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Titolo:
Coimmobilization of L-asparaginase and glutamate dehydrogenases onto highly activated supports
Autore:
Balcao, VM; Mateo, C; Fernandez-Lafuente, R; Malcata, FX; Guisan, JM;
Indirizzi:
Univ Catolica Portuguesa, Escola Super Biotecnol, P-4200072 Porto, Portugal Univ Catolica Portuguesa Porto Portugal P-4200072 200072 Porto, Portugal Univ Fernando Pessoa, P-4249004 Porto, Portugal Univ Fernando Pessoa Porto Portugal P-4249004 P-4249004 Porto, Portugal CSIC, Inst Catalisis & Petroquim, E-28049 Madrid, Spain CSIC Madrid Spain E-28049 t Catalisis & Petroquim, E-28049 Madrid, Spain
Titolo Testata:
ENZYME AND MICROBIAL TECHNOLOGY
fascicolo: 7-8, volume: 28, anno: 2001,
pagine: 696 - 704
SICI:
0141-0229(20010507)28:7-8<696:COLAGD>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLY(ETHYLENE GLYCOL)-ALBUMIN HYDROGEL; POST-IMMOBILIZATION TECHNIQUES; CRYSTAL-STRUCTURE; IN-VITRO; STABILIZATION; ENZYMES; DERIVATIVES; PERFORMANCE; ATTACHMENT; CELLS;
Keywords:
enzyme; agarose; structural stabilization; immobilization; biochemical engineering; biomedical engineering;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Malcata, FX Univ Catolica Portuguesa, Escola Super Biotecnol, Rua Dr Antonio Bernardino de Almeida, P-4200072 Porto, Portugal Univ Catolica Portuguesa Rua Dr Antonio Bernardino de Almeida Porto Portugal P-4200072
Citazione:
V.M. Balcao et al., "Coimmobilization of L-asparaginase and glutamate dehydrogenases onto highly activated supports", ENZYME MICR, 28(7-8), 2001, pp. 696-704

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 theinduction period (time before the maximum reaction rate is virtually achieved! and an increase in the maximum reaction rate. The effectiveness of theindependent 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 ammoniaformed), with the nanoenvironment surrounding each enzyme molecule being essentially devoid of steric hindrance. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 04:51:50