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Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine
Phosphatidylserine (PS) is useful as the additive in industries for memory improvement, mood enhancement and drug delivery. Conventionally, PS was extracted from soybeans, vegetable oils, egg yolk, and biomass; however, their low availability and high extraction cost were limiting factors. Phospholi...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5972935/ https://www.ncbi.nlm.nih.gov/pubmed/28509615 http://dx.doi.org/10.1080/21655979.2017.1308992 |
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author | Zhou, Wen-Bin Gong, Jin-Song Hou, Hai-Juan Li, Heng Lu, Zhen-Ming Xu, Hong-Yu Xu, Zheng-Hong Shi, Jin-Song |
author_facet | Zhou, Wen-Bin Gong, Jin-Song Hou, Hai-Juan Li, Heng Lu, Zhen-Ming Xu, Hong-Yu Xu, Zheng-Hong Shi, Jin-Song |
author_sort | Zhou, Wen-Bin |
collection | PubMed |
description | Phosphatidylserine (PS) is useful as the additive in industries for memory improvement, mood enhancement and drug delivery. Conventionally, PS was extracted from soybeans, vegetable oils, egg yolk, and biomass; however, their low availability and high extraction cost were limiting factors. Phospholipase D (PLD) is a promising tool for enzymatic synthesis of PS due to its transphosphatidylation activity. In this contribution, a new and uncharacterized PLD was first obtained from GenBank database via genome mining strategy. The open reading frame consisted of 1614 bp and potentially encoded a protein of 538-amino-acid with a theoretical molecular mass of 60 kDa. The gene was successfully cloned and expressed in Escherichia coli. Its enzymatic properties were experimentally characterized. The temperature and pH optima of PLD were determined to be 60°C and 7.5, respectively. Its hydrolytic activity was improved by addition of Ca(2+) at 5 mM as compared with the control. The enzyme displayed suitable transphosphatidylation activity and PS could be synthesized with L-serine and soybean lecithin as substrates under the catalysis of PLD. This PLD enzyme might be a potential candidate for industrial applications in PS production. To the best of our knowledge, this is the first report on genome mining of PLDs from GenBank database. |
format | Online Article Text |
id | pubmed-5972935 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-59729352018-05-31 Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine Zhou, Wen-Bin Gong, Jin-Song Hou, Hai-Juan Li, Heng Lu, Zhen-Ming Xu, Hong-Yu Xu, Zheng-Hong Shi, Jin-Song Bioengineered Research Paper Phosphatidylserine (PS) is useful as the additive in industries for memory improvement, mood enhancement and drug delivery. Conventionally, PS was extracted from soybeans, vegetable oils, egg yolk, and biomass; however, their low availability and high extraction cost were limiting factors. Phospholipase D (PLD) is a promising tool for enzymatic synthesis of PS due to its transphosphatidylation activity. In this contribution, a new and uncharacterized PLD was first obtained from GenBank database via genome mining strategy. The open reading frame consisted of 1614 bp and potentially encoded a protein of 538-amino-acid with a theoretical molecular mass of 60 kDa. The gene was successfully cloned and expressed in Escherichia coli. Its enzymatic properties were experimentally characterized. The temperature and pH optima of PLD were determined to be 60°C and 7.5, respectively. Its hydrolytic activity was improved by addition of Ca(2+) at 5 mM as compared with the control. The enzyme displayed suitable transphosphatidylation activity and PS could be synthesized with L-serine and soybean lecithin as substrates under the catalysis of PLD. This PLD enzyme might be a potential candidate for industrial applications in PS production. To the best of our knowledge, this is the first report on genome mining of PLDs from GenBank database. Taylor & Francis 2017-05-16 /pmc/articles/PMC5972935/ /pubmed/28509615 http://dx.doi.org/10.1080/21655979.2017.1308992 Text en © 2018 The Author(s). Published with license by Taylor & Francis http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Zhou, Wen-Bin Gong, Jin-Song Hou, Hai-Juan Li, Heng Lu, Zhen-Ming Xu, Hong-Yu Xu, Zheng-Hong Shi, Jin-Song Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine |
title | Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine |
title_full | Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine |
title_fullStr | Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine |
title_full_unstemmed | Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine |
title_short | Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine |
title_sort | mining of a phospholipase d and its application in enzymatic preparation of phosphatidylserine |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5972935/ https://www.ncbi.nlm.nih.gov/pubmed/28509615 http://dx.doi.org/10.1080/21655979.2017.1308992 |
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