The Analysis of The Immobilization of Enzyme by Orthogonal Collocation Method

• Main Authors: Xu, Han-Fu, 許涵富
• Other Authors: Hung-Jye Lin
• Format: Others
• Language: zh-TW
• Published: 1996
• Online Access: http://ndltd.ncl.edu.tw/handle/64442992241225125579

碩士 === 國立成功大學 === 化學工程學系 === 84 === A restricted-diffusion model of immobilized enzyme in porous support has beenestablished in this work. The model is solved by orthogonal method and Runge-Kutta method.The distribution of immobilized enzyme in the pores,and the para-meter of the immobilization process have been investigated by using this model. Our conception is to use glutaraldehyde as the crosslinking agent between supports and urease,and make their binding stable.The exxperiments were operated at 25℃,and used 0.1M phosphate solution buffered at pH6.5.The ureaseconcentration was measured by UV-VIS spectrophotometer. A510 and A400 resins were used as the supports of urease. Because of the differences in resin pore diameter,the amount of adsorbed urease and the effective urea hydrolysis rate were different. Our experiment shows that the amount of urease adsorbed were29.3mg/ml and 12.6mg/ml for A510 and A400 respectively.The amount of urease adsorbed per mililiter of A510 resin is about 2.3 times that of A400 resin.The best activities of these immobilized urease occur at pH6.5 and the rate ofurea hydrolysis is about 31.4 and 20.3 μmol NH3/min mg urease for A510 resinand A400 resin respectively. The parameters in restricted-diffusion model were obtained by curve fitting the experimental data. The system parameter for using A510 resin as support are N=0.018,ψ=0.0059,α=0.0022,φ=60,and kim=1.3e-1 1/sec g ,while system parameter that use A400 resin as support are N=0.036,ψ=0.0065,α=0.292,φ=60and kim=1.8e-3 1/sec g . In accordance with the effect of the whole immobilized process and the hydrolysis rate,we conclude that A510 resin is a better support for enzyme immobilization than A400 resin.