Partial purification and characterization of activity peak B amylolytic enzyme from Saccharomycopsis bubodii 2066 / Leslie Pearl Mansilita Cancio
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TextLanguage: English Publication details: 2009Description: 74 leavesSubject(s): Dissertation note: Thesis (BS Food Technology) -- University of the Philippines Mindanao, 2009 Abstract: Extracellular amylolytic enzyme production of Saccharomycopsis bubodii 2066 was enhanced using raw sago starch as carbon source and incubating the culture for 9 h without agitation. After DEAE-cellulose column chromatography, two activity peaks were observed. Activity peak B, obtaining the highest specific activity of 46.57 U/mg and was partially purified by 2.02 fold, was used for further characterization. Optimum activity of the enzyme was observed at 400C and pH 4.5. maximum stability was obtained at 30-400C and pH range of 4.0-5.0. the enzyme was activated by Ca2+ and was inactivated by Ba2+, Cu2+, Mg2+, Zn2+ and K+. other chemical modifiers like Cd2+, Al3+, Fe3+, EDTA and iodoacetic acid showed no significant effect on the activity of the enzyme.
| Item type | Current library | Collection | Call number | Status | Date due | Barcode |
|---|---|---|---|---|---|---|
| University Library Theses | Room-Use Only | LG993.5 2009 F62 C36 (Browse shelf(Opens below)) | Not For Loan | 3UPML00012498 | ||
| University Library Archives and Records | Preservation Copy | LG993.5 2009 F62 C36 (Browse shelf(Opens below)) | Not For Loan | 3UPML00033168 |
Thesis (BS Food Technology) -- University of the Philippines Mindanao, 2009
Extracellular amylolytic enzyme production of Saccharomycopsis bubodii 2066 was enhanced using raw sago starch as carbon source and incubating the culture for 9 h without agitation. After DEAE-cellulose column chromatography, two activity peaks were observed. Activity peak B, obtaining the highest specific activity of 46.57 U/mg and was partially purified by 2.02 fold, was used for further characterization. Optimum activity of the enzyme was observed at 400C and pH 4.5. maximum stability was obtained at 30-400C and pH range of 4.0-5.0. the enzyme was activated by Ca2+ and was inactivated by Ba2+, Cu2+, Mg2+, Zn2+ and K+. other chemical modifiers like Cd2+, Al3+, Fe3+, EDTA and iodoacetic acid showed no significant effect on the activity of the enzyme.
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