The use of poly(ethylene oxide) for the efficient stabilization of entrapped alpha-chymotrypsin in silicone elastomers: a chemometric study.
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The enzyme alpha-chymotrypsin, a model for catalytic proteins, was entrapped in different silicone elastomers that were formed via the condensation-cure room temperature vulcanization (CC-RTV) of silanol terminated poly(dimethylsiloxane) with tetraethyl orthosilicate as a crosslinker, in the presence of different poly(ethylene oxide) oligomers that were functionalized with triethoxysilyl groups. The effects of various chemical factors on both the activity and entrapping efficiency of proteins (leaching) were studied using a 2-level fractional factorial design--a chemometrics approach. The factors studied include the concentration and chain length of poly(ethylene oxide), enzyme content, and crosslinker (TEOS) concentration. The study indicated that poly(ethylene oxide) can stabilize the entrapped alpha-chymotrypsin in silicone rubber: the specific activity can be maximized by incorporating a relatively high content of short chain, functional PEO. Increased enzyme concentration was found to adversely affect the specific activity. The effect of TEOS was found to be insignificant when PEO was present in the elastomer, however, it does affect the activity positively in the case of simple elastomers.
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