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Isolation and characterization of bioactive lactoferrin from camel milk by novel pH-dependent method for large scale production

The present article exemplifies a novel method to isolate highly purified bioactive lactoferrin from camel milk. Cytotoxicity of lactoferrin against the Hela cells was used to evaluate its bioactivity. SDS-PAGE and LC-MS analysis was done for its identification and characterization. The purified cam...

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Detalles Bibliográficos
Autores principales: Mahala, Neelam, Mittal, Aastha, Lal, Manohar, Dubey, Uma S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9519473/
https://www.ncbi.nlm.nih.gov/pubmed/36188118
http://dx.doi.org/10.1016/j.btre.2022.e00765
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author Mahala, Neelam
Mittal, Aastha
Lal, Manohar
Dubey, Uma S.
author_facet Mahala, Neelam
Mittal, Aastha
Lal, Manohar
Dubey, Uma S.
author_sort Mahala, Neelam
collection PubMed
description The present article exemplifies a novel method to isolate highly purified bioactive lactoferrin from camel milk. Cytotoxicity of lactoferrin against the Hela cells was used to evaluate its bioactivity. SDS-PAGE and LC-MS analysis was done for its identification and characterization. The purified camel milk lactoferrin was found to be 708 amino acids in length with a molecular weight of 77.3 kDa and a pI value of 8.24. This pH-dependent isolation procedure ensures the retention of bioactive lactoferrin from camel milk. The importance of the present work lies in its simplicity and scalability for manufacturing bioactive lactoferrin at an industrial level.
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spelling pubmed-95194732022-09-30 Isolation and characterization of bioactive lactoferrin from camel milk by novel pH-dependent method for large scale production Mahala, Neelam Mittal, Aastha Lal, Manohar Dubey, Uma S. Biotechnol Rep (Amst) Research Article The present article exemplifies a novel method to isolate highly purified bioactive lactoferrin from camel milk. Cytotoxicity of lactoferrin against the Hela cells was used to evaluate its bioactivity. SDS-PAGE and LC-MS analysis was done for its identification and characterization. The purified camel milk lactoferrin was found to be 708 amino acids in length with a molecular weight of 77.3 kDa and a pI value of 8.24. This pH-dependent isolation procedure ensures the retention of bioactive lactoferrin from camel milk. The importance of the present work lies in its simplicity and scalability for manufacturing bioactive lactoferrin at an industrial level. Elsevier 2022-09-21 /pmc/articles/PMC9519473/ /pubmed/36188118 http://dx.doi.org/10.1016/j.btre.2022.e00765 Text en © 2022 The Authors. Published by Elsevier B.V. https://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 Research Article
Mahala, Neelam
Mittal, Aastha
Lal, Manohar
Dubey, Uma S.
Isolation and characterization of bioactive lactoferrin from camel milk by novel pH-dependent method for large scale production
title Isolation and characterization of bioactive lactoferrin from camel milk by novel pH-dependent method for large scale production
title_full Isolation and characterization of bioactive lactoferrin from camel milk by novel pH-dependent method for large scale production
title_fullStr Isolation and characterization of bioactive lactoferrin from camel milk by novel pH-dependent method for large scale production
title_full_unstemmed Isolation and characterization of bioactive lactoferrin from camel milk by novel pH-dependent method for large scale production
title_short Isolation and characterization of bioactive lactoferrin from camel milk by novel pH-dependent method for large scale production
title_sort isolation and characterization of bioactive lactoferrin from camel milk by novel ph-dependent method for large scale production
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9519473/
https://www.ncbi.nlm.nih.gov/pubmed/36188118
http://dx.doi.org/10.1016/j.btre.2022.e00765
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