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Biomimetic Mineralization of the Alginate/Gelatin/Calcium Oxalate Matrix for Immobilization of Pectinase: Influence of Matrix on the Pectinolytic Activity

Cindy Elena Bustamante-Vargas, Débora de Oliveira, Eunice Valduga, Luciana Dornelles Venquiaruto, Natalia Paroul, Geciane Toniazzo Backes, Rogério Marcos Dallago
Applied biochemistry and biotechnology 2016 v.179 no.6 pp. 1060-1072
Aspergillus niger, biomimetics, calcium oxalate, encapsulation, enzyme activity, gelatin, immobilized enzymes, mineralization, pH, pectins, polygalacturonase, storage quality, storage time, temperature, textile industry
Pectinases catalyze the degradation of pectic substances and are used in several processes, mainly in food and textile industries. In this study, a biomimetic matrix of alginate/gelatin/calcium oxalate (AGOCa) was synthesized for the in situ immobilization via encapsulation of crude pectinase from Aspergillus niger ATCC 9642, obtaining an immobilization efficiency of about 61.7 %. To determine the performance of AGOCa matrix, this was compared to control matrices of alginate/calcium oxalate (AOxal) and alginate/water (ACa). By the evaluation of pH and temperature effects on the enzyme activity, it was observed an increase on pectinolytic activity for both three tested matrices with an increase on pH and temperature. The kinetic parameters for pectinase immobilized in the three matrices were determined using citric pectin as substrate. Values of K ₘ of 0.003, 0.0013, and 0.0022 g mL⁻¹ and V ₘₐₓ of 3.85, 4.32, and 3.17 μmol min⁻¹ g⁻¹ for AGOCa, AOxal, and ACa matrices were obtained, respectively. After 33 days of storage, the pectinase immobilized in the three different matrices kept its initial activity, but that immobilized in AGOCa presented high stability to the storage with a relative activity of about 160 %. The enzyme immobilized in AGOCa, AOxal, and ACa could be used in 10, 8, and 7 cycles, respectively, keeping 40 % of its initial activity.