Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports

Enzyme and Microbial Technology
Victor M BalcãoJ M Guisán

Abstract

In the present research work, production of coimmobilized derivatives of L-asparaginase and glutamate dehydrogenase was attempted. Comparison of immobilization of each enzyme independently with coimmobilization of the two enzymes unfolded important advantages of the latter, namely a decrease in the induction period (time before the maximum reaction rate is virtually achieved) and an increase in the maximum reaction rate. The effectiveness of the independent enzyme derivatives was low; however, it was enhanced by three-fold when the enzymes were coimmobilized onto the same agarose-glutaraldehyde support. Each supporting agarose bead may in fact be viewed as a nano-reactor with in situ reaction and separation (i.e. elimination of the ammonia formed), with the nanoenvironment surrounding each enzyme molecule being essentially devoid of steric hindrance.

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Citations

Feb 11, 2010·Applied Microbiology and Biotechnology·Ashraf S El-Sayed
May 21, 2013·Enzyme and Microbial Technology·Victor M BalcãoMarta M D C Vila
Feb 2, 2013·Applied Biochemistry and Biotechnology·Johan Alftrén, Timothy John Hobley
Aug 30, 2008·International Journal of Pharmaceutics·Rui WangSheng Zhang
Oct 15, 2014·Advanced Drug Delivery Reviews·Victor M Balcão, Marta M D C Vila
Apr 1, 2015·Biomolecules·Maristella MaggiClaudia Scotti
May 16, 2017·Bioconjugate Chemistry·Ahmet Ulu, Burhan Ates
Apr 27, 2018·Physical Chemistry Chemical Physics : PCCP·Alexandra LoukaClaudio Luchinat
Oct 3, 2014·Biotechnology and Applied Biochemistry·Ashraf S A El-SayedHend Ibrahim
May 18, 2007·Chembiochem : a European Journal of Chemical Biology·Kai Holland-Nell, Annette G Beck-Sickinger
May 20, 2019·Applied Microbiology and Biotechnology·Marcela Medeiros de FreitasPérola Oliveira Magalhães

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