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Antibacterial potential of inulinase enzyme obtained from Nocardiopsis sp.
The enriched nutritional and functional properties of inulinase with wide attention are considered commercial/industrial food enzymes. It can be produced by many microorganisms such as yeasts, fungi, and bacteria. Nocardiopsis is a genus under Actinomycetes, which has biotechnologically important mi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Wolters Kluwer - Medknow
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9836159/ https://www.ncbi.nlm.nih.gov/pubmed/36643101 http://dx.doi.org/10.4103/japtr.japtr_332_22 |
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author | Neha, N Sivaperumal, Pitchiah Roy, Anitha |
author_facet | Neha, N Sivaperumal, Pitchiah Roy, Anitha |
author_sort | Neha, N |
collection | PubMed |
description | The enriched nutritional and functional properties of inulinase with wide attention are considered commercial/industrial food enzymes. It can be produced by many microorganisms such as yeasts, fungi, and bacteria. Nocardiopsis is a genus under Actinomycetes, which has biotechnologically important microorganisms. This study aims to isolate and identify marine Actinomycetes Nocardiopsis species and to evaluate the antibacterial potential of the inulinase enzyme obtained from it. Marine actinobacteria (Nocardiopsis sp.) were isolated from sediment samples on YM agar. The isolate was identified by biochemical analysis of cell walls (amino acid and sugar). Enzyme screening assay was performed with temperature and pH influence in the production inulinase enzyme production. Antibacterial activity and minimal inhibitory activity of inulinase enzyme were performed with Staphylococcus, Klebsiella pneumoniae, and Pseudomonas aeruginosa. Antimicrobial testing revealed that with higher concentrations of inulinase enzyme, the zone of inhibition of bacterial growth increased, and the minimum inhibitory concentration of inulinase enzyme that prevented the growth of bacteria was close to the standard tetracycline. Inulinase enzyme obtained from Nocardiopsis species shows good antibacterial activity against Staphylococcus aureus, K. pneumoniae, and P. aeruginosa in comparison to the standard, tetracycline. |
format | Online Article Text |
id | pubmed-9836159 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Wolters Kluwer - Medknow |
record_format | MEDLINE/PubMed |
spelling | pubmed-98361592023-01-13 Antibacterial potential of inulinase enzyme obtained from Nocardiopsis sp. Neha, N Sivaperumal, Pitchiah Roy, Anitha J Adv Pharm Technol Res Original Article The enriched nutritional and functional properties of inulinase with wide attention are considered commercial/industrial food enzymes. It can be produced by many microorganisms such as yeasts, fungi, and bacteria. Nocardiopsis is a genus under Actinomycetes, which has biotechnologically important microorganisms. This study aims to isolate and identify marine Actinomycetes Nocardiopsis species and to evaluate the antibacterial potential of the inulinase enzyme obtained from it. Marine actinobacteria (Nocardiopsis sp.) were isolated from sediment samples on YM agar. The isolate was identified by biochemical analysis of cell walls (amino acid and sugar). Enzyme screening assay was performed with temperature and pH influence in the production inulinase enzyme production. Antibacterial activity and minimal inhibitory activity of inulinase enzyme were performed with Staphylococcus, Klebsiella pneumoniae, and Pseudomonas aeruginosa. Antimicrobial testing revealed that with higher concentrations of inulinase enzyme, the zone of inhibition of bacterial growth increased, and the minimum inhibitory concentration of inulinase enzyme that prevented the growth of bacteria was close to the standard tetracycline. Inulinase enzyme obtained from Nocardiopsis species shows good antibacterial activity against Staphylococcus aureus, K. pneumoniae, and P. aeruginosa in comparison to the standard, tetracycline. Wolters Kluwer - Medknow 2022-11 2022-11-30 /pmc/articles/PMC9836159/ /pubmed/36643101 http://dx.doi.org/10.4103/japtr.japtr_332_22 Text en Copyright: © 2022 Journal of Advanced Pharmaceutical Technology & Research https://creativecommons.org/licenses/by-nc-sa/4.0/This is an open access journal, and articles are distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as appropriate credit is given and the new creations are licensed under the identical terms. |
spellingShingle | Original Article Neha, N Sivaperumal, Pitchiah Roy, Anitha Antibacterial potential of inulinase enzyme obtained from Nocardiopsis sp. |
title | Antibacterial potential of inulinase enzyme obtained from Nocardiopsis sp. |
title_full | Antibacterial potential of inulinase enzyme obtained from Nocardiopsis sp. |
title_fullStr | Antibacterial potential of inulinase enzyme obtained from Nocardiopsis sp. |
title_full_unstemmed | Antibacterial potential of inulinase enzyme obtained from Nocardiopsis sp. |
title_short | Antibacterial potential of inulinase enzyme obtained from Nocardiopsis sp. |
title_sort | antibacterial potential of inulinase enzyme obtained from nocardiopsis sp. |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9836159/ https://www.ncbi.nlm.nih.gov/pubmed/36643101 http://dx.doi.org/10.4103/japtr.japtr_332_22 |
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