Response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (PGMA)
Immobilization of lipase enzyme originated from wheat germ on nylon -6- grafted with PGMA was studied. Face centered central composite design (FCCCD) under response surface methodology (RSM) was used to design the experiment in order to distinguish the optimum immobilization conditions for highest e...
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iium-598222017-12-07T04:02:59Z http://irep.iium.edu.my/59822/ Response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (PGMA) Alkhatib, Ma'an Fahmi Rashid Bahrudin, Nik Adlin Mohd. Salleh, Hamzah Nasef, Mohamed Mahmoud TA164 Bioengineering TP155 Chemical engineering Immobilization of lipase enzyme originated from wheat germ on nylon -6- grafted with PGMA was studied. Face centered central composite design (FCCCD) under response surface methodology (RSM) was used to design the experiment in order to distinguish the optimum immobilization conditions for highest enzyme activity and to study the interactions between the various parameters. The polymer was activated with diethyl amine/ethanol to introduce amine functional group to facilitate covalent bonding with the enzyme. The immobilization conditions were 2-10 h for immobilization time; 6-8 for pH and 0.4-1.0 mg/ml for enzyme concentration. ANOVA revealed that optimum lipase activity of 0.287 U/ml was achieved at immobilization time of 5 h, pH of 6 and 1.0 mg/ml for enzyme concentration. Kinetics studies of both immobilized and free lipase were conducted to study the effect of immobilization on enzyme behavior. Amongst the tested models, Lineweaver-Burk Plot best fitted the data with Vmax and Km values of 0.024 mM/min and 10.321 mM for free lipase and 0.012 and 7.250 for immobilized lipase, respectively. The lower value of Km for immobilized lipase enzyme compared to free enzyme indicates a stronger and more efficient binding of substrate. Vmax on the other hand exemplify how quick the enzyme catalyzes the reaction. Lower Vmax for immobilized enzyme designates lower enzyme rate. IMDD 2017-11-08 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/59822/1/59822_Response%20Surface%20Methodology.pdf Alkhatib, Ma'an Fahmi Rashid and Bahrudin, Nik Adlin and Mohd. Salleh, Hamzah and Nasef, Mohamed Mahmoud (2017) Response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (PGMA). In: 3rd International Symposium on Materials and Sustainable Development (ISMSD2017), 7th-8th November 2017, Boumerdes, Algeria. https://cimdd2017.sciencesconf.org/ |
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TA164 Bioengineering TP155 Chemical engineering Alkhatib, Ma'an Fahmi Rashid Bahrudin, Nik Adlin Mohd. Salleh, Hamzah Nasef, Mohamed Mahmoud Response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (PGMA) |
description |
Immobilization of lipase enzyme originated from wheat germ on nylon -6- grafted with PGMA was studied. Face centered central composite design (FCCCD) under response surface methodology (RSM) was used to design the experiment in order to distinguish the optimum immobilization conditions for highest enzyme activity and to study the interactions between the various parameters. The polymer was activated with diethyl amine/ethanol to introduce amine functional group to facilitate covalent bonding with the enzyme. The immobilization conditions were 2-10 h for immobilization time; 6-8 for pH and 0.4-1.0 mg/ml for enzyme concentration. ANOVA revealed that optimum lipase activity of 0.287 U/ml was achieved at immobilization time of 5 h, pH of 6 and 1.0 mg/ml for enzyme concentration. Kinetics studies of both immobilized and free lipase were conducted to study the effect of immobilization on enzyme behavior. Amongst the tested models, Lineweaver-Burk Plot best fitted the data with Vmax and Km values of 0.024 mM/min and 10.321 mM for free lipase and 0.012 and 7.250 for immobilized lipase, respectively. The lower value of Km for immobilized lipase enzyme compared to free enzyme indicates a stronger and more efficient binding of substrate. Vmax on the other hand exemplify how quick the enzyme catalyzes the reaction. Lower Vmax for immobilized enzyme designates lower enzyme rate. |
format |
Conference or Workshop Item |
author |
Alkhatib, Ma'an Fahmi Rashid Bahrudin, Nik Adlin Mohd. Salleh, Hamzah Nasef, Mohamed Mahmoud |
author_facet |
Alkhatib, Ma'an Fahmi Rashid Bahrudin, Nik Adlin Mohd. Salleh, Hamzah Nasef, Mohamed Mahmoud |
author_sort |
Alkhatib, Ma'an Fahmi Rashid |
title |
Response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (PGMA) |
title_short |
Response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (PGMA) |
title_full |
Response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (PGMA) |
title_fullStr |
Response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (PGMA) |
title_full_unstemmed |
Response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (PGMA) |
title_sort |
response surface methodology for optimization of lipase immobilization conditions on nanofibers grafted with polyglycidyl methachrylate (pgma) |
publisher |
IMDD |
publishDate |
2017 |
url |
http://irep.iium.edu.my/59822/ http://irep.iium.edu.my/59822/ http://irep.iium.edu.my/59822/1/59822_Response%20Surface%20Methodology.pdf |
first_indexed |
2023-09-18T21:24:47Z |
last_indexed |
2023-09-18T21:24:47Z |
_version_ |
1777412119279435776 |