Immobilization of Cellulolytic Enzymes in Accurel® MP1000

Cellulases are a class of enzymes great industrial interest that present several strategic applications. However, the high cost enzyme production, coupled with instabilities and complexities proteins required for hydrolytic processes, still limits their use in protocols. Therefore, immobilization may be an essential tool to overcome these issues. The work aimed evaluate cellulolytic commercial cocktail Celluclast® 1.5 L comparison produced from wild strain Trichoderma harzianum I14-12 Accurel® MP1000. Among variables studied were temperature at 40 °C, ionic strength 50 mM, 72 h immobilization, 15 m·L −1 generated biocatalysts efficiencies (87% ACC-Celluclast biocatalyst 95% ACC-ThI1412 biocatalyst), retention activity, specific activities support CMCase (DNS method), FPase (filter paper method) β-glucosidase (p-nitrophenyl-β-D-glucopyranoside method). Presenting lower protein concentration (0.32 m·L−1) than preparation (45 m·L−1), ACC-ThI1412-derived immobilized showed thermal stability temperatures higher 60 maintaining more 90% residual FPase, CMCase, β-glucosidase. In contrast, commercial-free presented maximum catalytic activity only °C. Moreover, difference molecular weight between component extract was responsible different hydrophobic lodging interactions on support, generating robust competitive biocatalyst.