@article {Rajoka:2003:0929-8665:561,
title = "Kinetics and thermodynamics of the Native and Mutated Extracellular Endoglucanases From Cellulomonas Biazotea",
journal = "Protein and Peptide Letters",
parent_itemid = "infobike://ben/ppl",
publishercode ="ben",
year = "2003",
volume = "10",
number = "6",
publication date ="2003-12-01T00:00:00",
pages = "561-568",
itemtype = "ARTICLE",
issn = "0929-8665",
url = "https://www.ingentaconnect.com/content/ben/ppl/2003/00000010/00000006/art00004",
doi = "doi:10.2174/0929866033478609",
keyword = "cellulomonas biazotea, enzyme kinetics, thermodynamics, melting point, derepressed mutant, endo-glucanase enthalpy",
author = "Rajoka, M. I. and Ashraf, Yasmin and Rashid, Hamid and Khalid, A. M.",
abstract = "The mutation had dramatic effect on the kinetic and thermodynamic parameters inferring thermostability of endo-glucanase from Cellulomonas biazotea mutant 51 SMr .The denaturation activation energies of native and mutated enzymes were 73.3 and 68.8 kJ / mol respectively. They showed compensation effect at 55\textdegreeC. Both enthalpy and entropy values of irreversible thermal inactivation for mutated enzyme were decreased suggesting that the mutation partly stabilized the enzyme.",
}