Molecular Characterization of Cold-inducible beta-Galactosidase from Arthrobacter sp ON14 Isolated from Antarctica
National Infrastructure of Natural Resources for Science and Technology Program of China [2005DKA21209]; National High-Tech Program [2007AA091904]; China Ocean Mineral Resources RD Association [COMRA DYXM-115-02-2-03] A psychrotrophic bacterium, Arthrobacter sp. ON14, isolated from Antarctica, was s...
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ftxiamenuniv:oai:dspace.xmu.edu.cn:2288/90565 2023-05-15T13:51:20+02:00 Molecular Characterization of Cold-inducible beta-Galactosidase from Arthrobacter sp ON14 Isolated from Antarctica Xu, Ke Tang, Xixiang Gai, Yingbao Mehmood, Muhammad Aamer Xiao, Xiang Wang, Fengping 许可 2011-03 http://dspace.xmu.edu.cn/handle/2288/90565 en_US eng J MICROBIOL BIOTECHN JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, 2011,21(3):236-242 WOS:000289008400002 http://dspace.xmu.edu.cn/handle/2288/90565 http://dx.doi.org/10.4014/jmb.1009.09010 GLYCOSYL HYDROLASES HYPOCREA-JECORINA MICROORGANISMS PURIFICATION PROTEIN GENE Article 2011 ftxiamenuniv 2020-07-21T11:44:25Z National Infrastructure of Natural Resources for Science and Technology Program of China [2005DKA21209]; National High-Tech Program [2007AA091904]; China Ocean Mineral Resources RD Association [COMRA DYXM-115-02-2-03] A psychrotrophic bacterium, Arthrobacter sp. ON14, isolated from Antarctica, was shown to exhibit a high beta-galactosidase activity at a low temperature. A genomic library of ON14 was constructed and screened for beta-galactosidase genes on functional plates containing 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal) as the substrate. Two different beta-galactosidase genes, named as galA, gal B, were found in ON14. Computational analyses of the genes revealed that the encoded protein GalA belongs to family 2 of glycosyl hydrolysases and is a cold-active protein, whereas GalB belongs to family 42 of glycosyl hydrolysases and is a mesophilic protein. Reverse transcription analyses revealed that the expression of galA is highly induced at a low temperature (4 degrees C) and repressed at a high temperature (28 degrees C) when lactose is used as the sole carbon source. Conversely, the expression of galB is inhibited at a low temperature and induced at a high temperature. The purified GalA showed its peak activity at 15 degrees C and pH 8. The mineral ions Na(+), K(+), Mg(2+), and Mn(2+) were identified as enzyme activators, whereas Ca(2+) had no influence on the enzyme activity. An enzyme stability assay revealed that the activity of GalA is significantly decreased when it is incubated at 45 degrees C for 2 h, and all its activity is lost when it is incubated at 50 degrees C. Article in Journal/Newspaper Antarc* Antarctica Xiamen University Institutional Repository |
institution |
Open Polar |
collection |
Xiamen University Institutional Repository |
op_collection_id |
ftxiamenuniv |
language |
English |
topic |
GLYCOSYL HYDROLASES HYPOCREA-JECORINA MICROORGANISMS PURIFICATION PROTEIN GENE |
spellingShingle |
GLYCOSYL HYDROLASES HYPOCREA-JECORINA MICROORGANISMS PURIFICATION PROTEIN GENE Xu, Ke Tang, Xixiang Gai, Yingbao Mehmood, Muhammad Aamer Xiao, Xiang Wang, Fengping 许可 Molecular Characterization of Cold-inducible beta-Galactosidase from Arthrobacter sp ON14 Isolated from Antarctica |
topic_facet |
GLYCOSYL HYDROLASES HYPOCREA-JECORINA MICROORGANISMS PURIFICATION PROTEIN GENE |
description |
National Infrastructure of Natural Resources for Science and Technology Program of China [2005DKA21209]; National High-Tech Program [2007AA091904]; China Ocean Mineral Resources RD Association [COMRA DYXM-115-02-2-03] A psychrotrophic bacterium, Arthrobacter sp. ON14, isolated from Antarctica, was shown to exhibit a high beta-galactosidase activity at a low temperature. A genomic library of ON14 was constructed and screened for beta-galactosidase genes on functional plates containing 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal) as the substrate. Two different beta-galactosidase genes, named as galA, gal B, were found in ON14. Computational analyses of the genes revealed that the encoded protein GalA belongs to family 2 of glycosyl hydrolysases and is a cold-active protein, whereas GalB belongs to family 42 of glycosyl hydrolysases and is a mesophilic protein. Reverse transcription analyses revealed that the expression of galA is highly induced at a low temperature (4 degrees C) and repressed at a high temperature (28 degrees C) when lactose is used as the sole carbon source. Conversely, the expression of galB is inhibited at a low temperature and induced at a high temperature. The purified GalA showed its peak activity at 15 degrees C and pH 8. The mineral ions Na(+), K(+), Mg(2+), and Mn(2+) were identified as enzyme activators, whereas Ca(2+) had no influence on the enzyme activity. An enzyme stability assay revealed that the activity of GalA is significantly decreased when it is incubated at 45 degrees C for 2 h, and all its activity is lost when it is incubated at 50 degrees C. |
format |
Article in Journal/Newspaper |
author |
Xu, Ke Tang, Xixiang Gai, Yingbao Mehmood, Muhammad Aamer Xiao, Xiang Wang, Fengping 许可 |
author_facet |
Xu, Ke Tang, Xixiang Gai, Yingbao Mehmood, Muhammad Aamer Xiao, Xiang Wang, Fengping 许可 |
author_sort |
Xu, Ke |
title |
Molecular Characterization of Cold-inducible beta-Galactosidase from Arthrobacter sp ON14 Isolated from Antarctica |
title_short |
Molecular Characterization of Cold-inducible beta-Galactosidase from Arthrobacter sp ON14 Isolated from Antarctica |
title_full |
Molecular Characterization of Cold-inducible beta-Galactosidase from Arthrobacter sp ON14 Isolated from Antarctica |
title_fullStr |
Molecular Characterization of Cold-inducible beta-Galactosidase from Arthrobacter sp ON14 Isolated from Antarctica |
title_full_unstemmed |
Molecular Characterization of Cold-inducible beta-Galactosidase from Arthrobacter sp ON14 Isolated from Antarctica |
title_sort |
molecular characterization of cold-inducible beta-galactosidase from arthrobacter sp on14 isolated from antarctica |
publisher |
J MICROBIOL BIOTECHN |
publishDate |
2011 |
url |
http://dspace.xmu.edu.cn/handle/2288/90565 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
http://dx.doi.org/10.4014/jmb.1009.09010 |
op_relation |
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, 2011,21(3):236-242 WOS:000289008400002 http://dspace.xmu.edu.cn/handle/2288/90565 |
_version_ |
1766255152362160128 |