Cold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis
peer reviewed The beta-galactosidase from the Antarctic gram-negative bacterium Pseudoalteromonas haloplanktis TAE 79 was purified to homogeneity. The nucleotide sequence and the NH(2)-terminal amino acid sequence of the purified enzyme indicate that the beta-galactosidase subunit is composed of 1,0...
Published in: | Applied and Environmental Microbiology |
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American Society for Microbiology
2001
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Online Access: | https://orbi.uliege.be/handle/2268/9845 https://orbi.uliege.be/bitstream/2268/9845/1/AEM_2001_betagal.pdf https://doi.org/10.1128/AEM.67.4.1529-1535.2001 |
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ftorbi:oai:orbi.ulg.ac.be:2268/9845 2024-04-21T07:48:53+00:00 Cold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis Hoyoux, A. Jennes, I. Dubois, P. Genicot, S. Dubail, F. François, Jean-Marie Baise, Etienne Feller, Georges Gerday, Charles 2001-04 https://orbi.uliege.be/handle/2268/9845 https://orbi.uliege.be/bitstream/2268/9845/1/AEM_2001_betagal.pdf https://doi.org/10.1128/AEM.67.4.1529-1535.2001 en eng American Society for Microbiology urn:issn:0099-2240 urn:issn:1098-5336 https://orbi.uliege.be/handle/2268/9845 info:hdl:2268/9845 https://orbi.uliege.be/bitstream/2268/9845/1/AEM_2001_betagal.pdf doi:10.1128/AEM.67.4.1529-1535.2001 scopus-id:2-s2.0-0035319361 info:pmid:11282601 open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess Applied and Environmental Microbiology, 67 (4), 1529-35 (2001-04) Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire journal article http://purl.org/coar/resource_type/c_6501 info:eu-repo/semantics/article peer reviewed 2001 ftorbi https://doi.org/10.1128/AEM.67.4.1529-1535.2001 2024-03-27T14:52:34Z peer reviewed The beta-galactosidase from the Antarctic gram-negative bacterium Pseudoalteromonas haloplanktis TAE 79 was purified to homogeneity. The nucleotide sequence and the NH(2)-terminal amino acid sequence of the purified enzyme indicate that the beta-galactosidase subunit is composed of 1,038 amino acids with a calculated M(r) of 118,068. This beta-galactosidase shares structural properties with Escherichia coli beta-galactosidase (comparable subunit mass, 51% amino sequence identity, conservation of amino acid residues involved in catalysis, similar optimal pH value, and requirement for divalent metal ions) but is characterized by a higher catalytic efficiency on synthetic and natural substrates and by a shift of apparent optimum activity toward low temperatures and lower thermal stability. The enzyme also differs by a higher pI (7.8) and by specific thermodynamic activation parameters. P. haloplanktis beta-galactosidase was expressed in E. coli, and the recombinant enzyme displays properties identical to those of the wild-type enzyme. Heat-induced unfolding monitored by intrinsic fluorescence spectroscopy showed lower melting point values for both P. haloplanktis wild-type and recombinant beta-galactosidase compared to the mesophilic enzyme. Assays of lactose hydrolysis in milk demonstrate that P. haloplanktis beta-galactosidase can outperform the current commercial beta-galactosidase from Kluyveromyces marxianus var. lactis, suggesting that the cold-adapted beta-galactosidase could be used to hydrolyze lactose in dairy products processed in refrigerated plants. Article in Journal/Newspaper Antarc* Antarctic University of Liège: ORBi (Open Repository and Bibliography) Applied and Environmental Microbiology 67 4 1529 1535 |
institution |
Open Polar |
collection |
University of Liège: ORBi (Open Repository and Bibliography) |
op_collection_id |
ftorbi |
language |
English |
topic |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
spellingShingle |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire Hoyoux, A. Jennes, I. Dubois, P. Genicot, S. Dubail, F. François, Jean-Marie Baise, Etienne Feller, Georges Gerday, Charles Cold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis |
topic_facet |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed The beta-galactosidase from the Antarctic gram-negative bacterium Pseudoalteromonas haloplanktis TAE 79 was purified to homogeneity. The nucleotide sequence and the NH(2)-terminal amino acid sequence of the purified enzyme indicate that the beta-galactosidase subunit is composed of 1,038 amino acids with a calculated M(r) of 118,068. This beta-galactosidase shares structural properties with Escherichia coli beta-galactosidase (comparable subunit mass, 51% amino sequence identity, conservation of amino acid residues involved in catalysis, similar optimal pH value, and requirement for divalent metal ions) but is characterized by a higher catalytic efficiency on synthetic and natural substrates and by a shift of apparent optimum activity toward low temperatures and lower thermal stability. The enzyme also differs by a higher pI (7.8) and by specific thermodynamic activation parameters. P. haloplanktis beta-galactosidase was expressed in E. coli, and the recombinant enzyme displays properties identical to those of the wild-type enzyme. Heat-induced unfolding monitored by intrinsic fluorescence spectroscopy showed lower melting point values for both P. haloplanktis wild-type and recombinant beta-galactosidase compared to the mesophilic enzyme. Assays of lactose hydrolysis in milk demonstrate that P. haloplanktis beta-galactosidase can outperform the current commercial beta-galactosidase from Kluyveromyces marxianus var. lactis, suggesting that the cold-adapted beta-galactosidase could be used to hydrolyze lactose in dairy products processed in refrigerated plants. |
format |
Article in Journal/Newspaper |
author |
Hoyoux, A. Jennes, I. Dubois, P. Genicot, S. Dubail, F. François, Jean-Marie Baise, Etienne Feller, Georges Gerday, Charles |
author_facet |
Hoyoux, A. Jennes, I. Dubois, P. Genicot, S. Dubail, F. François, Jean-Marie Baise, Etienne Feller, Georges Gerday, Charles |
author_sort |
Hoyoux, A. |
title |
Cold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis |
title_short |
Cold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis |
title_full |
Cold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis |
title_fullStr |
Cold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis |
title_full_unstemmed |
Cold-Adapted Beta-Galactosidase from the Antarctic Psychrophile Pseudoalteromonas Haloplanktis |
title_sort |
cold-adapted beta-galactosidase from the antarctic psychrophile pseudoalteromonas haloplanktis |
publisher |
American Society for Microbiology |
publishDate |
2001 |
url |
https://orbi.uliege.be/handle/2268/9845 https://orbi.uliege.be/bitstream/2268/9845/1/AEM_2001_betagal.pdf https://doi.org/10.1128/AEM.67.4.1529-1535.2001 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Applied and Environmental Microbiology, 67 (4), 1529-35 (2001-04) |
op_relation |
urn:issn:0099-2240 urn:issn:1098-5336 https://orbi.uliege.be/handle/2268/9845 info:hdl:2268/9845 https://orbi.uliege.be/bitstream/2268/9845/1/AEM_2001_betagal.pdf doi:10.1128/AEM.67.4.1529-1535.2001 scopus-id:2-s2.0-0035319361 info:pmid:11282601 |
op_rights |
open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1128/AEM.67.4.1529-1535.2001 |
container_title |
Applied and Environmental Microbiology |
container_volume |
67 |
container_issue |
4 |
container_start_page |
1529 |
op_container_end_page |
1535 |
_version_ |
1796951971403399168 |