000 | 02028nam a22003613a 4500 | ||
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001 | UPMIN-00003300492 | ||
003 | UPMIN | ||
005 | 20230126164550.0 | ||
008 | 230126b |||||||| |||| 00| 0 eng d | ||
040 |
_aDLC _cDLC _dupmin |
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041 | _aeng | ||
090 | 0 |
_aLG993.5 2009 _bF62 B84 |
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100 |
_aBullo, Lani Lee Rigor. _91670 |
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245 |
_aProduction studies, purification,and characterization of amylolytic enzyme from saccharomycopsis fibuligera 2074 isolated from Philippine bubod starter / _cLani Lee Rigor Bullo. |
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260 | _c2009 | ||
300 | _a73 leaves. | ||
502 | _aThesis (BS Food Technology) -- University of the Philippines Mindanao, 2009 | ||
520 | 3 | _aSaccharomycopsis 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. | |
650 | 1 | 7 |
_aAmylases. _91671 |
650 | 1 | 7 |
_aBubod yeasts. _91672 |
650 | 1 | 7 |
_aAmylase isolation. _91673 |
650 | 1 | 7 |
_aEnzyme characterization. _91674 |
650 | 1 | 7 |
_aEnzyme production. _91675 |
650 | 1 | 7 |
_aProtein purification. _91676 |
650 | 1 | 7 |
_aSaccharomycopsis fubuligera 2074. _91677 |
650 | 1 | 7 |
_aStarch-digesting amylase. _91678 |
650 | 1 | 7 |
_aHydrolysis. _91679 |
650 | 1 | 7 |
_aStarch. _91680 |
658 |
_aUndergraduate Thesis _cFST200, _2BSFT |
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905 | _aFi | ||
905 | _aUP | ||
942 |
_2lcc _cTHESIS |
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999 |
_c2301 _d2301 |