Overproduction of an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" in Escherichia coli

Ernst Lüthi; Nila Bhana Jasmat; Peter L. Bergquist

doi:10.1007/BF00166783

Overproduction of an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" in Escherichia coli

Ernst Lüthi^*, Nila Bhana Jasmat, Peter L. Bergquist

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

The xynC gene coding for an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" was overexpressed in Escherichia coli strain RR28 by cloning the gene downstream from the lacZ promoter region of pUC18 (pNZ1447) or downstream from the temperature-inducible λp_rp_l promoters of pJLA602 (pNZ1600). The protein formed high molecular weight aggregates in induced cells of RR28/pNZ1600 but not in RR28/pNZ1447. The enzyme constituted up to 10% of the total cell protein and was located in the cytoplasmic fraction of RR28/pNZ1447. The acetyl esterase was most active at pH 6.0 and 70-75° C with a half-life of 64 h at 70° C and 30 h at 80° C, respectively.

Original language	English
Pages (from-to)	214-219
Number of pages	6
Journal	Applied Microbiology and Biotechnology
Volume	34
Issue number	2
DOIs	https://doi.org/10.1007/BF00166783
Publication status	Published - Nov 1990
Externally published	Yes

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title = "Overproduction of an acetylxylan esterase from the extreme thermophile {"}Caldocellum saccharolyticum{"} in Escherichia coli",

abstract = "The xynC gene coding for an acetylxylan esterase from the extreme thermophile {"}Caldocellum saccharolyticum{"} was overexpressed in Escherichia coli strain RR28 by cloning the gene downstream from the lacZ promoter region of pUC18 (pNZ1447) or downstream from the temperature-inducible λprpl promoters of pJLA602 (pNZ1600). The protein formed high molecular weight aggregates in induced cells of RR28/pNZ1600 but not in RR28/pNZ1447. The enzyme constituted up to 10% of the total cell protein and was located in the cytoplasmic fraction of RR28/pNZ1447. The acetyl esterase was most active at pH 6.0 and 70-75° C with a half-life of 64 h at 70° C and 30 h at 80° C, respectively.",

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T1 - Overproduction of an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" in Escherichia coli

AU - Lüthi, Ernst

AU - Jasmat, Nila Bhana

AU - Bergquist, Peter L.

PY - 1990/11

Y1 - 1990/11

N2 - The xynC gene coding for an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" was overexpressed in Escherichia coli strain RR28 by cloning the gene downstream from the lacZ promoter region of pUC18 (pNZ1447) or downstream from the temperature-inducible λprpl promoters of pJLA602 (pNZ1600). The protein formed high molecular weight aggregates in induced cells of RR28/pNZ1600 but not in RR28/pNZ1447. The enzyme constituted up to 10% of the total cell protein and was located in the cytoplasmic fraction of RR28/pNZ1447. The acetyl esterase was most active at pH 6.0 and 70-75° C with a half-life of 64 h at 70° C and 30 h at 80° C, respectively.

AB - The xynC gene coding for an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" was overexpressed in Escherichia coli strain RR28 by cloning the gene downstream from the lacZ promoter region of pUC18 (pNZ1447) or downstream from the temperature-inducible λprpl promoters of pJLA602 (pNZ1600). The protein formed high molecular weight aggregates in induced cells of RR28/pNZ1600 but not in RR28/pNZ1447. The enzyme constituted up to 10% of the total cell protein and was located in the cytoplasmic fraction of RR28/pNZ1447. The acetyl esterase was most active at pH 6.0 and 70-75° C with a half-life of 64 h at 70° C and 30 h at 80° C, respectively.

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ER -

Overproduction of an acetylxylan esterase from the extreme thermophile "Caldocellum saccharolyticum" in Escherichia coli

Abstract

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