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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, Murad, Abdul Munir Abdul, Rabu, Amir, Bakar, Farah Diba Abu, Klappa, Peter, Illias, Rosli Md. (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 0141-5492. E-ISSN 1573-6776. (doi:10.1007/s10529-011-0517-8) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:64986)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
https://doi.org/10.1007/s10529-011-0517-8

Abstract

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.

Item Type: Article
DOI/Identification number: 10.1007/s10529-011-0517-8
Subjects: Q Science
Q Science > QR Microbiology
Divisions: Faculties > Sciences > School of Biosciences
Faculties > Sciences > School of Biosciences > Protein Science Group
Depositing User: Peter Klappa
Date Deposited: 05 Dec 2017 12:37 UTC
Last Modified: 29 May 2019 19:58 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/64986 (The current URI for this page, for reference purposes)
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