Abstract
In this study the immobilization of lipase in matrices produced with gelatin with different Bloom values and with the addition of plastifiers was investigated to evaluate the influence of the Bloom value, as well as the capacity of the plastifiers to maintain the enzyme immobilized and the immobilization yield. The results indicated the need for crosslinking of the matrices with glutaraldehyde due to the high solubility in water, explained by the amino acid profile, which confirms the solubility of gelatin. Mannitol showed greater efficiency in the lipase immobilization, since it led to more porous structures and more uniform pores. These structures were also influenced by the gelatin concentration; greater concentrations associated with intermediate concentrations of plastifier led to matrices with a greater immobilization yield (87.92%). The X-ray diffraction analysis revealed that the structure of the immobilization matrices was partially crystalline.
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