ArticleBioengineered2018
Mining of a phospholipase D and its application in enzymatic preparation of phosphatidylserine.
Article in Bioengineered, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 28 citations in OpenAlex.
- Whole-Cell Display of Phospholipase D inBiomolecules · 2024Article
- Efficient secretory expression of phospholipase D for the high-yield production of phosphatidylserine and phospholipid derivates from soybean lecithin.Synthetic and systems biotechnology · 2023Article
- Article
- Study on the mechanism of efficient extracellular expression of toxic streptomyces phospholipase D in Brevibacillus choshinensis under MgMicrobial cell factories · 2022Article
- Acyl Chain Specificity of MarineInternational journal of molecular sciences · 2021Article
- Extracellular Vesicles in the Development of the Non-Alcoholic Fatty Liver Disease: An Update.Biomolecules · 2020Review
- Identification of a novel phospholipase D gene and effects of carbon sources on its expression in Bacillus cereus ZY12.Journal of microbiology (Seoul, Korea) · 2018Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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
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Registered trials
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