Performance of β-glucosidase immobilized on calcium alginate beads
Performance of immobilized β-glucosidase obtained from almonds (EC 3.2.1.21) on calcium alginate beads was studied by measuring the activity of the enzyme in terms of the generation of pnitrophenol from the hydrolysis of p-nitrophenyl-β-D-glucopyranoside (PNPG).The immobilized enzyme activity was c...
| Main Authors: | , , |
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| Format: | Conference or Workshop Item |
| Language: | English English |
| Published: |
2013
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| Subjects: | |
| Online Access: | http://irep.iium.edu.my/48525/ http://irep.iium.edu.my/48525/ http://irep.iium.edu.my/48525/1/ICBIOE-2013-PERFORMANCE_OF_%CE%B2-GLUCOSIDASE_IMMOBILIZED_ON_CALCIUM.pdf http://irep.iium.edu.my/48525/4/1175_Acceptance.pdf |
| Summary: | Performance of immobilized β-glucosidase obtained from almonds (EC 3.2.1.21) on calcium alginate beads was studied by measuring the activity of the enzyme in terms of the generation of pnitrophenol from the hydrolysis of p-nitrophenyl-β-D-glucopyranoside (PNPG).The immobilized
enzyme activity was compared with soluble enzyme and was found to decrease by 36.6% albeit with an increased operational stability in terms of easy recovery from the finished product, recurrent use and scale-up in various reactor configurations. The hydrolysis rate data exhibit Michaelis-Menten kinetics. The Michaelis constant were determined using Langmuir linearized plot which
obtained vmax and Km as 20.88 μmol/mL.min and 0.0125 mol/L respectively. However, the immobilized β-Glucosidase did not show a sufficiently good operational stability on reuse.
Keywords: Immobilized enzyme, enzyme activity, Michaelis-Menten kinetics, β-glucosidase, pnitrophenyl-
β-D-glucopyranoside (PNPG), alginate gel |
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