Cloning and expression of Clostridium stercorarium cellulase genes in Escherichia coli

Wolfgang H. Schwarz; Sigrid Jauris; Monika Kouba; Karin Bronnenmeier; Walter L. Staudenbauer

doi:10.1007/BF01026642

Cloning and expression of Clostridium stercorarium cellulase genes in Escherichia coli

Wolfgang H. Schwarz, Sigrid Jauris, Monika Kouba, Karin Bronnenmeier, Walter L. Staudenbauer

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Technische Universität München

Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

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Abstract

A genomic library of the cellulolytic thermophile Clostridium stercorarium NCIB 11745 was constructed in Escherichia coli using the cosmid vector pHC79. Recombinant clones expressing cellulase components were identified by screening for hydrolysis of carboxymethyl cellulose (CMC), 4-methylumbelliferyl-β-D-cellobioside, and 4-methylumbelliferyl-β-glucoside. Analysis of substrate specificity and restriction endonuclease mapping revealed three groups of clones carrying genes for an endo-β-1,4-glucanase (celZ), a β-cellobiosidase (celX), and a β-glucosidase (bglZ), respectively. All three enzymes were capable of degrading cellodextrins. Furthermore, the celZ gene product was active on microcrystalline cellulose (Avicel), while the bglZ β-glucosidase showed cellobiase activity.

Originalsprache	Englisch
Seiten (von - bis)	461-466
Seitenumfang	6
Fachzeitschrift	Biotechnology Letters
Jahrgang	11
Ausgabenummer	7
DOIs	https://doi.org/10.1007/BF01026642
Publikationsstatus	Veröffentlicht - Juli 1989

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title = "Cloning and expression of Clostridium stercorarium cellulase genes in Escherichia coli",

abstract = "A genomic library of the cellulolytic thermophile Clostridium stercorarium NCIB 11745 was constructed in Escherichia coli using the cosmid vector pHC79. Recombinant clones expressing cellulase components were identified by screening for hydrolysis of carboxymethyl cellulose (CMC), 4-methylumbelliferyl-β-D-cellobioside, and 4-methylumbelliferyl-β-glucoside. Analysis of substrate specificity and restriction endonuclease mapping revealed three groups of clones carrying genes for an endo-β-1,4-glucanase (celZ), a β-cellobiosidase (celX), and a β-glucosidase (bglZ), respectively. All three enzymes were capable of degrading cellodextrins. Furthermore, the celZ gene product was active on microcrystalline cellulose (Avicel), while the bglZ β-glucosidase showed cellobiase activity.",

author = "Schwarz, {Wolfgang H.} and Sigrid Jauris and Monika Kouba and Karin Bronnenmeier and Staudenbauer, {Walter L.}",

year = "1989",

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doi = "10.1007/BF01026642",

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T1 - Cloning and expression of Clostridium stercorarium cellulase genes in Escherichia coli

AU - Schwarz, Wolfgang H.

AU - Jauris, Sigrid

AU - Kouba, Monika

AU - Bronnenmeier, Karin

AU - Staudenbauer, Walter L.

PY - 1989/7

Y1 - 1989/7

N2 - A genomic library of the cellulolytic thermophile Clostridium stercorarium NCIB 11745 was constructed in Escherichia coli using the cosmid vector pHC79. Recombinant clones expressing cellulase components were identified by screening for hydrolysis of carboxymethyl cellulose (CMC), 4-methylumbelliferyl-β-D-cellobioside, and 4-methylumbelliferyl-β-glucoside. Analysis of substrate specificity and restriction endonuclease mapping revealed three groups of clones carrying genes for an endo-β-1,4-glucanase (celZ), a β-cellobiosidase (celX), and a β-glucosidase (bglZ), respectively. All three enzymes were capable of degrading cellodextrins. Furthermore, the celZ gene product was active on microcrystalline cellulose (Avicel), while the bglZ β-glucosidase showed cellobiase activity.

AB - A genomic library of the cellulolytic thermophile Clostridium stercorarium NCIB 11745 was constructed in Escherichia coli using the cosmid vector pHC79. Recombinant clones expressing cellulase components were identified by screening for hydrolysis of carboxymethyl cellulose (CMC), 4-methylumbelliferyl-β-D-cellobioside, and 4-methylumbelliferyl-β-glucoside. Analysis of substrate specificity and restriction endonuclease mapping revealed three groups of clones carrying genes for an endo-β-1,4-glucanase (celZ), a β-cellobiosidase (celX), and a β-glucosidase (bglZ), respectively. All three enzymes were capable of degrading cellodextrins. Furthermore, the celZ gene product was active on microcrystalline cellulose (Avicel), while the bglZ β-glucosidase showed cellobiase activity.

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JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 7

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Cloning and expression of Clostridium stercorarium cellulase genes in Escherichia coli

Abstract

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