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Sökning: onr:"swepub:oai:lup.lub.lu.se:546d8c6f-1a9c-47b8-9b55-3605df3bb3e5" > Deletion of a cytot...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004022naa a2200373 4500
001oai:lup.lub.lu.se:546d8c6f-1a9c-47b8-9b55-3605df3bb3e5
003SwePub
008181114s2001 | |||||||||||000 ||eng|
0247 a https://lup.lub.lu.se/record/546d8c6f-1a9c-47b8-9b55-3605df3bb3e52 URI
0247 a https://doi.org/10.1007/s0025300005592 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
1001 a Wicher, K. B.u Lund University4 aut
2451 0a Deletion of a cytotoxic, N-terminal putative signal peptide results in a significant increase in production yields in Escherichia coli and improved specific activity of Cel12A from Rhodothermus marinus
264 1b Springer Science and Business Media LLC,c 2001
300 a 7 s.
520 a The thermostable cellulase Cel12A from Rhodothermus marinus was produced at extremely low levels when expressed in Escherichia coli and was cytotoxic to the cells. In addition, severe aggregation occurred when moderately high concentrations of the enzyme were heat-treated at 65°C, the growth optimum of R. marinus. Sequence analysis revealed that the catalytic module of this enzyme is preceded by a typical linker sequence and a highly hydrophobic putative signal peptide. Two deletion mutants lacking this hydrophobic region were cloned and successfully expressed in E. coli. These results indicated that the N-terminal putative signal peptide was responsible for the toxicity of the full-length enzyme in the host organism. This was further corroborated by cloning and expressing the hydrophobic N-terminal domain in E. coli, which resulted in extensive cell lysis. The deletion mutants, made up of either the catalytic module of Cel12A or the catalytic module and the putative linker sequence, were characterised and their properties compared to those of the full-length enzyme. The specific activity of the mutants was approximately threefold higher than that of the full-length enzyme. Both mutant proteins were highly thermostable, with half-lives exceeding 2 h at 90°C and unfolding temperatures up to 103°C.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
7001 a Abou-Hachem, M.u Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biot-mah
7001 a Halldórsdóttir, S.u University of Iceland4 aut
7001 a Thorbjarnadóttir, S. H.u University of Iceland4 aut
7001 a Eggertsson, G.u University of Iceland4 aut
7001 a Hreggvidsson, G. O.u University of Iceland4 aut
7001 a Nordberg Karlsson, E.u Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biot-eno
7001 a Holst, O.u Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biot-oho
7102 a Lund Universityb Bioteknik4 org
7730 t Applied Microbiology and Biotechnologyd : Springer Science and Business Media LLCg 55:5, s. 578-584q 55:5<578-584x 0175-7598x 1432-0614
8564 u http://dx.doi.org/10.1007/s002530000559y FULLTEXT
8564 8u https://lup.lub.lu.se/record/546d8c6f-1a9c-47b8-9b55-3605df3bb3e5
8564 8u https://doi.org/10.1007/s002530000559

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