Production studies, purification,and characterization of amylolytic enzyme from saccharomycopsis fibuligera 2074 isolated from Philippine bubod starter / Lani Lee Rigor Bullo.
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TextLanguage: English Publication details: 2009Description: 73 leavesSubject(s): Dissertation note: Thesis (BS Food Technology) -- University of the Philippines Mindanao, 2009 Abstract: Saccharomycopsis fibuligera 2074 was identified to produce the highest extracellular raw starch-digesting amylase among eight amylolytic bubod isolates screened. Maximum growth and amylase production was obtained from 36-hour culture using 1% raw sago starch as the major carbon source. The enzyme was purified 2.56- fold, with a specific activity of 180.49 U/mg after DEAE-cellulose anion-exchange column chromatography. Amylase activity was optimum at pH of 6 and at 400C, Although the enzyme was inhibited by CU2+, Zn2+ and Al3+, it was activated by Ca2+, Fe3+, Ba2+, phenylmethylsulfonyl fluoride and ethylenediaminetetraacetic acid. On the other hand, iodoacetic acid K+, Cd2+, and Mg2+, showed no significant effect on amylase activity. The purified amylase showed interesting properties necessary for industrial application.
| Item type | Current library | Collection | Call number | Status | Date due | Barcode |
|---|---|---|---|---|---|---|
| University Library Theses | Room-Use Only | LG993.5 2009 F62 B84 (Browse shelf(Opens below)) | Not For Loan | 3UPML00012390 | ||
| University Library Archives and Records | Preservation Copy | LG993.5 2009 F62 B84 (Browse shelf(Opens below)) | Not For Loan | 3UPML00032701 |
Thesis (BS Food Technology) -- University of the Philippines Mindanao, 2009
Saccharomycopsis fibuligera 2074 was identified to produce the highest extracellular raw starch-digesting amylase among eight amylolytic bubod isolates screened. Maximum growth and amylase production was obtained from 36-hour culture using 1% raw sago starch as the major carbon source. The enzyme was purified 2.56- fold, with a specific activity of 180.49 U/mg after DEAE-cellulose anion-exchange column chromatography. Amylase activity was optimum at pH of 6 and at 400C, Although the enzyme was inhibited by CU2+, Zn2+ and Al3+, it was activated by Ca2+, Fe3+, Ba2+, phenylmethylsulfonyl fluoride and ethylenediaminetetraacetic acid. On the other hand, iodoacetic acid K+, Cd2+, and Mg2+, showed no significant effect on amylase activity. The purified amylase showed interesting properties necessary for industrial application.
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