Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.14/6833
Título: Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports
Autor: Balcão, Victor M.
Mateo, Cesar
Fernández-Lafuente, R.
Malcata, F. Xavier
Guisán, José M.
Palavras-chave: Enzyme
Agarose
Structural stabilization
Immobilization
Biochemical engineering
Biomedical engineering
Data: 2001
Citação: BALCÃO, Vitor M... [et al.] - Coimmobilization of L-asparaginase and glutamate dehydrogenase onto highly activated supports. Enzyme and Microbial Technology. ISSN 0141-0229. Vol. 28, n.º 7-8 (2001), p. 696–704
Resumo: 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.
Peer review: yes
URI: http://hdl.handle.net/10400.14/6833
Versão do Editor: doi:10.1016/S0141-0229(01)00307-6
Aparece nas colecções:ESB - Artigos em revistas internacionais com Arbitragem / Papers in international journals with Peer-review

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