Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2075692 | Biocatalysis and Agricultural Biotechnology | 2012 | 6 Pages |
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. Km values of 1.46 and 0.38 mM, and vmax of 0.2487 and 0.2396 mol/L min, were obtained, respectively, for sucrose and inulin.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Agricultural and Biological Sciences (General)
Authors
Chaline C. Coghetto, Robison P. Scherer, Marceli F. Silva, Simone Golunski, Sibele B.C. Pergher, Débora de Oliveira, J. Vladimir Oliveira, Helen Treichel,