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Effect of Mg2+ and Al3+ Ions on Thermodynamic and Physiochemical Properties of Aspergillus niger Invertases

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In the present study, we reported for the first time the effect of various concentrations (0.5– 3.0 mM) of Mg2+ and Al3+ ions on the kinetics and thermodynamics of Aspergillus niger invertases for sucrose hydrolysis. We found that both metal ions enhanced the affinity of invertase for sucrose by decreasing the Km. In the presence of 0.5 mM Al3+ ions invertase have maximum affinity for sucrose (Km = 0.00914 M sucrose). Invertase was activated by Mg2+ ions at low concentrations (0.5–2.0 mM) and 341% increase in turnover (Kcat) and maximum decrease in ΔG* was observed in the presence of 0.5 mM Mg2+ ions. The entropy change for activation of substrate hydrolysis (ΔS*) was increased by all concentrations of Mg2+ ions and was highest (-94 J mol-1 K-1) for invertases bound with 1.5 mM Mg2+ ions.
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Keywords: Al3+ ions; Aspergillus niger; Mg2+ ions; invertase; kinetics; physiochemical characterization; thermodynamics

Document Type: Research Article

Publication date: August 1, 2015

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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