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Interactions in bovine serum albumin–calcium alginate gel systems
Authors:S Neiser  K I Draget  O Smidsrd
Affiliation:Norwegian Biopolymer Laboratory (NOBIPOL), Department of Biotechnology, Norwegian University of Science and Technology (NTNU), Sem Sælands Vei 6-8, N-7491 Trondheim, Norway
Abstract:Young's modulus of heat-denatured gels of calcium alginate and bovine serum albumin (BSA) was determined and compared to the modulus of BSA gels containing sodium alginate and to pure BSA gels. Ionic strength, pH, and calcium concentration were varied. The BSA/Ca-alginate gels were either prepared with -glucono-δ-lactone (GDL) and CaCO3 to induce alginate gelation before the gelation of BSA, or by soaking heat-denatured BSA/Na-alginate gels in a CaCl2 solution. BSA/Ca-alginate gels were stronger than BSA/Na-alginate gels at all conditions, and stronger than pure BSA gels up to higher pH values and up to somewhat higher ionic strengths than BSA/Na-alginate gels. The strength of BSA/Ca-alginate gels was highly dependent on the strength of the alginate gel. This was shown by variation of the calcium concentration and by soaking the gels in EDTA, NaCl, and CaCl2 solutions. When BSA/Na-alginate or BSA/Ca-alginate gels prepared at optimum conditions were soaked in solutions of higher ionic strength or pH, no reduction in gel strength was observed. Consequently, they were much stronger than gels that were prepared directly at high pH or ionic strength. The results may suggest that the alginate network in a BSA/Ca-alginate gel increases the effectiveness of electrostatic BSA-alginate cross-links or entanglements. However, other explanations are also possible.
Keywords:Protein–  polysaccharide interactions  Gel–  gel interactions  Alginate  BSA
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