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Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix

By Muhammad Asif Nawaz, Haneef Ur Rehman, Zainab Bibi, Afsheen Aman and Shah Ali Ul Qader


AbstractMaltase from Bacillus licheniformis KIBGE-IB4 was immobilized within calcium alginate beads using entrapment technique. Immobilized maltase showed maximum immobilization yield with 4% sodium alginate and 0.2M calcium chloride within 90.0min of curing time. Entrapment increases the enzyme–substrate reaction time and temperature from 5.0 to 10.0min and 45°C to 50°C, respectively as compared to its free counterpart. However, pH optima remained same for maltose hydrolysis. Diffusional limitation of substrate (maltose) caused a declined in Vmax of immobilized enzyme from 8411.0 to 4919.0Uml−1min−1 whereas, Km apparently increased from 1.71 to 3.17mMml−1. Immobilization also increased the stability of free maltase against a broad temperature range and enzyme retained 45% and 32% activity at 55°C and 60°C, respectively after 90.0min. Immobilized enzyme also exhibited recycling efficiency more than six cycles and retained 17% of its initial activity even after 6th cycles. Immobilized enzyme showed relatively better storage stability at 4°C and 30°C after 60.0 days as compared to free enzyme

Publisher: The Authors. Published by Elsevier B.V.
Year: 2015
DOI identifier: 10.1016/j.bbrep.2015.09.025
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