Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571

 Chaline C. Coghetto^a, Robison P. Scherer^a, Marceli F. Silva^a, Simone Golunski^a, Sibele B.C. Pergher^b,  Débora de Oliveira^{c, 1}, J. Vladimir Oliveira^{c, 1},Helen Treichel^{d, e}

                                                                                                                         

Abstract

The objective of this study was to investigate the process of immobilization of inulinases using natural montmorillonite as inorganic support. The enzyme to buffer ratio of 3:10 and 10 min of immobilization led to the highest specific activity, 375.07 U/mg protein. The immobilized inulinase kept its activity after 1968 h under storage at low temperatures and after 456–1826 h at high temperatures. The pH value of 3.5 led to the highest specific activity. K_m values of 1.46 and 0.38 mM, and v_max of 0.2487 and 0.2396 mol/L min, were obtained, respectively, for sucrose and inulin.

Source:Visit Here

Keywords

• Kluyveromyces marxianus NRRL Y-7571; Inulinase; Inorganic support; Immobilization