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Invertase from Hyper Producer Strain of Aspergillus niger: Physiochemical Properties, Thermodynamics and Active Site Residues Heat of Ionization

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Here we report for the first time heat of ionization of invertase (E.C. active site residues from hyperproducer strain of Aspergillus niger (34.1 U ml-1), along with its physiochemical properties, kinetics and thermodynamics of stability-function. The Invertase showed great potential for industry as being highly efficient (kcat = 24167 s-1 at 65 °C, pH 5.0) and stable (half life= 12 h at 56°C).

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Keywords: Enthalpy; Entropy; Free energy; Ionization energy; Thermostability

Document Type: Research Article

Publication date: September 1, 2009

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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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