This study focused on improving activity and stability of industrial lipases by means of enzymatic immobilization onto spherelike bacterial cellulose (SBC) newly synthesized by a particular bacterial strain (Gluconacetobacter xylinus, JCM 9730). The results revealed that immobilizing lipases onto aldehyde-modified SBC with a size of 6.10±0.50mm could lead to two optimal hydrolytic activities of lipases under both acidic (pH 5) and alkaline conditions (pH 8), which was superior to free lipases that only exhibited an alkaline activity at pH 9. In addition, immobilizing lipases onto SBC could also achieve an improved active temperature below 30°C for lipases, which would help to reduce the energy consumption in the industrial production. Overall, this novel biomaterial has great potential as a green carrier for the immobilization of industrial lipases to enhance the recycling hydrolytic capability of oils and fats in various industrial divisions.
Keywords: Aldehyde-modification; Hydrolytic activity; Lipase immobilization; Spherelike bacterial cellulose.
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