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Eldin Mohy M.S.,Advanced Technologies and New Material Research Institute | Seuror .E.I.,Genetic Engineering and Biotechnology Research Institute | Nasr M.A.,Alexandria University | Tieama H.A.,Advanced Technologies and New Material Research Institute
Applied Biochemistry and Biotechnology | Year: 2011

A novel affinity covalent immobilization technique of glucoamylase enzyme onto ρ-benzoquinone-activated alginate beads was presented and compared with traditional entrapment one. Factors affecting the immobilization process such as enzyme concentration, alginate concentration, calcium chloride concentration, cross-linking time, and temperature were studied. No shift in the optimum temperature and pH of immobilized enzymes was observed. In addition, K m values of free and entrapped glucoamylase were found to be almost identical, while the covalently immobilized enzyme shows the lowest affinity for substrate. In accordance, Vm value of covalently immobilized enzyme was found lowest among free and immobilized counter parts. On the other hand, the retained activity of covalently immobilized glucoamylase has been improved and was found higher than that of entrapped one. Finally, the industrial applicability of covalently immobilized glucoamylase has been investigated through monitoring both shelf and operational stability characters. The covalently immobilized enzyme kept its activity over 36 days of shelf storage and after 30 repeated use runs. Drying the catalytic beads greatly reduced its activity in the beginning but recovered its lost part during use. In general, the newly developed affinity covalent immobilization technique of glucoamylase onto ρ-benzoquinoneactivated alginate carrier is simple yet effective and could be used for the immobilization of some other enzymes especially amylases. © Springer Science+Business Media, LLC 2010. Source


Eldin M.S.M.,Advanced Technologies and New Material Research Institute | Seuror E.I.,Genetic Engineering and Biotechnology Research Institute | Nasr M.A.,Alexandria University | El-Aassar M.R.,Advanced Technologies and New Material Research Institute | Tieama H.A.,Advanced Technologies and New Material Research Institute
Applied Biochemistry and Biotechnology | Year: 2011

Ρ-Benzoquinone-activated alginate beads were presented as a new carrier for affinity covalent immobilization of glucoamylase enzyme. Evidences of alginate modification were extracted from FT-IR and thermal gravimetric analysis and supported by morphological changes recognized through SEM examination. Factors affecting the modification process such as ρ-benzoquinone (PBQ) concentration, reaction time, reaction temperature, reaction pH and finally alginate concentration, have been studied. Its influence on the amount of coupled PBQ was consequently correlated to the changes of the catalytic activity and the retained activity of immobilized enzyme, the main parameters judging the success of the immobilization process. The immobilized glucoamylase was found kept almost 80% of its native activity giving proof of non-significant substrate, starch, diffusion limitation. The proposed affinity covalent immobilizing technique would rank among the potential strategies for efficient immobilization of glucoamylase enzyme. © Springer Science+Business Media, LLC 2010. Source

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