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dc.contributor.authorSatar, Rukhsana-
dc.contributor.authorMatto, Mahreen-
dc.contributor.authorHusain, Qayyum-
dc.description.abstractAmmonium sulfate fractionated proteins of bitter gourd (Momordica charantia) were precipitated using jack bean extract as a source of concanavalin A. Concanavalin A-bitter gourd peroxidase retained nearly 86% original activity. This complex was entrapped into calcium alginate-pectin gel. Entrapped concanavalin A-peroxidase complex retained 51% original activity. Soluble and immobilized peroxidase preparations exhibited maximum activity at 40°C and pH 5.5. Concanavalin A-peroxidase complex and entrapped concanavalin A-enzyme complex retained greater fraction of catalytic activity at higher temperatures as compared to soluble form and also showed more broadening in pH-activity profiles, indicating a marked increase in stability. Concanavalin A-bitter gourd peroxidase and calcium alginate-pectin entrapped concanavalin A-bitter gourd peroxidase preparations were more stable as compared to soluble counterpart against denaturation induced by heat, pH, urea, organic solvents and detergents.en_US
dc.sourceJSIR Vol.67(8) [August 2008]en_US
dc.subjectAlginateBitter gourd, Concanavalin A, Entrapped, Pectin, Peroxidaseen_US
dc.subjectBitter gourden_US
dc.subjectConcanavalin Aen_US
dc.titleStudies on calcium alginate-pectin gel entrapped concanavalin A-bitter gourd (Momordica charantia) peroxidase complexen_US
Appears in Collections: JSIR Vol.67(08) [August 2008]

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