Literature DB >> 14584926

Kinetics of enhanced thermostability of an extracellular glucoamylase from Arachniotus sp.

Zafar Iqbal1, M H Rashid, A Jabbar, M A Malana, A M Khalid, M I Rajoka.   

Abstract

Purified extracelluar glucoamylase from Arachniotus sp. was used for kinetic and thermodynamic characterization. Thermal inactivation followed first order kinetics. The denaturation/activation energies of enzyme were 57 and 89 kJ mol(-1), respectively. Both enthalpy and entropy of activation for inactivation were lower than those for glucoamylases reported in literature. It is suggested that the enzyme is highly thermostable and is suitable for industrial applications.

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Year:  2003        PMID: 14584926     DOI: 10.1023/a:1025665831426

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN: 0141-5492            Impact factor:   2.461


  3 in total

1.  Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1.

Authors:  Vimal S Prajapati; Ujjval B Trivedi; Kamlesh C Patel
Journal:  Indian J Microbiol       Date:  2013-04-28       Impact factor: 2.461

2.  Thermal Characterization of Purified Glucose Oxidase from A Newly Isolated Aspergillus Niger UAF-1.

Authors:  Muhammad Anjum Zia; Muhammad K Saeed; Fozia Andaleeb; Muhammad I Rajoka; Munir A Sheikh; Iftikhar A Khan; Azeem I Khan
Journal:  J Clin Biochem Nutr       Date:  2007-09       Impact factor: 3.114

3.  A new method to determine optimum temperature and activation energies for enzymatic reactions.

Authors:  M Wojcik; J Miłek
Journal:  Bioprocess Biosyst Eng       Date:  2016-04-11       Impact factor: 3.210

  3 in total

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