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Properties of an amylase from thermophilic Bacillus SP
α-Amylase production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing soluble starch as a carbon source and supplemented with 0.05% whey protein and 0.2% peptone reached a maximum activity at 32 h, with levels of 37 U/mL. Studies on the amylase characterization reve...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Sociedade Brasileira de Microbiologia
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3768357/ https://www.ncbi.nlm.nih.gov/pubmed/24031188 http://dx.doi.org/10.1590/S1517-838220080001000023 |
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author | de Carvalho, Raquel Vieira Côrrea, Thamy Lívia Ribeiro da Silva, Júlia Caroline Matos de Oliveira Mansur, Luciana Ribeiro Coutinho Martins, Meire Lelis Leal |
author_facet | de Carvalho, Raquel Vieira Côrrea, Thamy Lívia Ribeiro da Silva, Júlia Caroline Matos de Oliveira Mansur, Luciana Ribeiro Coutinho Martins, Meire Lelis Leal |
author_sort | de Carvalho, Raquel Vieira |
collection | PubMed |
description | α-Amylase production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing soluble starch as a carbon source and supplemented with 0.05% whey protein and 0.2% peptone reached a maximum activity at 32 h, with levels of 37 U/mL. Studies on the amylase characterization revealed that the optimum temperature of this enzyme was 90°C. The enzyme was stable for 1 h at temperatures ranging from 40-50°C while at 90°C, 66% of its maximum activity was lost. However, in the presence of 5 mM CaCl2, the enzyme was stable at 90°C for 30 min and retained about 58% residual activity after 1 h. The optimum pH of the enzyme was found to be 8.5. After incubation of enzyme for 2 h at pH 9.5 and 11.0 was observed a decrease of about 6.3% and 16.5% of its original activity. At pH 6.0 the enzyme lost about 36% of its original activity. The enzyme was strongly inhibited by Co(2+), Cu(2+) and Ba(2+), but less affected by Mg(2+), Na(+) and K(+). In the presence of 2.0 M NaCl, 63% of amylase activity was retained after 2 h incubation at 45°C. The amylase exhibited more than 70% activity when incubated for 1 h at 50°C with sodium dodecyl sulphate. However, very little residual activity was obtained with sodium hypochlorite and with hydrogen peroxide the enzyme was completely inhibited. The compatibility of Bacillus sp SMIA-2 amylase with certain commercial detergents was shown to be good as the enzyme retained 86%, 85% and 75% of its activity after 20 min incubation at 50°C in the presence of the detergent brands Omo(®), Campeiro(®) and Tide(®), respectively. |
format | Online Article Text |
id | pubmed-3768357 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Sociedade Brasileira de Microbiologia |
record_format | MEDLINE/PubMed |
spelling | pubmed-37683572013-09-12 Properties of an amylase from thermophilic Bacillus SP de Carvalho, Raquel Vieira Côrrea, Thamy Lívia Ribeiro da Silva, Júlia Caroline Matos de Oliveira Mansur, Luciana Ribeiro Coutinho Martins, Meire Lelis Leal Braz J Microbiol Industrial Microbiology α-Amylase production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing soluble starch as a carbon source and supplemented with 0.05% whey protein and 0.2% peptone reached a maximum activity at 32 h, with levels of 37 U/mL. Studies on the amylase characterization revealed that the optimum temperature of this enzyme was 90°C. The enzyme was stable for 1 h at temperatures ranging from 40-50°C while at 90°C, 66% of its maximum activity was lost. However, in the presence of 5 mM CaCl2, the enzyme was stable at 90°C for 30 min and retained about 58% residual activity after 1 h. The optimum pH of the enzyme was found to be 8.5. After incubation of enzyme for 2 h at pH 9.5 and 11.0 was observed a decrease of about 6.3% and 16.5% of its original activity. At pH 6.0 the enzyme lost about 36% of its original activity. The enzyme was strongly inhibited by Co(2+), Cu(2+) and Ba(2+), but less affected by Mg(2+), Na(+) and K(+). In the presence of 2.0 M NaCl, 63% of amylase activity was retained after 2 h incubation at 45°C. The amylase exhibited more than 70% activity when incubated for 1 h at 50°C with sodium dodecyl sulphate. However, very little residual activity was obtained with sodium hypochlorite and with hydrogen peroxide the enzyme was completely inhibited. The compatibility of Bacillus sp SMIA-2 amylase with certain commercial detergents was shown to be good as the enzyme retained 86%, 85% and 75% of its activity after 20 min incubation at 50°C in the presence of the detergent brands Omo(®), Campeiro(®) and Tide(®), respectively. Sociedade Brasileira de Microbiologia 2008 2008-03-01 /pmc/articles/PMC3768357/ /pubmed/24031188 http://dx.doi.org/10.1590/S1517-838220080001000023 Text en © Sociedade Brasileira de Microbiologia http://creativecommons.org/licenses/by-nc/3.0/ All the content of the journal, except where otherwise noted, is licensed under a Creative Commons License |
spellingShingle | Industrial Microbiology de Carvalho, Raquel Vieira Côrrea, Thamy Lívia Ribeiro da Silva, Júlia Caroline Matos de Oliveira Mansur, Luciana Ribeiro Coutinho Martins, Meire Lelis Leal Properties of an amylase from thermophilic Bacillus SP |
title | Properties of an amylase from thermophilic Bacillus SP |
title_full | Properties of an amylase from thermophilic Bacillus SP |
title_fullStr | Properties of an amylase from thermophilic Bacillus SP |
title_full_unstemmed | Properties of an amylase from thermophilic Bacillus SP |
title_short | Properties of an amylase from thermophilic Bacillus SP |
title_sort | properties of an amylase from thermophilic bacillus sp |
topic | Industrial Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3768357/ https://www.ncbi.nlm.nih.gov/pubmed/24031188 http://dx.doi.org/10.1590/S1517-838220080001000023 |
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