Amylase from Lactobacillus cellobiosus D-39 isolated from vegetable wastes: characteristics of immobilized enzyme and whole cell

Cells and partially purified α-amylase (EC 3.2.1.1) of the producer strain, Lactobacillus cellobiosus D-39 were immobilized on acrylamide gel. The enzyme showed marked improvement in operational stability. Both immobilized cells and enzyme were stable for a long period and no appreciable loss activity was detected on keeping at 4°C for 4 months. The amylase activity of immobilized cells and enzyme attained maximum at pH 6.0 and 7.6 respectively and at temperature 60°C for both cases. The effects of various solvents, detergent and metal ions were tested; Triton X-100 gave maximum stimulation of the enzyme activity of immobilized cells whereas metal ions exhibited no such enhancement for either of immobilized cells or enzyme.