Journal
FOOD CHEMISTRY
Volume 373, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.131425
Keywords
Immobilization; alpha-Amylase , Cloisite 30B; Support activation
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This study successfully immobilized alpha-amylase from Bacillus subtilis on three different supports using adsorption and covalent immobilization methods. The immobilized enzymes showed improved thermal and storage stability, higher specific activity, and good catalytic performance in starch hydrolysis compared to free enzymes.
In this paper, alpha-amylase from Bacillus subtilis was successfully immobilized on three supports. First, alpha-amylase was immobilized on cloisite 30B via the adsorption method. Then cloisite 30B was activated with tosyl chloride and epichlorohydrin. These activated supports were used for covalent immobilization of alpha-amylase, and their enzymatic activities were effectively tested in the starch hydrolysis. The results demonstrated that the specific activity of alpha-amylase immobilized on cloisite 30B was 2.39 +/- 0.03, for alpha-amylase immobilized on activated cloisite 30B with epichlorohydrin was 1.96 +/- 0.05 and for alpha-amylase immobilized on activated cloisite 30B with tosyl chloride was 2.17 +/- 0.05 U mg(- 1). The optimum pH for the activity of free alpha-amylase was 7, but for alpha-amylase immobilized on cloisite 30B was 8, and for alpha-amylase immobilized on activated supports was 7.5. The immobilized enzymes had better thermal resistance and storage stability than free alpha-amylase, and they also showed excellent reusability.
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