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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...

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Autores principales: Al-Agamy, Mohamed H., Alhuzani, Mohammad R., Kelany, Mahmoud S., Hamed, Moaz M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi 2021
Materias:
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.
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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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