Immobilization of catalase on a novel polymer support, crosslinked polystyrene ethylene glycol acrylate resin: Role of the macromolecular matrix on enzyme activity

Abstract

ABSTRACT:Crosslinked polystyrene ethylene glycol acrylate resin (CLPSER) was developed for the immobilization of the enzyme catalase by the introduction of a crosslinker, O,OЈ-bis(2-acrylamidopropyl) poly(ethylene glycol) 1900 , to styrene. The crosslinker was prepared by the treatment of acryloyl chloride with O,OЈ-bis(2-aminopropyl) poly(ethylene glycol) 1900 in the presence of diisopropylethylamine. The resin was characterized with IR and 13 C-NMR spectroscopy. The catalytic activity of the catalase-immobilized system of CLPSER was compared with divinylbenzenecrosslinked polystyrene, ethylene glycol dimethacrylate crosslinked polystyrene, and 1,4-butanediol dimethacrylate crosslinked polystyrene systems. Crosslink levels of 2, 8, and 20 mol % were evaluated. Among these crosslinked systems, the 2 mol % system was found to be most suitable to support catalytic activity. When a long flexible hydrophilic poly(ethylene glycol) crosslink, introduced between the polystyrene (PS) backbone and functional groups was used for immobilization, the extent of coupling and enzyme activity increased. Depending on the nature of the support, the catalytic activity of the system varied. The hydrophilic CLPSER support was most efficient for immobilization compared to the other PS-based supports.

Immobilization of Proteins in Poly-Styrene-Divinylbenzene Matrices: Functional Properties and Applications

“…The problems generated by the hydrophobicity have been studied in a systematic way in several cases. For example, the comparison of PSD with other styrene crosslinked polymers (that offer a lower hydrophobicity like ethylene glycol dimethacrylate, 1,4-butanediol dimethacrylate and ethylene glycol acrylate) produced an improvement on the expressed activity of catalase covalently attached to carboxylated supports [21]. An inverse correlation between hydrophobicity and activity retention was found in this study.…”

Co-localization of glucose oxidase and catalase enabled by a self-assembly approach: Matching between molecular dimensions and hierarchical pore sizes

“…But excessive crosslinking reaction might lead to giant protein molecules and do harm to the structure enzyme. It turned out that the immobilization procedure should be performed at pH 6.4. the diffusion of protein into the pore of amino resin can be accelerated, facilitating the process of immobilization (Kumar & Kumar, 2005;Zhuang, Zhang, Zhu, An, Li, Mu, et al, 2016). On the other hand at the temperature above 25 o C, thermos-stability of the conformation of enzymes turned to be the main restraint.…”

Immobilization of catalase onto hydrophilic mesoporous poly(ethylene‐co‐vinyl alcohol) monoliths

“…Recently, we have fabricated an EVOH‐based monolith by using TIPS technique for the first time . The EVOH monolith possessing hydrophilic hydroxyl groups has many superior properties over other hydrophobic polymers for enzyme immobilization …”