci. USA. 76: Gaucheron, F., D. Molle, V. Briard, and J. Leonil Identification of low molar mass peptides released during sterilization of milk. Int. Dairy J. 9:

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