Modelling and simulation of a bienzymatic reaction system co-immobilised within hydrogel-membrane liquid-core capsules

被引:18
作者
Blandino, A [1 ]
Macías, M [1 ]
Cantero, D [1 ]
机构
[1] Univ Cadiz, Fac Sci, Dept Chem Engn Food Technol & Environm Technol, Biol & Enzymat Reactors Res Grp, Cadiz 11510, Spain
关键词
bienzymatic system; co-encapsulation; enzyme distribution; deactivation; mathematical model;
D O I
10.1016/S0141-0229(02)00154-0
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A mathematical model applicable to the analysis and simulation of a heterogeneous bienzymatic reaction system is presented. The glucose oxidase-catalase (GOD-CAT) system co-encapsulated within hydrogel-membrane liquid-core capsules was chosen as the model system in this study. The proposed model considers a non-uniform biocatalyst concentration profile within the support and the deactivation phenomena of the two enzymes. Simulation experiments allowed us to elucidate the distribution of the two enzymes within the capsules. It seemed that GOD was distributed across the whole of the particle while CAT was confined almost exclusively to the core of the capsule. From the simulated glucose and hydrogen peroxide concentrations within the capsules, it was deduced that the hydrogen peroxide formed in the glucose oxidation reaction led firstly to the deactivation of the catalase and, after this point, GOD deactivation was accelerated. (C) 2002 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:556 / 565
页数:10
相关论文
共 20 条
[1]   Glucose oxidase release from calcium alginate gel capsules [J].
Blandino, A ;
Macías, M ;
Cantero, D .
ENZYME AND MICROBIAL TECHNOLOGY, 2000, 27 (3-5) :319-324
[2]   Immobilization of glucose oxidase within calcium alginate gel capsules [J].
Blandino, A ;
Macías, M ;
Cantero, D .
PROCESS BIOCHEMISTRY, 2001, 36 (07) :601-606
[3]  
BOLTZ DF, 1987, COLORIMETRIC DETERMI, P543
[4]   Maximisation of the yield of final product on substrate in the case of sequential reactions catalysed by coimmobilised enzymes: a theoretical analysis [J].
Celayeta, JF ;
Silva, AH ;
Balcao, VM ;
Malcata, FX .
BIOPROCESS AND BIOSYSTEMS ENGINEERING, 2001, 24 (03) :143-149
[5]   DISTRIBUTION OF IMMOBILIZED ENZYMES ON POROUS MEMBRANES [J].
DALVIE, SK ;
BALTUS, RE .
BIOTECHNOLOGY AND BIOENGINEERING, 1992, 40 (10) :1173-1180
[6]   Kinetic modelling of the synthesis of 2-hydroxy-5-hexenyl 2-chlorobutyrate ester by an immobilised lipase [J].
García, R ;
García, T ;
Martínez, M ;
Aracil, J .
BIOCHEMICAL ENGINEERING JOURNAL, 2000, 5 (03) :185-190
[7]   ANALYSIS OF NONISOTHERMAL TUBULAR REACTOR PACKED WITH IMMOBILIZED ENZYME-SYSTEMS [J].
HASSAN, MM ;
ATIQULLAH, M ;
BEG, SA ;
CHOWDHURY, MHM .
CHEMICAL ENGINEERING JOURNAL AND THE BIOCHEMICAL ENGINEERING JOURNAL, 1995, 58 (03) :275-283
[8]  
HOSSAIN M, 1992, BIOTECHNOL BIOENG, V40, P747
[9]   Encapsulation of lactic acid bacteria with alginate/starch capsules [J].
Jankowski, T ;
Zielinska, M ;
Wysakowska, A .
BIOTECHNOLOGY TECHNIQUES, 1997, 11 (01) :31-34
[10]   Kinetic modeling of lactose hydrolysis with an immobilized β-galactosidase from Kluyveromyces fragilis [J].
Ladero, M ;
Santos, A ;
García-Ochoa, F .
ENZYME AND MICROBIAL TECHNOLOGY, 2000, 27 (08) :583-592