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|Title:||Stabilization of DEAE cellulose adsorbed and glutaraldehyde crosslinkedwhite radish (Raphanus sativus) peroxidase|
|Abstract:||Present work demonstrates adsorption of ammonium sulphate fractionated proteins of white radish (Raphanus sativus) onDEAE cellulose and its crosslinking by glutaraldehyde. Adsorbed enzyme exhibited an immobilization yield of 88% and itsactivity decreased to 81% after crosslinking. Temperature and pH optima for soluble and immobilized enzyme were same. Therewas a significant enhancement in activity of adsorbed and crosslinked peroxidase to 136%, 143%, and 126% after its exposure60% dimethylformamide, 60% n-propanol and 60% acetone, respectively. However, soluble enzyme under similar experimental conditions, exhibited only 60%, 35% and 16% activity, respectively. Soluble enzyme lost 27% activity after its exposure to 4.0urea for 1 h, whereas activity of adsorbed crosslinked and uncrosslinked enzyme was enhanced to 153% and 142%,respectively. Adsorbed and crosslinked peroxidase retained 63% activity after 1 h exposure to 1.0 M sodium sulphite, whereasonly adsorbed and soluble enzyme lost 74% and 97% of their initial activity. Adsorbed and crosslinked enzyme retained 61% ofactivity after 7th repeated use as compared to adsorbed enzyme, which retained a marginal activity of 21%.|
|ISSN:||0975-1084 (Online); 0022-4456 (Print)|
|Appears in Collections:||JSIR Vol.69(08) [August 2010]|
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