Characterization and thermostability study of invertase by Aspergillus niger in submerged culture / (Record no. 4320)

MARC details
000 -LEADER
fixed length control field 02387nam a2200265 a 4500
001 - CONTROL NUMBER
control field vtls000076046
003 - CONTROL NUMBER IDENTIFIER
control field KUKTEM
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20251114204554.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 131113t2013 my da f m 000 0 eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number THE0002134(Local)
039 #9 - LEVEL OF BIBLIOGRAPHIC CONTROL AND CODING DETAIL [OBSOLETE]
Level of rules in bibliographic description 201905131654
Level of effort used to assign nonsubject heading access points yusri
-- 201311130921
-- nabilah
040 ## - CATALOGING SOURCE
Original cataloging agency UMP
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) QD321 .I99 2013 rs Bc.
100 0# - MAIN ENTRY--PERSONAL NAME
Personal name Nurul Izzah Ahmad
245 10 - TITLE STATEMENT
Title Characterization and thermostability study of invertase by Aspergillus niger in submerged culture /
Statement of responsibility, etc. Nurul Izzah Ahmad
260 ## - PUBLICATION, DISTRIBUTION, ETC.
Place of publication, distribution, etc. Kuantan, Pahang :
Name of publisher, distributor, etc. UMP,
Date of publication, distribution, etc. 2013
300 ## - PHYSICAL DESCRIPTION
Extent xiv, 41 p. :
Other physical details ill. ;
Dimensions 30 cm. +
Accompanying material 1 CD-ROM
502 ## - DISSERTATION NOTE
Dissertation note Project paper (Bachelor of Chemical Engineering (Biotechnology)) -- Universiti Malaysia Pahang – 2013
504 ## - BIBLIOGRAPHY, ETC. NOTE
Bibliography, etc. note Bibliography : p. 36-38
520 3# - SUMMARY, ETC.
Summary, etc. Invertase is a commercially important enzyme used for hydrolysis of sucrose. The hydrolysis of sucrose yields a mixture of glucose and fructose, or famous as name invert syrup, this enzyme was widely used in food and beverage industries. Objectives of this research are to study the pH and thermostability of invertase by Aspergillus niger, to study the enzyme kinetics of invertase and to study the effect of sucrose concentration during incubation towards invertase activity. A. niger produced high levels of invertase under culture conditions (potato dextrose agar) on fourth day of incubation at an optimum temperature 30OC, inoculum at 30OC at 250 rpm and using sucrose as a substrate by submerged fermentation (SmF) also with same culture conditions. Separation between enzyme and other cell was done by centrifugation and continued with study the pH and thermostability of enzyme by terminated by heating. Thermostability of enzyme were investigated by determining the enzymatic reaction subjected to 40OC, 45OC, 50OC, 55OC and 60OC. Michaelis-Menten parameters (Vmax and Km) were determined for four different sucrose concentration which are 0.2, 0.4, 0.6, 0.8 g/L. Result suggested that optimum pH is 5.0 and temperature is 55OC. While both Vmax and Km would increase at higher temperatures because temperature will alter the shape of enzyme by changing its ionic form at active site.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Invertase
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Enzymes
General subdivision Thermal properties
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Aspergillus niger
Holdings
Withdrawn status Lost status Damaged status Not for loan Home library Current library Date acquired Total checkouts Full call number Barcode Date last seen Copy number Price effective from Koha item type
  Not lost   Not for loan UMPLIB GAMBANG UMPLIB GAMBANG 04/09/2019   QD321 .I99 2013 rs Bc. 0000074731 04/09/2019 1 04/09/2019 Final Year Report
  Not lost   Not for loan UMPLIB GAMBANG UMPLIB GAMBANG 04/09/2019   CD 7065 | QD321 .I99 2013 rs Bc. 0000074732 04/09/2019 1 04/09/2019 Final Year Report

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