A simple entrapment of glucoamylase into LentiKats® as an efficient catalyst for maltodextrin hydrolysis

The glucoamylase from Aspergillus niger was immobilized into a poly(vinylalcohol) hydrogel lens-shaped capsules LentiKats®. Immobilization broadened the pH optimum of the enzyme. The KM of glucoamylase increased after immobilization (approximately 1.5 times on maltose), which reflected the decrease in affinity of enzyme for its substrate. Immobilized enzyme retained excellent long-term operational stability for both, batch and continuous mode of hydrolysis. Specific enzymatic activity of the immobilized enzyme (0.67 g g−1 h−1) was constant for 63 days of continuous operation at 45 °C.