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Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings
This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric po...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5398193/ https://www.ncbi.nlm.nih.gov/pubmed/28330183 http://dx.doi.org/10.1007/s13205-016-0427-5 |
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author | Aanangi, Raveendra Kotapati, Kasi Viswanath Palaka, Bhagath Kumar Kedam, Thyagaraju Kanika, Nirmala Devi Ampasala, Dinakara Rao |
author_facet | Aanangi, Raveendra Kotapati, Kasi Viswanath Palaka, Bhagath Kumar Kedam, Thyagaraju Kanika, Nirmala Devi Ampasala, Dinakara Rao |
author_sort | Aanangi, Raveendra |
collection | PubMed |
description | This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified LOX has molecular mass of approximately 97 kDa and showed high activity with linoleic acid than linolenic acid and arachidonic acid. The optimal activity of LOX was observed at pH 6.5 and temperature 35 °C. Far-UV circular dichroism (CD) studies revealed that the purified mung bean LOX possess secondary structural elements with significant α-helix and β-strands. Further, the secondary structure of mung bean LOX was stable up to 60 °C at pH 6.5. Biophysical and chemical properties of the mung bean LOX are similar to the other legume LOXs and may be considered as type-1 LOX. |
format | Online Article Text |
id | pubmed-5398193 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-53981932017-04-21 Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings Aanangi, Raveendra Kotapati, Kasi Viswanath Palaka, Bhagath Kumar Kedam, Thyagaraju Kanika, Nirmala Devi Ampasala, Dinakara Rao 3 Biotech Original Article This study reports purification and characterization of lipoxygenase protein from mung bean germinating seedlings. Lipoxygenases (LOXs) are key enzymes in seed germination. The purified mung bean LOX has resolved into two peaks by chromatofocusing, one has highest LOX activity with an isoelectric point of 5.84 and the other has lowest LOX activity with an isoelectric point of 5.52. The purified LOX has molecular mass of approximately 97 kDa and showed high activity with linoleic acid than linolenic acid and arachidonic acid. The optimal activity of LOX was observed at pH 6.5 and temperature 35 °C. Far-UV circular dichroism (CD) studies revealed that the purified mung bean LOX possess secondary structural elements with significant α-helix and β-strands. Further, the secondary structure of mung bean LOX was stable up to 60 °C at pH 6.5. Biophysical and chemical properties of the mung bean LOX are similar to the other legume LOXs and may be considered as type-1 LOX. Springer Berlin Heidelberg 2016-05-17 2016-06 /pmc/articles/PMC5398193/ /pubmed/28330183 http://dx.doi.org/10.1007/s13205-016-0427-5 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Original Article Aanangi, Raveendra Kotapati, Kasi Viswanath Palaka, Bhagath Kumar Kedam, Thyagaraju Kanika, Nirmala Devi Ampasala, Dinakara Rao Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings |
title | Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings |
title_full | Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings |
title_fullStr | Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings |
title_full_unstemmed | Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings |
title_short | Purification and characterization of lipoxygenase from mung bean (Vigna radiata L.) germinating seedlings |
title_sort | purification and characterization of lipoxygenase from mung bean (vigna radiata l.) germinating seedlings |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5398193/ https://www.ncbi.nlm.nih.gov/pubmed/28330183 http://dx.doi.org/10.1007/s13205-016-0427-5 |
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