Kinetics of glucose isomerization to fructose by immobilized glucose isomerase in the presence of substrate protection

被引:40
作者
Converti A. [1 ]
Del Borghi M. [1 ]
机构
[1] Inst. Chem. Proc. Eng. G.B. Bonino, Faculty of Engineering, University of Genoa, I-16145 Genoa, Via Opera Pia
关键词
Immobilization; Fructose; Streptomyces; Immobilize Enzyme; Isomerase;
D O I
10.1007/s004490050406
中图分类号
学科分类号
摘要
The activity of immobilized glucose isomerase of Streptomyces murinus has been tested batchwise under different conditions in order to gather the related kinetic parameters necessary to optimize an immobilized enzyme column for the continuous production of high fructose corn syrup (HFCS). To this purpose, the Briggs-Haldane model incorporating an apparent first-order inactivation constant has been used with success. A comparison of the equilibrium constants and of the maximum theoretical conversion yields calculated at different temperatures with those estimated for the native enzyme demonstrates that the immobilization favours the transformation of glucose to fructose only at T > 70°C, as a possible consequence of a combined effect of catalysis and equilibrium thermodynamics enhancement. Enzyme inactivation has also been tested at different temperatures and sugar concentrations to evaluate the related kinetic parameters under different conditions of substrate protection.
引用
收藏
页码:27 / 33
页数:6
相关论文
共 25 条
[1]  
Riscolo A., Fisichella A., Ottimizzazione del Processo Continue di Isomerizzazione del Glucosio in Fruttosio Mediante Isomerasi Immobilizzata, (1996)
[2]  
Lloyd N.E., Nelson W.J., Glucose- and fructose-containing sweetners from starch, Starch - Chemistry and Technology, pp. 611-660, (1984)
[3]  
Chen K.C., Chang C.M., Operational stability of immobilized D-glucose isomerase in a continuous feed stirred tank reactor, Enzyme Microb. Technol., 6, pp. 359-364, (1984)
[4]  
Kobayashi T., Katogiri K., Ohmiya K., Effect of mass transfer on operational stability of immobilized enzyme, J. Ferment. Technol., 58, pp. 23-32, (1980)
[5]  
Lee G.K., Reilly P.J., The effect of slow intraparticle diffusion on observed immobilized enzyme stability, Chem. Eng. Sci., 36, pp. 1967-1975, (1981)
[6]  
Ollis D.F., Diffusion influences in denaturable insolubilized enzyme catalysts, Biotechnol. Bioeng., 14, pp. 871-884, (1972)
[7]  
Korus R.A., O'Driscoll K.F., The influence of diffusion on the apparent rate of denaturation of gel entrapped enzymes, Biotechnol. Bioeng., 17, pp. 441-444, (1975)
[8]  
Sproull R.D., Lim H.C., Schneider D.R., A model for enzymatic isomerization of D-glucose to D-fructose in a batch reactor, Biotechnol. Bioeng., 18, pp. 633-648, (1976)
[9]  
Korus R.A., O'Driscoll K.F., The influence of diffusion on the apparent rate of denaturation of gel entrapped enzymes, Biotechnol. Bioeng., 18, (1976)
[10]  
Chen K.C., Suga K., Taguchi H., Effects of pore and film diffusion resistances and inactivation of enzyme on the overall reaction rate of immobilized enzyme, J. Ferment. Technol., 58, pp. 439-448, (1980)