RESUMO
This study investigated the impact of a support matrix and active group on the support to the nutritional properties of orange juice after juice clarification. Pectinase was immobilized on chitosan and aminated silica supports, activated with genipin or glutaraldehyde, and applied for juice clarification. The effects on various juice properties, including reducing sugars, total soluble solids, vitamin C, and phenolic compounds, juice color, and pH, were evaluated. The results revealed that the immobilization on chitosan activated using genipin resulted in the highest biocatalyst activity (1211.21 U·g-1). The juice treatments using the biocatalysts led to turbidity reduction in the juice (up to 90%), with the highest reductions observed in treatments involving immobilized enzyme on chitosan. Importantly, the enzymatic treatments preserved the natural sugar content, total soluble solids, and pH of the juice. Color differences between treated and raw juice samples were especially relevant for those treated using enzymes, with significant differences in L* and b*, showing loss of yellow vivid color. Analysis of phenolic compounds and vitamin C showed no significant alterations after the enzymatic treatment of the raw juice. According to our results, the clarification of orange juice using immobilized enzymes can be a compromise in turbidity reduction and color reduction to maintain juice quality.
RESUMO
This study aimed to modify the porosity of chitosan beads using Na2CO3 as a porogen agent and to crosslink them with genipin for the immobilization of ß-galactosidase from Aspergillus oryzae. Immobilization was performed under four different pH conditions (4.5, 6.0, 7.5, and 9.0), resulting in biocatalysts named B4, B6, B7, and B9, respectively. The immobilized enzymes were characterized for immobilization parameters and stability, including thermal, pH, storage, and operational stability. The optimal conditions for the support were determined as 50 mM Na2CO3. The biocatalyst exhibited nearly 100 % retention of initial activity after 5 h of incubation at different pH conditions and showed improved thermal stability compared to the free enzyme across all pH conditions. After 50 cycles of lactose hydrolysis, all biocatalysts retained at least 71 % of their initial activity, with B6 retaining nearly 100 %. Scanning electron microscopy revealed structural modifications, particularly in B4, leading to weakened support structure after reuse. Continuous lactose hydrolysis showed increased productivity from 41.3 to 48.1 g L-1 h-1 for B6, with 78.1 % retention of initial capacity. All biocatalysts retained >95 % activity when stored at 4 °C for 20 weeks, highlighting their suitability for enzyme immobilization in continuous and discontinuous bioprocesses.
