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

• Published in: Enzyme and microbial technology 2001-05, Vol.28 (7), p.696-704
• Main Authors: Balcão, Victor M., Mateo, Cesar, Fernández-Lafuente, R., Malcata, F.Xavier, Guisán, José M.
• Format: Article
• Language: English
• Subjects: Agarose; asparaginase; Biochemical engineering; Biological and medical sciences; Biomedical engineering; Biotechnology; Enzyme; Fundamental and applied biological sciences. Psychology; glutaraldehyde; Immobilization; Immobilization of enzymes and other molecules; Immobilization techniques; Methods. Procedures. Technologies; Structural stabilization
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/S0141-0229(01)00307-6

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.