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Thermostable chitinase from Cohnella sp. A01: isolation and product optimization
Twelve bacterial strains isolated from shrimp farming ponds were screened for their growth activity on chitin as the sole carbon source. The highly chitinolytic bacterial strain was detected by qualitative cup plate assay and tentatively identified to be Cohnella sp. A01 based on 16S rDNA sequencing...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5052389/ https://www.ncbi.nlm.nih.gov/pubmed/27528085 http://dx.doi.org/10.1016/j.bjm.2016.07.009 |
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author | Aliabadi, Nasrin Aminzadeh, Saeed Karkhane, Ali Asghar Haghbeen, Kamahldin |
author_facet | Aliabadi, Nasrin Aminzadeh, Saeed Karkhane, Ali Asghar Haghbeen, Kamahldin |
author_sort | Aliabadi, Nasrin |
collection | PubMed |
description | Twelve bacterial strains isolated from shrimp farming ponds were screened for their growth activity on chitin as the sole carbon source. The highly chitinolytic bacterial strain was detected by qualitative cup plate assay and tentatively identified to be Cohnella sp. A01 based on 16S rDNA sequencing and by matching the key morphological, physiological, and biochemical characteristics. The cultivation of Cohnella sp. A01 in the suitable liquid medium resulted in the production of high levels of enzyme. The colloidal chitin, peptone, and K(2)HPO(4) represented the best carbon, nitrogen, and phosphorus sources, respectively. Enzyme production by Cohnella sp. A01 was optimized by the Taguchi method. Our results demonstrated that inoculation amount and temperature of incubation were the most significant factors influencing chitinase production. From the tested values, the best pH/temperature was obtained at pH 5 and 70 °C, with K(m) and V(max) values of chitinase to be 5.6 mg/mL and 0.87 μmol/min, respectively. Ag(+), Co(2+), iodoacetamide, and iodoacetic acid inhibited the enzyme activity, whereas Mn(2+), Cu(2+), Tweens (20 and 80), Triton X-100, and EDTA increased the same. In addition, the study of the morphological alteration of chitin treated by enzyme by SEM revealed cracks and pores on the chitin surface, indicating a potential application of this enzyme in several industries. |
format | Online Article Text |
id | pubmed-5052389 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-50523892016-10-12 Thermostable chitinase from Cohnella sp. A01: isolation and product optimization Aliabadi, Nasrin Aminzadeh, Saeed Karkhane, Ali Asghar Haghbeen, Kamahldin Braz J Microbiol Industrial Microbiology Twelve bacterial strains isolated from shrimp farming ponds were screened for their growth activity on chitin as the sole carbon source. The highly chitinolytic bacterial strain was detected by qualitative cup plate assay and tentatively identified to be Cohnella sp. A01 based on 16S rDNA sequencing and by matching the key morphological, physiological, and biochemical characteristics. The cultivation of Cohnella sp. A01 in the suitable liquid medium resulted in the production of high levels of enzyme. The colloidal chitin, peptone, and K(2)HPO(4) represented the best carbon, nitrogen, and phosphorus sources, respectively. Enzyme production by Cohnella sp. A01 was optimized by the Taguchi method. Our results demonstrated that inoculation amount and temperature of incubation were the most significant factors influencing chitinase production. From the tested values, the best pH/temperature was obtained at pH 5 and 70 °C, with K(m) and V(max) values of chitinase to be 5.6 mg/mL and 0.87 μmol/min, respectively. Ag(+), Co(2+), iodoacetamide, and iodoacetic acid inhibited the enzyme activity, whereas Mn(2+), Cu(2+), Tweens (20 and 80), Triton X-100, and EDTA increased the same. In addition, the study of the morphological alteration of chitin treated by enzyme by SEM revealed cracks and pores on the chitin surface, indicating a potential application of this enzyme in several industries. Elsevier 2016-07-26 /pmc/articles/PMC5052389/ /pubmed/27528085 http://dx.doi.org/10.1016/j.bjm.2016.07.009 Text en © 2016 Sociedade Brasileira de Microbiologia. Published by Elsevier Editora Ltda. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Industrial Microbiology Aliabadi, Nasrin Aminzadeh, Saeed Karkhane, Ali Asghar Haghbeen, Kamahldin Thermostable chitinase from Cohnella sp. A01: isolation and product optimization |
title | Thermostable chitinase from Cohnella sp. A01: isolation and product optimization |
title_full | Thermostable chitinase from Cohnella sp. A01: isolation and product optimization |
title_fullStr | Thermostable chitinase from Cohnella sp. A01: isolation and product optimization |
title_full_unstemmed | Thermostable chitinase from Cohnella sp. A01: isolation and product optimization |
title_short | Thermostable chitinase from Cohnella sp. A01: isolation and product optimization |
title_sort | thermostable chitinase from cohnella sp. a01: isolation and product optimization |
topic | Industrial Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5052389/ https://www.ncbi.nlm.nih.gov/pubmed/27528085 http://dx.doi.org/10.1016/j.bjm.2016.07.009 |
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