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Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes
Amylase producing actinobacteria were isolated and characterized from terrestrial environment. There are a limited number of reports investigating the marine environment; hence, in the present study, four marine enzymes were tested for their amylase production ability. On starch agar plates, the Str...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Hindawi
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8670945/ https://www.ncbi.nlm.nih.gov/pubmed/34917683 http://dx.doi.org/10.1155/2021/5289848 |
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author | Al-Agamy, Mohamed H. Alhuzani, Mohammad R. Kelany, Mahmoud S. Hamed, Moaz M. |
author_facet | Al-Agamy, Mohamed H. Alhuzani, Mohammad R. Kelany, Mahmoud S. Hamed, Moaz M. |
author_sort | Al-Agamy, Mohamed H. |
collection | PubMed |
description | Amylase producing actinobacteria were isolated and characterized from terrestrial environment. There are a limited number of reports investigating the marine environment; hence, in the present study, four marine enzymes were tested for their amylase production ability. On starch agar plates, the Streptomyces rochei strain showed a higher hydrolytic zone (24 mm) than the other isolates. Growth under optimized culture conditions using Plackett-Burman's experimental design led to a 1.7, 9.8, 7.7, and 3.12-fold increase for the isolates S. griseorubens, S. rochei, S. parvus, and Streptomyces sp., respectively, in the specific activity measurement. When applying the Box-Behnken design on S. rochei using the most significant parameters (starch, K(2)HPO(4), pH, and temperature), there was a 12.22-fold increase in the specific activity measurement 7.37 U/mg. The α-amylase was partially purified, and its molecular weight was determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. α-Amylase was particularly active at pH 6 and 65°C. The purified enzyme was most active at 65°C and pH 6, thermal stability of 70°C for 40 min, and salt concentration of 1 M with Km and Vmax of 6.58 mg/ml and 21.93 μmol/ml/min, respectively. The α-amylase was improved by adding Cu(+2), Zn(+2), and Fe(+2) (152.21%, 207.24%, and 111.89%). Increased production of α-amylase enzyme by S. rochei KR108310 leads to production of significant industrial products. |
format | Online Article Text |
id | pubmed-8670945 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Hindawi |
record_format | MEDLINE/PubMed |
spelling | pubmed-86709452021-12-15 Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes Al-Agamy, Mohamed H. Alhuzani, Mohammad R. Kelany, Mahmoud S. Hamed, Moaz M. Biomed Res Int Research Article Amylase producing actinobacteria were isolated and characterized from terrestrial environment. There are a limited number of reports investigating the marine environment; hence, in the present study, four marine enzymes were tested for their amylase production ability. On starch agar plates, the Streptomyces rochei strain showed a higher hydrolytic zone (24 mm) than the other isolates. Growth under optimized culture conditions using Plackett-Burman's experimental design led to a 1.7, 9.8, 7.7, and 3.12-fold increase for the isolates S. griseorubens, S. rochei, S. parvus, and Streptomyces sp., respectively, in the specific activity measurement. When applying the Box-Behnken design on S. rochei using the most significant parameters (starch, K(2)HPO(4), pH, and temperature), there was a 12.22-fold increase in the specific activity measurement 7.37 U/mg. The α-amylase was partially purified, and its molecular weight was determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. α-Amylase was particularly active at pH 6 and 65°C. The purified enzyme was most active at 65°C and pH 6, thermal stability of 70°C for 40 min, and salt concentration of 1 M with Km and Vmax of 6.58 mg/ml and 21.93 μmol/ml/min, respectively. The α-amylase was improved by adding Cu(+2), Zn(+2), and Fe(+2) (152.21%, 207.24%, and 111.89%). Increased production of α-amylase enzyme by S. rochei KR108310 leads to production of significant industrial products. Hindawi 2021-12-07 /pmc/articles/PMC8670945/ /pubmed/34917683 http://dx.doi.org/10.1155/2021/5289848 Text en Copyright © 2021 Mohamed H. Al-Agamy et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Al-Agamy, Mohamed H. Alhuzani, Mohammad R. Kelany, Mahmoud S. Hamed, Moaz M. Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes |
title | Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes |
title_full | Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes |
title_fullStr | Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes |
title_full_unstemmed | Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes |
title_short | Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes |
title_sort | production and partial characterization of α-amylase enzyme from marine actinomycetes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8670945/ https://www.ncbi.nlm.nih.gov/pubmed/34917683 http://dx.doi.org/10.1155/2021/5289848 |
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