Partial purification and characterization of activity peak B amylolytic enzyme from Saccharomycopsis bubodii 2066 / (Record no. 2321)
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000 -LEADER | |
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fixed length control field | 01528nam a2200241 4500 |
001 - CONTROL NUMBER | |
control field | UPMIN-00004099663 |
003 - CONTROL NUMBER IDENTIFIER | |
control field | UPMIN |
005 - DATE AND TIME OF LATEST TRANSACTION | |
control field | 20230130105049.0 |
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION | |
fixed length control field | 100129s2009 ph eng |
040 ## - CATALOGING SOURCE | |
Original cataloging agency | DLC |
Transcribing agency | UPMin |
Modifying agency | upmin |
041 ## - LANGUAGE CODE | |
Language code of text/sound track or separate title | eng |
090 #0 - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN) | |
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) | LG993.5 2009 |
Local cutter number (OCLC) ; Book number/undivided call number, CALL (RLIN) | F62 C36 |
100 1# - MAIN ENTRY--PERSONAL NAME | |
Personal name | Cancio, Leslie pearl Mansilita |
9 (RLIN) | 1710 |
245 00 - TITLE STATEMENT | |
Title | Partial purification and characterization of activity peak B amylolytic enzyme from Saccharomycopsis bubodii 2066 / |
Statement of responsibility, etc. | Leslie Pearl Mansilita Cancio |
260 ## - PUBLICATION, DISTRIBUTION, ETC. | |
Date of publication, distribution, etc. | 2009 |
300 ## - PHYSICAL DESCRIPTION | |
Extent | 74 leaves |
502 ## - DISSERTATION NOTE | |
Dissertation note | Thesis (BS Food Technology) -- University of the Philippines Mindanao, 2009 |
520 3# - SUMMARY, ETC. | |
Summary, etc. | 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. |
658 ## - INDEX TERM--CURRICULUM OBJECTIVE | |
Main curriculum objective | Undergraduate Thesis |
Curriculum code | FST200, |
Source of term or code | BSFT |
905 ## - LOCAL DATA ELEMENT E, LDE (RLIN) | |
a | Fi |
905 ## - LOCAL DATA ELEMENT E, LDE (RLIN) | |
a | UP |
942 ## - ADDED ENTRY ELEMENTS (KOHA) | |
Source of classification or shelving scheme | Library of Congress Classification |
Koha item type | Thesis |
Withdrawn status | Lost status | Source of classification or shelving scheme | Damaged status | Status | Collection | Home library | Current library | Shelving location | Date acquired | Source of acquisition | Accession Number | Total Checkouts | Full call number | Barcode | Date last seen | Price effective from |
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Library of Congress Classification | Not For Loan | Preservation Copy | University Library | University Library | Archives and Records | 2010-07-06 | donation | UAR-T-gd1495 | LG993.5 2009 F62 C36 | 3UPML00033168 | 2022-10-05 | 2022-10-05 | ||||
Library of Congress Classification | Not For Loan | Room-Use Only | College of Science and Mathematics | University Library | Theses | 2010-01-22 | donation | CSM-T-gd2224 | LG993.5 2009 F62 C36 | 3UPML00012498 | 2022-10-05 | 2022-10-05 |