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. 1989 Nov;22(2):205-14.
doi: 10.1007/BF02921745.

DNase activity of micrococcal endonuclease insolubilized on corn cob

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DNase activity of micrococcal endonuclease insolubilized on corn cob

J M Sánchez-Montero et al. Appl Biochem Biotechnol. 1989 Nov.

Abstract

The endonuclease from S. aureus has been immobilized on ground maize cob, previously activated with tosyl chloride. Pretreatment of the support on 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 degrees C). For these long reaction times, the extent of hydrolysis in the presence of small amounts of organic solvent (dimethyl sulfoxide at 2 percent) 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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