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Stability and kinetics of β-1,3-glucanse from Trichoderma harzianum
Kalaimahan Théodore, G. Sathya Narayana Naidu,
Published in Elsevier BV
Volume: 39
Issue: 2
Pages: 149 - 155
Stability studies and kinetics of β-1,3-glucanase from Trichoderma harzianum NCIM 1185 are reported. The critical parameters, pH and temperature, affecting the stability of β-1,3-glucanase were optimized using response surface methodology. The optimal combination of pH and temperature were 3.6 and 41 °C, respectively. The stability of β-1,3-glucanase was studied at various conditions of pH and temperature above the optimal conditions. Since the final activity was not zero, a non-first order deactivation model was used to explain the experimental data. Enzyme kinetic studies were carried out with and without inhibitors. Cu2+ behaved as a noncompetitive- uncompetitive mixed inhibitor, whereas EDTA and NH4+ behaved as competitive-noncompetitive type mixed inhibitors during the hydrolysis of β-1,3-glucan. © 2002 Elsevier Ltd. All rights reserved.
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JournalData powered by TypesetProcess Biochemistry
PublisherData powered by TypesetElsevier BV
Open AccessNo
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