Effect of freeze and thaw cycle and incubation period on the solubilisation of inclusion body protein / (Record no. 7673)

MARC details
000 -LEADER
fixed length control field 03607ntm a2200373 i 4500
001 - CONTROL NUMBER
control field vtls000102809
003 - CONTROL NUMBER IDENTIFIER
control field KUKTEM
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20251117113359.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 180118s2017 my da f a m 000 0 eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number THE0000981(Local)
039 #9 - LEVEL OF BIBLIOGRAPHIC CONTROL AND CODING DETAIL [OBSOLETE]
Level of rules in bibliographic description 201905241626
Level of effort used to assign nonsubject heading access points nazirah
Level of effort used to assign subject headings 201802081544
Level of effort used to assign classification fateeha
Level of effort used to assign subject headings 201802021152
Level of effort used to assign classification fateeha
Level of effort used to assign subject headings 201801231143
Level of effort used to assign classification fateeha
-- 201801181553
-- fateeha
040 ## - CATALOGING SOURCE
Original cataloging agency UMP
Language of cataloging eng
Transcribing agency UMP
Description conventions rda
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) FKKSA .N87 2017 r Bc.
100 0# - MAIN ENTRY--PERSONAL NAME
Personal name Nursyahira Mohd Rafi,
Relator term author.
245 10 - TITLE STATEMENT
Title Effect of freeze and thaw cycle and incubation period on the solubilisation of inclusion body protein /
Statement of responsibility, etc. Nursyahira Mohd Rafi
264 #1 - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE
Place of production, publication, distribution, manufacture Kuantan, Pahang :
Name of producer, publisher, distributor, manufacturer UMP,
Date of production, publication, distribution, manufacture, or copyright notice 2017
264 #4 - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE
Date of production, publication, distribution, manufacture, or copyright notice © 2017
300 ## - PHYSICAL DESCRIPTION
Extent xiii, 70 pages :
Other physical details illustrations (some color), charts ;
Dimensions 30 cm. +
Accompanying material 1 CD-ROM
336 ## - CONTENT TYPE
Content type term text
Source rdacontent
336 ## - CONTENT TYPE
Content type term text
Source rdacontent
337 ## - MEDIA TYPE
Media type term unmediated
Source rdamedia
337 ## - MEDIA TYPE
Media type term computer
Source rdamedia
338 ## - CARRIER TYPE
Carrier type term volume
Source rdacarrier
338 ## - CARRIER TYPE
Carrier type term computer disc
Source rdacarrier
347 ## - DIGITAL FILE CHARACTERISTICS
File type text file
Encoding format PDF
Source rda
500 ## - GENERAL NOTE
General note Faculty of Chemical & Natural Resources Engineering
502 ## - DISSERTATION NOTE
Dissertation note Project Paper (Bachelors of Chemical Engineering) -- Universiti Malaysia Pahang – 2017
504 ## - BIBLIOGRAPHY, ETC. NOTE
Bibliography, etc. note Includes bibliographical references
520 3# - SUMMARY, ETC.
Summary, etc. Overexpression of recombinant protein in bacteria result in the formation of inactive protein. These inactive proteins associate forming insoluble protein aggregates which is referring to inclusion bodies (IBs). Generally, IBs are pure and the aggregated protein inside it has native-like secondary structure which is a bioactive protein. To recover the insoluble and active protein is a major problem encountered. Solubilisation does play a crucial role by unfolded the protein and thus help it to refold properly so that functional bioactive protein can be recovered. Example of mild solubilisation method using low concentration of urea and combine with freeze and thaw method has been proven to increase the efficiency of the recovering of bioactive protein. For freeze and thaw process there are factors that affect the overall process which are freezing incubation period and number of process cycle. Incubation period affect the process by determining the amount of stress needed to be applied so that unfolding process can occur. Number of cycle does affect the protein stability in terms of the occurrence of protein degradation probability. Thus the objective of this research is to investigate effect of freeze and thaw cycle an incubation period on the solubilisation of IBs. For incubation period the experiment was conducted between 1 to 4 days whereas for freeze and thaw cycle experiment conducted between cycle 1 to 4. Moreover, the performance of these two parameters were analysed using native-polyacrylamide gel electrophoresis (n-PAGE) to determine the functional for enhance green fluorescent protein (EGFP) amount and Bradford assay to determine the total protein amount. In this study, incubation period did affected the performance of solubilisation rate in which the IBs being solubilised and then proceed for refolding process and has been proven achieved active form of EGFP. For number of process cycle, it did not affect the solubilisation rate on determining the amount of functional EGFP recovered.
610 20 - SUBJECT ADDED ENTRY--CORPORATE NAME
Corporate name or jurisdiction name as entry element Faculty of Chemical & Natural Resources Engineering
General subdivision Dissertations
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Universities and Colleges
General subdivision Dissertations
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Theses
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   FKKSA .N87 2017 r Bc. 0000122138 04/09/2019 1 04/09/2019 Final Year Report
  Not lost   Not for loan UMPLIB GAMBANG UMPLIB GAMBANG 04/09/2019   CD 11149 | FKKSA .N87 2017 r Bc. 0000122139 04/09/2019 1 04/09/2019 Final Year Report

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