Abstract
The endonuclease from S.aureus has been immobilized on ground maize cob, previously activated with tosyl chloride. Pretreatment of the support in acid before tosylation yielded the best insoluble enzyme derivatives. The catalytic activity has been evaluated as percent of total hydrolysis attained in a batch reactor using DNA as a model substrate. The derivatives prepared are very resistant to high temperatures under conditions of catalysis (24 h at 45°C). For these long reaction times, the extent of hydrolysis in the presence of small amounts of organic solvents (dimethyl sulfoxide at 2%) is larger than in plain buffer (Tris). This type of derivative could be very useful for the removal of nucleic acids from single-cell protein concentrates.
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Sánchez-Montero, J.M., Slnisterra, J.V. & Ballesteros, A. DNase activity ofMicrococcal endonuclease insolubilized on corn cob. Appl Biochem Biotechnol 22, 205–214 (1989). https://doi.org/10.1007/BF02921745
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DOI: https://doi.org/10.1007/BF02921745