Preparation and application of porous poly(styrene-divinylbenzene) beads for enzyme immobilization

碩士 === 國立中正大學 === 化學工程研究所 === 87 === Highly porous and cross-linked styrene-divinylbenzene copolymer (PS-DVB) particles have been widely used as the stationary phases for size exclusion and ion-exchange chromatography. For biological applications, for example, protein chromatography and e...

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Bibliographic Details
Main Authors: Cheng-Ho Ke, 柯成河
Other Authors: Wen-Chien Lee
Format: Others
Language:zh-TW
Published: 1999
Online Access:http://ndltd.ncl.edu.tw/handle/34418445839209639118
Description
Summary:碩士 === 國立中正大學 === 化學工程研究所 === 87 === Highly porous and cross-linked styrene-divinylbenzene copolymer (PS-DVB) particles have been widely used as the stationary phases for size exclusion and ion-exchange chromatography. For biological applications, for example, protein chromatography and enzyme immobilization, the porous structure of the particles could lead to diffusional limitation. In this study, the PS-DVB particles having a porous structure with large pores near the periphery of the particles were prepared for biological applications. Styrene-divinylbenzene copolymer particles were prepared via a method of multi-step swelling and polymerization in this research. The influences of the amount of styrene used for preparing polymeric porogen particles and toluene used for copolymerization on the particle morphology and porous structure were studied. The prepared PS-DVB particles then were used for immobilization of Candida rugosa lipase. The thermostability of resultant immobilized lipase in organic solvent was also studied. Increasing the amounts of the styrene and toluene, respectively, used for preparing polymeric porogen particles and copolymer could result in copolymer particles having a higher specific surface area and uniform size distribution, according to the results from Micromeritics (ASAP 2000) and the photographs of SEM. When C. rugosa lipase was immobilized on PS-DVB, the optimum temperature for enzymatic activity was increased and thermodeactivation in organic solvent was slowed down. However, in comparison with that immobilized on PP, the immobilized enzyme on PS-DVB retained a lower activity after the first stage deactivation due to a probable change in the conformation of enzyme molecule by immobilization.