Abstract
Here we report for the first time heat of ionization of invertase (E.C.3.2.1.26) 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).
Keywords: Thermostability, Enthalpy, Entropy, Free energy, Ionization energy
Protein & Peptide Letters
Title: Invertase from Hyper Producer Strain of Aspergillus niger: Physiochemical Properties, Thermodynamics and Active Site Residues Heat of Ionization
Volume: 16 Issue: 9
Author(s): Habibullah Nadeem, Muhammad Hamid Rashid, Muhammad Riaz, Bibi Asma, Muhammad Rizwan Javed and Raheela Perveen
Affiliation:
Keywords: Thermostability, Enthalpy, Entropy, Free energy, Ionization energy
Abstract: Here we report for the first time heat of ionization of invertase (E.C.3.2.1.26) 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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Cite this article as:
Nadeem Habibullah, Rashid Hamid Muhammad, Riaz Muhammad, Asma Bibi, Javed Rizwan Muhammad and Perveen Raheela, Invertase from Hyper Producer Strain of Aspergillus niger: Physiochemical Properties, Thermodynamics and Active Site Residues Heat of Ionization, Protein & Peptide Letters 2009; 16 (9) . https://dx.doi.org/10.2174/092986609789055322
DOI https://dx.doi.org/10.2174/092986609789055322 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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