Kinetic and thermodynamic parameters of immobilized glucoamylase on different mesoporous silica for starch hydrolysis A comparative study Journal Article


Author(s): George R; Sugunan, S
Article Title: Kinetic and thermodynamic parameters of immobilized glucoamylase on different mesoporous silica for starch hydrolysis A comparative study
Alternate Title: Journal of Molecular Catalysis B: Enzymatic
Keywords: Aspergillus niger glucoamylase; Bifunctional agent; Enthalpy of activation; Entropy of activation; Hydrothermal method; Mesosilica; Substrate binding
Journal Title: Unknown
Volume: 106
Publisher: Kerala Science Congress  
Date Published: 2014
Start Page: 81
End Page: 89
DOI/URL:
Notes: --- - "Large ordered mesoporous silica materials having different pore diameters were synthesized by hydrothermal method functionalized with 3-APTES and bifuctional agent glutaraldehyde. Aspergillus niger glucoamylase was immobilized onto mesosilica via simple adsorption technique and covalent binding. The bare and enzyme immobilized supports were characterized by low angle XRD, nitrogen adsorption studies, FT-IR spectroscopy, thermogravimetric analysis (TG) and scanning electron microscopy (SEM). Kinetic and thermodynamic parameters were evaluated for soluble starch hydrolysis. Kinetic parameters were calculated according to Lineweaver-Burk plot and Km value was found to increase and Vmax was found to decrease after immobilization. Activation energy for free enzyme was found to 20.43 kJ mol-1. The enthalpy of activation (\xCE\x94H), Gibbs free energy (\xCE\x94G substrate binding) and entropy of activation (\xCE\x94S) for soluble starch hydrolysis by glucoamylase are reported. \xC2\xA9 2014 Elsevier B.V." - <p>Cited By :2</p> - "<p>Export Date: 6 February 2015</p>"
CUSAT Authors
  1. Dr. S. Sugunan
    390 Sugunan