author_facet Alkhatib, Maan
Bahrudin, Nik Adlin
SALLEH, HAMZAH M.
Nasef, Mohamed M. E.
Ting, Teo M.
Alkhatib, Maan
Bahrudin, Nik Adlin
SALLEH, HAMZAH M.
Nasef, Mohamed M. E.
Ting, Teo M.
author Alkhatib, Maan
Bahrudin, Nik Adlin
SALLEH, HAMZAH M.
Nasef, Mohamed M. E.
Ting, Teo M.
spellingShingle Alkhatib, Maan
Bahrudin, Nik Adlin
SALLEH, HAMZAH M.
Nasef, Mohamed M. E.
Ting, Teo M.
IIUM Engineering Journal
LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
Applied Mathematics
General Engineering
General Chemical Engineering
General Computer Science
author_sort alkhatib, maan
spelling Alkhatib, Maan Bahrudin, Nik Adlin SALLEH, HAMZAH M. Nasef, Mohamed M. E. Ting, Teo M. 2289-7860 1511-788X IIUM Press Applied Mathematics General Engineering General Chemical Engineering General Computer Science http://dx.doi.org/10.31436/iiumej.v20i1.1002 <jats:p>ABSTRACT: Lipase enzyme originated from wheat germ was immobilized on nylon -6- grafted with polyglycidyl methachrylate (PGMA). The immobilization of enzyme experiments were designed and studied using face centred central composite design (FCCCD) under response surface methodology (RSM). Prior to immobilization, the polymer was activated with diethyl amine/ethanol to introduce an amine functional group to facilitate covalent bonding with the enzyme. The immobilized and free enzymes were characterized for effect of temperature and pH on enzyme activity, stability, storage and reusability as well as kinetics studies. 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. The optimum temperatures and pH for immobilized and free enzymes were 45 °C and 35 °C, and 8 and 7, respectively. The immobilized enzyme showed higher stability compared to free enzyme. The immobilized enzyme retained 18% of its activity after being recycled 8 times. In a storage stability test, immobilized lipase was able to retain 70% of its activity after being stored for 30 days, while free enzyme activity dropped to 15 % after 20 days of storage. ABSTRAK:Enzim Lipase telah dihasilkan daripada mikroorganisma pegun gandum di atas nilon -6- dan digraf bersama poliglisidel methakrilet (PGMA). Enzim pegun ini direka dan dikaji secara eksperimen menggunakan reka bentuk campuran pusat pada permukaan (FCCCD) di bawah kaedah tindak balas permukaan (RSM). Sebelum menjadi pegun, polimer ini telah diaktifkan dengan dietil amine/ethanol bagi menghasilkan kumpulan fungsi amine bagi membantu ikatan kovalen atom pada enzim. Enzim pegun dan bebas ini telah dikategorikan mengikut kesan enzim ke atas suhu, aktiviti enzim ke atas kesan pH, kestabilan, keboleh-simpanan dan keboleh-gunaan balik, serta ujian tindak balas kinetik. ANOVA membuktikan bahawa aktiviti optimum enzim lipase ini adalah sebanyak 0.287 U/ml telah terhasil selama 5 jam pegun, pada pH 6 dan kepekatan enzim sebanyak 1.0 mg/ml. Suhu dan pH optimum, pada enzim pegun dan enzim bebas ini adalah pada 45 °C dan 35 °C, dan pH 8 dan 7, masing-masing. Enzim pegun ini menunjukkan lebih stabil daripada enzim bebas. Enzim pegun dilihat kekal 18% daripada aktivitinya selepas 8 kali ulangan. Melalui ujian kestabilan simpanan, enzim lipase pegun dapat mengekalkan 70% daripada aktivinya selepas disimpan selama 30 hari, manakala aktiviti enzim bebas telah menurun kepada 15% selepas 20 hari dalam simpanan.</jats:p> LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE IIUM Engineering Journal
doi_str_mv 10.31436/iiumej.v20i1.1002
facet_avail Online
Free
finc_class_facet Mathematik
format ElectronicArticle
fullrecord blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMzE0MzYvaWl1bWVqLnYyMGkxLjEwMDI
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMzE0MzYvaWl1bWVqLnYyMGkxLjEwMDI
institution DE-Gla1
DE-Zi4
DE-15
DE-Pl11
DE-Rs1
DE-105
DE-14
DE-Ch1
DE-L229
DE-D275
DE-Bn3
DE-Brt1
DE-Zwi2
DE-D161
imprint IIUM Press, 2019
imprint_str_mv IIUM Press, 2019
issn 2289-7860
1511-788X
issn_str_mv 2289-7860
1511-788X
language Undetermined
mega_collection IIUM Press (CrossRef)
match_str alkhatib2019lipaseimmobilizationonfibersgraftedwithpolyglycidylmethachrylate
publishDateSort 2019
publisher IIUM Press
recordtype ai
record_format ai
series IIUM Engineering Journal
source_id 49
title LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_unstemmed LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_full LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_fullStr LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_full_unstemmed LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_short LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_sort lipase immobilization on fibers grafted with polyglycidyl methachrylate
topic Applied Mathematics
General Engineering
General Chemical Engineering
General Computer Science
url http://dx.doi.org/10.31436/iiumej.v20i1.1002
publishDate 2019
physical 12-23
description <jats:p>ABSTRACT: Lipase enzyme originated from wheat germ was immobilized on nylon -6- grafted with polyglycidyl methachrylate (PGMA). The immobilization of enzyme experiments were designed and studied using face centred central composite design (FCCCD) under response surface methodology (RSM). Prior to immobilization, the polymer was activated with diethyl amine/ethanol to introduce an amine functional group to facilitate covalent bonding with the enzyme. The immobilized and free enzymes were characterized for effect of temperature and pH on enzyme activity, stability, storage and reusability as well as kinetics studies. 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. The optimum temperatures and pH for immobilized and free enzymes were 45 °C and 35 °C, and 8 and 7, respectively. The immobilized enzyme showed higher stability compared to free enzyme. The immobilized enzyme retained 18% of its activity after being recycled 8 times. In a storage stability test, immobilized lipase was able to retain 70% of its activity after being stored for 30 days, while free enzyme activity dropped to 15 % after 20 days of storage. ABSTRAK:Enzim Lipase telah dihasilkan daripada mikroorganisma pegun gandum di atas nilon -6- dan digraf bersama poliglisidel methakrilet (PGMA). Enzim pegun ini direka dan dikaji secara eksperimen menggunakan reka bentuk campuran pusat pada permukaan (FCCCD) di bawah kaedah tindak balas permukaan (RSM). Sebelum menjadi pegun, polimer ini telah diaktifkan dengan dietil amine/ethanol bagi menghasilkan kumpulan fungsi amine bagi membantu ikatan kovalen atom pada enzim. Enzim pegun dan bebas ini telah dikategorikan mengikut kesan enzim ke atas suhu, aktiviti enzim ke atas kesan pH, kestabilan, keboleh-simpanan dan keboleh-gunaan balik, serta ujian tindak balas kinetik. ANOVA membuktikan bahawa aktiviti optimum enzim lipase ini adalah sebanyak 0.287 U/ml telah terhasil selama 5 jam pegun, pada pH 6 dan kepekatan enzim sebanyak 1.0 mg/ml. Suhu dan pH optimum, pada enzim pegun dan enzim bebas ini adalah pada 45 °C dan 35 °C, dan pH 8 dan 7, masing-masing. Enzim pegun ini menunjukkan lebih stabil daripada enzim bebas. Enzim pegun dilihat kekal 18% daripada aktivitinya selepas 8 kali ulangan. Melalui ujian kestabilan simpanan, enzim lipase pegun dapat mengekalkan 70% daripada aktivinya selepas disimpan selama 30 hari, manakala aktiviti enzim bebas telah menurun kepada 15% selepas 20 hari dalam simpanan.</jats:p>
container_issue 1
container_start_page 12
container_title IIUM Engineering Journal
container_volume 20
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
_version_ 1792333567606390797
geogr_code not assigned
last_indexed 2024-03-01T14:14:49.593Z
geogr_code_person not assigned
openURL url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=LIPASE+IMMOBILIZATION+ON+FIBERS+GRAFTED+WITH+POLYGLYCIDYL+METHACHRYLATE&rft.date=2019-06-01&genre=article&issn=1511-788X&volume=20&issue=1&spage=12&epage=23&pages=12-23&jtitle=IIUM+Engineering+Journal&atitle=LIPASE+IMMOBILIZATION+ON+FIBERS+GRAFTED+WITH+POLYGLYCIDYL+METHACHRYLATE&aulast=Ting&aufirst=Teo+M.&rft_id=info%3Adoi%2F10.31436%2Fiiumej.v20i1.1002&rft.language%5B0%5D=und
SOLR
_version_ 1792333567606390797
author Alkhatib, Maan, Bahrudin, Nik Adlin, SALLEH, HAMZAH M., Nasef, Mohamed M. E., Ting, Teo M.
author_facet Alkhatib, Maan, Bahrudin, Nik Adlin, SALLEH, HAMZAH M., Nasef, Mohamed M. E., Ting, Teo M., Alkhatib, Maan, Bahrudin, Nik Adlin, SALLEH, HAMZAH M., Nasef, Mohamed M. E., Ting, Teo M.
author_sort alkhatib, maan
container_issue 1
container_start_page 12
container_title IIUM Engineering Journal
container_volume 20
description <jats:p>ABSTRACT: Lipase enzyme originated from wheat germ was immobilized on nylon -6- grafted with polyglycidyl methachrylate (PGMA). The immobilization of enzyme experiments were designed and studied using face centred central composite design (FCCCD) under response surface methodology (RSM). Prior to immobilization, the polymer was activated with diethyl amine/ethanol to introduce an amine functional group to facilitate covalent bonding with the enzyme. The immobilized and free enzymes were characterized for effect of temperature and pH on enzyme activity, stability, storage and reusability as well as kinetics studies. 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. The optimum temperatures and pH for immobilized and free enzymes were 45 °C and 35 °C, and 8 and 7, respectively. The immobilized enzyme showed higher stability compared to free enzyme. The immobilized enzyme retained 18% of its activity after being recycled 8 times. In a storage stability test, immobilized lipase was able to retain 70% of its activity after being stored for 30 days, while free enzyme activity dropped to 15 % after 20 days of storage. ABSTRAK:Enzim Lipase telah dihasilkan daripada mikroorganisma pegun gandum di atas nilon -6- dan digraf bersama poliglisidel methakrilet (PGMA). Enzim pegun ini direka dan dikaji secara eksperimen menggunakan reka bentuk campuran pusat pada permukaan (FCCCD) di bawah kaedah tindak balas permukaan (RSM). Sebelum menjadi pegun, polimer ini telah diaktifkan dengan dietil amine/ethanol bagi menghasilkan kumpulan fungsi amine bagi membantu ikatan kovalen atom pada enzim. Enzim pegun dan bebas ini telah dikategorikan mengikut kesan enzim ke atas suhu, aktiviti enzim ke atas kesan pH, kestabilan, keboleh-simpanan dan keboleh-gunaan balik, serta ujian tindak balas kinetik. ANOVA membuktikan bahawa aktiviti optimum enzim lipase ini adalah sebanyak 0.287 U/ml telah terhasil selama 5 jam pegun, pada pH 6 dan kepekatan enzim sebanyak 1.0 mg/ml. Suhu dan pH optimum, pada enzim pegun dan enzim bebas ini adalah pada 45 °C dan 35 °C, dan pH 8 dan 7, masing-masing. Enzim pegun ini menunjukkan lebih stabil daripada enzim bebas. Enzim pegun dilihat kekal 18% daripada aktivitinya selepas 8 kali ulangan. Melalui ujian kestabilan simpanan, enzim lipase pegun dapat mengekalkan 70% daripada aktivinya selepas disimpan selama 30 hari, manakala aktiviti enzim bebas telah menurun kepada 15% selepas 20 hari dalam simpanan.</jats:p>
doi_str_mv 10.31436/iiumej.v20i1.1002
facet_avail Online, Free
finc_class_facet Mathematik
format ElectronicArticle
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
geogr_code not assigned
geogr_code_person not assigned
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMzE0MzYvaWl1bWVqLnYyMGkxLjEwMDI
imprint IIUM Press, 2019
imprint_str_mv IIUM Press, 2019
institution DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161
issn 2289-7860, 1511-788X
issn_str_mv 2289-7860, 1511-788X
language Undetermined
last_indexed 2024-03-01T14:14:49.593Z
match_str alkhatib2019lipaseimmobilizationonfibersgraftedwithpolyglycidylmethachrylate
mega_collection IIUM Press (CrossRef)
physical 12-23
publishDate 2019
publishDateSort 2019
publisher IIUM Press
record_format ai
recordtype ai
series IIUM Engineering Journal
source_id 49
spelling Alkhatib, Maan Bahrudin, Nik Adlin SALLEH, HAMZAH M. Nasef, Mohamed M. E. Ting, Teo M. 2289-7860 1511-788X IIUM Press Applied Mathematics General Engineering General Chemical Engineering General Computer Science http://dx.doi.org/10.31436/iiumej.v20i1.1002 <jats:p>ABSTRACT: Lipase enzyme originated from wheat germ was immobilized on nylon -6- grafted with polyglycidyl methachrylate (PGMA). The immobilization of enzyme experiments were designed and studied using face centred central composite design (FCCCD) under response surface methodology (RSM). Prior to immobilization, the polymer was activated with diethyl amine/ethanol to introduce an amine functional group to facilitate covalent bonding with the enzyme. The immobilized and free enzymes were characterized for effect of temperature and pH on enzyme activity, stability, storage and reusability as well as kinetics studies. 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. The optimum temperatures and pH for immobilized and free enzymes were 45 °C and 35 °C, and 8 and 7, respectively. The immobilized enzyme showed higher stability compared to free enzyme. The immobilized enzyme retained 18% of its activity after being recycled 8 times. In a storage stability test, immobilized lipase was able to retain 70% of its activity after being stored for 30 days, while free enzyme activity dropped to 15 % after 20 days of storage. ABSTRAK:Enzim Lipase telah dihasilkan daripada mikroorganisma pegun gandum di atas nilon -6- dan digraf bersama poliglisidel methakrilet (PGMA). Enzim pegun ini direka dan dikaji secara eksperimen menggunakan reka bentuk campuran pusat pada permukaan (FCCCD) di bawah kaedah tindak balas permukaan (RSM). Sebelum menjadi pegun, polimer ini telah diaktifkan dengan dietil amine/ethanol bagi menghasilkan kumpulan fungsi amine bagi membantu ikatan kovalen atom pada enzim. Enzim pegun dan bebas ini telah dikategorikan mengikut kesan enzim ke atas suhu, aktiviti enzim ke atas kesan pH, kestabilan, keboleh-simpanan dan keboleh-gunaan balik, serta ujian tindak balas kinetik. ANOVA membuktikan bahawa aktiviti optimum enzim lipase ini adalah sebanyak 0.287 U/ml telah terhasil selama 5 jam pegun, pada pH 6 dan kepekatan enzim sebanyak 1.0 mg/ml. Suhu dan pH optimum, pada enzim pegun dan enzim bebas ini adalah pada 45 °C dan 35 °C, dan pH 8 dan 7, masing-masing. Enzim pegun ini menunjukkan lebih stabil daripada enzim bebas. Enzim pegun dilihat kekal 18% daripada aktivitinya selepas 8 kali ulangan. Melalui ujian kestabilan simpanan, enzim lipase pegun dapat mengekalkan 70% daripada aktivinya selepas disimpan selama 30 hari, manakala aktiviti enzim bebas telah menurun kepada 15% selepas 20 hari dalam simpanan.</jats:p> LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE IIUM Engineering Journal
spellingShingle Alkhatib, Maan, Bahrudin, Nik Adlin, SALLEH, HAMZAH M., Nasef, Mohamed M. E., Ting, Teo M., IIUM Engineering Journal, LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE, Applied Mathematics, General Engineering, General Chemical Engineering, General Computer Science
title LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_full LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_fullStr LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_full_unstemmed LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_short LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
title_sort lipase immobilization on fibers grafted with polyglycidyl methachrylate
title_unstemmed LIPASE IMMOBILIZATION ON FIBERS GRAFTED WITH POLYGLYCIDYL METHACHRYLATE
topic Applied Mathematics, General Engineering, General Chemical Engineering, General Computer Science
url http://dx.doi.org/10.31436/iiumej.v20i1.1002