Journal of Advances in Food Science & Technology
6(3): 146–157, 2019
ISSN: 2454-4213
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2019
The thermostability enhancement of specified nanomagnetic combi-CLEAs of α-amylase and maltogenic
amylase was evaluated by assessment of kinetic parameters, temperature dependence, enzyme half-life, thermal
inactivation energy barriers (Ea), and thermodynamic parameters in a storage thermostability approach at 55–
95° C for 120 minutes. The Michaelis constant (Ka(in)) values of NM-Combi-CLEAs was diminished within 1.5
folds while The catalytic efficiency was enhanced near 1.32 after CLEAs formation. The half-lives of the
fabricated nano-bio catalyst increased about 2.5 folds at 95º C. Besides, Ea(in)
of the native combined enzymes was appended from 44.75 into 54.76 (KJ.mol-1
and ΔH* increased from 41.69 to 51.70 (KJ.mol) while, ΔS*
decreased 28.2% after immobilization. The NM-Combi-CLEAs conserved 80.4% of its original activity after ten
cycles. Hence, the advanced technique for NM-Combi-CLEAs production is introduced as an effective and
secured method to fabrication of recyclable immobilized enzyme also, resolving of mass transfer limitation
difficulties and ease in enzyme handling.
amylase was evaluated by assessment of kinetic parameters, temperature dependence, enzyme half-life, thermal
inactivation energy barriers (Ea), and thermodynamic parameters in a storage thermostability approach at 55–
95° C for 120 minutes. The Michaelis constant (Ka(in)) values of NM-Combi-CLEAs was diminished within 1.5
folds while The catalytic efficiency was enhanced near 1.32 after CLEAs formation. The half-lives of the
fabricated nano-bio catalyst increased about 2.5 folds at 95º C. Besides, Ea(in)
of the native combined enzymes was appended from 44.75 into 54.76 (KJ.mol-1
and ΔH* increased from 41.69 to 51.70 (KJ.mol) while, ΔS*
decreased 28.2% after immobilization. The NM-Combi-CLEAs conserved 80.4% of its original activity after ten
cycles. Hence, the advanced technique for NM-Combi-CLEAs production is introduced as an effective and
secured method to fabrication of recyclable immobilized enzyme also, resolving of mass transfer limitation
difficulties and ease in enzyme handling.
