Digestive enzymes from human intestinal mucosa were solubilized by Triton X-100 and papain and covalently bound to cyanogen bromide-activated Sepharose 4-B gel. Triton X-100 solubilized most of the activities, and 39.1 to 63.5% were immobilized on the carrier. The other enzymes, still bound on the m
Enzyme immobilization on palmityl–sepharose
✍ Scribed by Mohsen Nemat-Gorgani; Khashayar Karimian
- Publisher
- John Wiley and Sons
- Year
- 1983
- Tongue
- English
- Weight
- 644 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
Enzymes adsorbed on palmityl-substituted Sepharose 4B by hydrophobic interactions have been used in reactor-type experiments. Results presented on immobilized glutamate dehydrogenase, trypsin, a-chymotrypsin, and amyloglucosidase indicate possible potential of the method for continuous catalytic operations. Glutamate dehydrogenase used as a model allosteric enzyme was found to retain its allosteric properties after binding to the absorbent in the form of column or suspension. Thermal stabilities of glutamate dehydrogenase and a-chymotrypsin were significantly decreased upon adsorption, while that of trypsin was apparently unaltered. Results are discussed in terms of specific interactions involving palmityl residues present on the matrix. Relevance of these observations to in vivo processes are also discussed.
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