Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B
A total of 59 bacteria samples from Antarctic sea water were collected and screened for their ability to produce α-amylase. The highest activity was recorded from an isolate identified as an Alteromonas species. The purified α-amylase shows a molecular mass of about 50 000 Da and a pI of 5.2. The en...
Published in: | Canadian Journal of Microbiology |
---|---|
Main Authors: | , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Canadian Science Publishing
1999
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1139/w99-021 http://www.nrcresearchpress.com/doi/pdf/10.1139/w99-021 |
id |
crcansciencepubl:10.1139/w99-021 |
---|---|
record_format |
openpolar |
spelling |
crcansciencepubl:10.1139/w99-021 2024-09-15T17:48:31+00:00 Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B Chessa, Jean-Pierre Feller, Georges Gerday, Charles 1999 http://dx.doi.org/10.1139/w99-021 http://www.nrcresearchpress.com/doi/pdf/10.1139/w99-021 en eng Canadian Science Publishing http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining Canadian Journal of Microbiology volume 45, issue 6, page 452-457 ISSN 0008-4166 1480-3275 journal-article 1999 crcansciencepubl https://doi.org/10.1139/w99-021 2024-06-27T04:10:58Z A total of 59 bacteria samples from Antarctic sea water were collected and screened for their ability to produce α-amylase. The highest activity was recorded from an isolate identified as an Alteromonas species. The purified α-amylase shows a molecular mass of about 50 000 Da and a pI of 5.2. The enzyme is stable from pH 7.5 to 9 and has a maximal activity at pH 7.5. Compared with other α-amylases from mesophiles and thermophiles, the "cold enzyme" displays a higher activity at low temperature and a lower stability at high temperature. The psychrophilic α-amylase requires both Cl - and Ca 2+ for its amylolytic activity. Br - is also quite effecient as an allosteric effector. The comparison of the amino acid composition with those of other α-amylases from various organisms shows that the cold α-amylase has the lowest content in Arg and Pro residues. This could be involved in the principle used by the psychrophilic enzyme to adapt its molecular structure to the low temperature of the environment. Key words: α-amylase, psychrophilic microorganisms, Antarctic. Article in Journal/Newspaper Antarc* Antarctic Canadian Science Publishing Canadian Journal of Microbiology 45 6 452 457 |
institution |
Open Polar |
collection |
Canadian Science Publishing |
op_collection_id |
crcansciencepubl |
language |
English |
description |
A total of 59 bacteria samples from Antarctic sea water were collected and screened for their ability to produce α-amylase. The highest activity was recorded from an isolate identified as an Alteromonas species. The purified α-amylase shows a molecular mass of about 50 000 Da and a pI of 5.2. The enzyme is stable from pH 7.5 to 9 and has a maximal activity at pH 7.5. Compared with other α-amylases from mesophiles and thermophiles, the "cold enzyme" displays a higher activity at low temperature and a lower stability at high temperature. The psychrophilic α-amylase requires both Cl - and Ca 2+ for its amylolytic activity. Br - is also quite effecient as an allosteric effector. The comparison of the amino acid composition with those of other α-amylases from various organisms shows that the cold α-amylase has the lowest content in Arg and Pro residues. This could be involved in the principle used by the psychrophilic enzyme to adapt its molecular structure to the low temperature of the environment. Key words: α-amylase, psychrophilic microorganisms, Antarctic. |
format |
Article in Journal/Newspaper |
author |
Chessa, Jean-Pierre Feller, Georges Gerday, Charles |
spellingShingle |
Chessa, Jean-Pierre Feller, Georges Gerday, Charles Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B |
author_facet |
Chessa, Jean-Pierre Feller, Georges Gerday, Charles |
author_sort |
Chessa, Jean-Pierre |
title |
Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B |
title_short |
Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B |
title_full |
Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B |
title_fullStr |
Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B |
title_full_unstemmed |
Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B |
title_sort |
purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium tac 240b |
publisher |
Canadian Science Publishing |
publishDate |
1999 |
url |
http://dx.doi.org/10.1139/w99-021 http://www.nrcresearchpress.com/doi/pdf/10.1139/w99-021 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Canadian Journal of Microbiology volume 45, issue 6, page 452-457 ISSN 0008-4166 1480-3275 |
op_rights |
http://www.nrcresearchpress.com/page/about/CorporateTextAndDataMining |
op_doi |
https://doi.org/10.1139/w99-021 |
container_title |
Canadian Journal of Microbiology |
container_volume |
45 |
container_issue |
6 |
container_start_page |
452 |
op_container_end_page |
457 |
_version_ |
1810289812176896000 |