Partial purification and characterization of activity peak B amylolytic enzyme from Saccharomycopsis bubodii 2066 / (Record no. 2321)

MARC details
000 -LEADER
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
Holdings
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
    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
 
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