MARC details
| 000 -LEADER |
| fixed length control field |
03181ntm a2200337 i 4500 |
| 003 - CONTROL NUMBER IDENTIFIER |
| control field |
MY-KuUP |
| 005 - DATE AND TIME OF LATEST TRANSACTION |
| control field |
20260713174452.0 |
| 006 - FIXED-LENGTH DATA ELEMENTS--ADDITIONAL MATERIAL CHARACTERISTICS |
| fixed length control field |
t|||||r|||| 000 0 |
| 007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION |
| fixed length control field |
ta |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION |
| fixed length control field |
260713t20252025my a|||fr|||| 000 0 eng d |
| 020 ## - INTERNATIONAL STANDARD BOOK NUMBER |
| International Standard Book Number |
THE0010724 (Local) |
| Qualifying information |
Hardback |
| 040 ## - CATALOGING SOURCE |
| Original cataloging agency |
UMPSA |
| Language of cataloging |
eng |
| Transcribing agency |
UMPSA |
| Description conventions |
rda |
| 090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN) |
| Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) |
FTKKP .Y37 2025 r Bc. |
| 100 1# - MAIN ENTRY--PERSONAL NAME |
| Personal name |
Yashini Devi A/P Subramaniam, , , |
| Relator term |
author. |
| 245 10 - TITLE STATEMENT |
| Title |
Laccase immobilization onto oxidized bacterial cellulose: the effect of oxidant and its oxidation degree analysis / |
| Statement of responsibility, etc. |
Yashini Devi A/P Subramaniam |
| 264 #1 - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE |
| Place of production, publication, distribution, manufacture |
Kuantan, Pahang : |
| Name of producer, publisher, distributor, manufacturer |
UMPSA, |
| Date of production, publication, distribution, manufacture, or copyright notice |
2025 |
| 264 #4 - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE |
| Date of production, publication, distribution, manufacture, or copyright notice |
© 2025 |
| 300 ## - PHYSICAL DESCRIPTION |
| Extent |
xv, 58 pages : |
| Other physical details |
illustrations ; |
| 336 ## - CONTENT TYPE |
| Source |
rdacontent |
| Content type term |
text |
| 337 ## - MEDIA TYPE |
| Source |
rdamedia |
| Media type term |
unmediated |
| 338 ## - CARRIER TYPE |
| Source |
rdacarrier |
| Carrier type term |
volume |
| 347 ## - DIGITAL FILE CHARACTERISTICS |
| Source |
rda |
| File type |
text file |
| Encoding format |
PDF |
| 500 ## - GENERAL NOTE |
| General note |
Faculty of Chemical and Process Engineering Technology |
| 502 ## - DISSERTATION NOTE |
| Dissertation note |
Final Year Report (Bachelor of Chemical Engineering ) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2025 |
| 504 ## - BIBLIOGRAPHY, ETC. NOTE |
| Bibliography, etc. note |
Include bibliographical reference |
| 520 3# - SUMMARY, ETC. |
| Summary, etc. |
Laccases, a subgroup of multicopper oxidases, play a crucial role in biotechnological applications but face limitations such as low stability, poor reusability, and recovery challenges. This study investigates the effects of oxidant to Bacterial Cellulose (BC) weight ratio and sodium periodate (NaIO4) concentration on oxidation degree (OD) and laccase immobilization efficiency to determine best condition for enzyme stability and activity. The results indicate that increasing the oxidant to BC ratio from 0.02:1 to 0.06:1 led to a gradual increase in OD, peaking at 12.3%, while further increments resulted in over oxidation, causing structural degradation and reduced immobilization efficiency. Similarly, NaIO4 concentrations between 0.2% and 0.6% improved enzyme binding by enhancing aldehyde functionalities, but concentrations beyond 0.6% led to excessive oxidation and mass loss, negatively impacting enzyme stability. Under best condition of 0.06:1 oxidant to BC ratio and 0.6% NaIO4 concentration, Oxidized Bacterial Cellulose (OxBC) demonstrated superior immobilization performance, achieving a laccase activity of 0.04 U, with a recovered activity of 0.2%, and bound laccase of 17.0 U/g of support. The aldehyde groups introduced through oxidation facilitated stable covalent binding, significantly improving enzyme retention and reusability. Compared to native BC, OxBC exhibited enhanced immobilization efficiency and structural integrity, making it a promising candidate for industrial enzyme applications. This study provides insight into the relationship between oxidation parameters and immobilization efficiency, contributing to the development of more effective and sustainable enzyme immobilization systems. Future research should explore long term operational stability and scalability of OxBC based immobilization for broader industrial and environmental applications. |
| 610 20 - SUBJECT ADDED ENTRY--CORPORATE NAME |
| Corporate name or jurisdiction name as entry element |
Faculty of Chemical and Process Engineering Technology |
| 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 |
| General subdivision |
Dissertations |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) |
| Source of classification or shelving scheme |
Library of Congress Classification |
| Koha item type |
Final Year Report |