Reusability and leakage of immobilized laccase enzyme

Laccase (EC 1.10.3.2, benzenediol: oxygen oxidoreductase), a copper containing enzyme which can catalyse the oxidation of various organic and inorganic substrates, is usually used to decolorize the wastewater effluent and render phenolic compounds to less toxic component. The objective of this resea...

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Main Author:	Lau Chin Yee, Cindy
Format:	Undergraduates Project Papers
Language:	English English English
Published:	2015
Subjects:	TP Chemical technology
Online Access:	http://umpir.ump.edu.my/id/eprint/11013/ http://umpir.ump.edu.my/id/eprint/11013/ http://umpir.ump.edu.my/id/eprint/11013/1/FKKSA%20-%20CINDY%20LAU%20CHIN%20YEE%20%28CD8966%29.pdf http://umpir.ump.edu.my/id/eprint/11013/2/FKKSA%20-%20CINDY%20LAU%20CHIN%20YEE%20%28CD8966%29%20CHAP%201.pdf http://umpir.ump.edu.my/id/eprint/11013/3/FKKSA%20-%20CINDY%20LAU%20CHIN%20YEE%20%28CD8966%29%20CHAP%203.pdf

id	ump-11013
recordtype	eprints
spelling	ump-110132015-11-02T01:10:17Z http://umpir.ump.edu.my/id/eprint/11013/ Reusability and leakage of immobilized laccase enzyme Lau Chin Yee, Cindy TP Chemical technology Laccase (EC 1.10.3.2, benzenediol: oxygen oxidoreductase), a copper containing enzyme which can catalyse the oxidation of various organic and inorganic substrates, is usually used to decolorize the wastewater effluent and render phenolic compounds to less toxic component. The objective of this research is to compare the reusability and leakage between entrapped and covalently bonded laccase enzymes. The reusability of immobilized laccase enzyme was studied by reacting a batch of immobilized laccase enzymes with ABTS repeatedly for 15 cycles. The study of the leakage of immobilized laccase enzyme was carried out by storing the immobilized laccase enzymes in acetate buffer solution for 32 days. The acetate buffer solution samples were taken and reacted with ABTS. The samples reacted with ABTS were analysed using a UV-Vis spectrophotometer at 415 nm. The absorbance readings were recorded and enzyme activities were calculated. The data collected showed that the retained enzyme activities of entrapped and covalently bonded enzyme after being reused for 15 cycles are 33.50% and 48.19% respectively. On the other hand, the leakages of entrapped and covalently bonded laccase enzyme after 32 days are 13.9 % and 14.46 % respectively. In conclusion, the covalently bonded laccase enzymes are more stable in terms of reusability and storage stability compared to entrapped laccase enzymes. 2015-01 Undergraduates Project Papers NonPeerReviewed application/pdf en http://umpir.ump.edu.my/id/eprint/11013/1/FKKSA%20-%20CINDY%20LAU%20CHIN%20YEE%20%28CD8966%29.pdf application/pdf en http://umpir.ump.edu.my/id/eprint/11013/2/FKKSA%20-%20CINDY%20LAU%20CHIN%20YEE%20%28CD8966%29%20CHAP%201.pdf application/pdf en http://umpir.ump.edu.my/id/eprint/11013/3/FKKSA%20-%20CINDY%20LAU%20CHIN%20YEE%20%28CD8966%29%20CHAP%203.pdf Lau Chin Yee, Cindy (2015) Reusability and leakage of immobilized laccase enzyme. Faculty of Chemical & Natural Resources Engineering, Universiti Malaysia Pahang. http://iportal.ump.edu.my/lib/item?id=chamo:91315&theme=UMP2
repository_type	Digital Repository
institution_category	Local University
institution	Universiti Malaysia Pahang
building	UMP Institutional Repository
collection	Online Access
language	English English English
topic	TP Chemical technology
spellingShingle	TP Chemical technology Lau Chin Yee, Cindy Reusability and leakage of immobilized laccase enzyme
description	Laccase (EC 1.10.3.2, benzenediol: oxygen oxidoreductase), a copper containing enzyme which can catalyse the oxidation of various organic and inorganic substrates, is usually used to decolorize the wastewater effluent and render phenolic compounds to less toxic component. The objective of this research is to compare the reusability and leakage between entrapped and covalently bonded laccase enzymes. The reusability of immobilized laccase enzyme was studied by reacting a batch of immobilized laccase enzymes with ABTS repeatedly for 15 cycles. The study of the leakage of immobilized laccase enzyme was carried out by storing the immobilized laccase enzymes in acetate buffer solution for 32 days. The acetate buffer solution samples were taken and reacted with ABTS. The samples reacted with ABTS were analysed using a UV-Vis spectrophotometer at 415 nm. The absorbance readings were recorded and enzyme activities were calculated. The data collected showed that the retained enzyme activities of entrapped and covalently bonded enzyme after being reused for 15 cycles are 33.50% and 48.19% respectively. On the other hand, the leakages of entrapped and covalently bonded laccase enzyme after 32 days are 13.9 % and 14.46 % respectively. In conclusion, the covalently bonded laccase enzymes are more stable in terms of reusability and storage stability compared to entrapped laccase enzymes.
format	Undergraduates Project Papers
author	Lau Chin Yee, Cindy
author_facet	Lau Chin Yee, Cindy
author_sort	Lau Chin Yee, Cindy
title	Reusability and leakage of immobilized laccase enzyme
title_short	Reusability and leakage of immobilized laccase enzyme
title_full	Reusability and leakage of immobilized laccase enzyme
title_fullStr	Reusability and leakage of immobilized laccase enzyme
title_full_unstemmed	Reusability and leakage of immobilized laccase enzyme
title_sort	reusability and leakage of immobilized laccase enzyme
publishDate	2015
url	http://umpir.ump.edu.my/id/eprint/11013/ http://umpir.ump.edu.my/id/eprint/11013/ http://umpir.ump.edu.my/id/eprint/11013/1/FKKSA%20-%20CINDY%20LAU%20CHIN%20YEE%20%28CD8966%29.pdf http://umpir.ump.edu.my/id/eprint/11013/2/FKKSA%20-%20CINDY%20LAU%20CHIN%20YEE%20%28CD8966%29%20CHAP%201.pdf http://umpir.ump.edu.my/id/eprint/11013/3/FKKSA%20-%20CINDY%20LAU%20CHIN%20YEE%20%28CD8966%29%20CHAP%203.pdf
first_indexed	2023-09-18T22:11:18Z
last_indexed	2023-09-18T22:11:18Z
_version_	1777415045142020096

Reusability and leakage of immobilized laccase enzyme

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