Abstract
A solution of 10 g/L of sodium alginate (Satialgine® types used [Sanofi trademark]: SG800® and S1100® with manuronic/guluronic ratio of 0.5 and 1.2, respectively) containing invertase (0.08 g of protein/L) was dropped into 0.1 M CaCl2 solution buffered at pH 4.0, 7.0, or 8.0. The beads were left to harden in CaCl2 solution for 24 h. The high immobilization yield of 60% occurred with SG800 at pH8.0. The activity of soluble and insoluble invertase was measured against pH (2.8–8.0), sucrose concentration (4.5–45 mM), and temperature (30–60°C). Both forms presented an optimum pH of 4.6. However, the soluble invertase was stable at the overall pH interval studied, whereas insoluble invertase lost 30% of its original activity at pH > 5.0. At temperatures above 40°C, the insoluble form was more stable than the soluble one. The kinetic constants and activation energies (E a ) for free invertase were K M =41.2 mM, V max=0.10 mg of TRS/(min · mL), and E a 28 kJ/mol for entrapped invertase they were (K M ) ap =7.2 mM, (V max) ap =0.060 mg of TRS/(min · mL), and (E a )ap=24 kJ/mol.
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Arruda, L.M.O., Vitolo, M. Characterization of invertase entrapped into calcium alginate beads. Appl Biochem Biotechnol 81, 23–33 (1999). https://doi.org/10.1385/ABAB:81:1:23
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DOI: https://doi.org/10.1385/ABAB:81:1:23