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A mutant l-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli

l-Asparaginase II signal peptide was used for the secretion of recombinant cyclodextrin glucanotransferase (CGTase) into the periplasmic space of E. coli. Despite its predominant localisation in the periplasm, CGTase activity was also detected in the extracellular medium, followed by cell lysis. Fiv...

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Main Authors: Ismail, Noor Faizah, Hamdan, Salehhuddin, Mahadi, Nor Muhammad, Abdul Murad, Abdul Munir, Rabu, Amir, Abu Bakar, Farah Diba, Klappa, Peter, Md. Illias, Rosli
Format: Article
Published: Springer Science+Business Media B.V. 2011
Subjects:
QH301 Biology
Online Access:http://eprints.utm.my/id/eprint/28580/
http://dx.doi.org/10.1007/s10529-011-0517-8
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spelling my.utm.285802019-10-31T10:10:06Z http://eprints.utm.my/id/eprint/28580/ A mutant l-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli Ismail, Noor Faizah Hamdan, Salehhuddin Mahadi, Nor Muhammad Abdul Murad, Abdul Munir Rabu, Amir Abu Bakar, Farah Diba Klappa, Peter Md. Illias, Rosli QH301 Biology l-Asparaginase II signal peptide was used for the secretion of recombinant cyclodextrin glucanotransferase (CGTase) into the periplasmic space of E. coli. Despite its predominant localisation in the periplasm, CGTase activity was also detected in the extracellular medium, followed by cell lysis. Five mutant signal peptides were constructed to improve the periplasmic levels of CGTase. N1R3 is a mutated signal peptide with the number of positively charged amino acid residues in the n-region increased to a net charge of +5. This mutant peptide produced a 1.7-fold enhancement of CGTase activity in the periplasm and significantly decreased cell lysis to 7.8% of the wild-type level. The formation of intracellular inclusion bodies was also reduced when this mutated signal peptide was used as judged by SDS-PAGE. Therefore, these results provide evidence of a cost-effective means of expression of recombinant proteins in E. coli. Springer Science+Business Media B.V. 2011-05 Article PeerReviewed Ismail, Noor Faizah and Hamdan, Salehhuddin and Mahadi, Nor Muhammad and Abdul Murad, Abdul Munir and Rabu, Amir and Abu Bakar, Farah Diba and Klappa, Peter and Md. Illias, Rosli (2011) A mutant l-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli. Biotechnology Letters, 33 (5). pp. 999-1005. ISSN 1573-6776 http://dx.doi.org/10.1007/s10529-011-0517-8 DOI:0.1007/s10529-011-0517-8
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
topic QH301 Biology
spellingShingle QH301 Biology
Ismail, Noor Faizah
Hamdan, Salehhuddin
Mahadi, Nor Muhammad
Abdul Murad, Abdul Munir
Rabu, Amir
Abu Bakar, Farah Diba
Klappa, Peter
Md. Illias, Rosli
A mutant l-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli
description l-Asparaginase II signal peptide was used for the secretion of recombinant cyclodextrin glucanotransferase (CGTase) into the periplasmic space of E. coli. Despite its predominant localisation in the periplasm, CGTase activity was also detected in the extracellular medium, followed by cell lysis. Five mutant signal peptides were constructed to improve the periplasmic levels of CGTase. N1R3 is a mutated signal peptide with the number of positively charged amino acid residues in the n-region increased to a net charge of +5. This mutant peptide produced a 1.7-fold enhancement of CGTase activity in the periplasm and significantly decreased cell lysis to 7.8% of the wild-type level. The formation of intracellular inclusion bodies was also reduced when this mutated signal peptide was used as judged by SDS-PAGE. Therefore, these results provide evidence of a cost-effective means of expression of recombinant proteins in E. coli.
format Article
author Ismail, Noor Faizah
Hamdan, Salehhuddin
Mahadi, Nor Muhammad
Abdul Murad, Abdul Munir
Rabu, Amir
Abu Bakar, Farah Diba
Klappa, Peter
Md. Illias, Rosli
author_facet Ismail, Noor Faizah
Hamdan, Salehhuddin
Mahadi, Nor Muhammad
Abdul Murad, Abdul Munir
Rabu, Amir
Abu Bakar, Farah Diba
Klappa, Peter
Md. Illias, Rosli
author_sort Ismail, Noor Faizah
title A mutant l-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli
title_short A mutant l-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli
title_full A mutant l-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli
title_fullStr A mutant l-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli
title_full_unstemmed A mutant l-asparaginase II signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli
title_sort mutant l-asparaginase ii signal peptide improves the secretion of recombinant cyclodextrin glucanotransferase and the viability of escherichia coli
publisher Springer Science+Business Media B.V.
publishDate 2011
url http://eprints.utm.my/id/eprint/28580/
http://dx.doi.org/10.1007/s10529-011-0517-8
_version_ 1651866580291682304
score 13.211869

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