Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities
| العنوان: | Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities |
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| المؤلفون: | Marcelo Facundo Berretta, Graciela Beatriz Benintende, Rubén O. Zandomeni, Monica Florin-Christensen, Laura Emilce Navas |
| المصدر: | Microbial Physiology. 28:99-106 |
| بيانات النشر: | S. Karger AG, 2018. |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | 0301 basic medicine, chemistry.chemical_classification, Phospholipase A, biology, Physiology, Thermus, Cell Biology, Phospholipase, biology.organism_classification, Applied Microbiology and Biotechnology, Biochemistry, Microbiology, Amino acid, 03 medical and health sciences, 030104 developmental biology, Enzyme, chemistry, Acyltransferase, Peptide sequence, Biotechnology, Thermostability |
| الوصف: | Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP_2.9) was identified in the genome of the thermophilic strain Thermus sp. 2.9. The analysis of the primary sequence unveiled a patatin-like domain. The alignment of the amino acid sequence of PLP_2.9 to other bacterial patatin-related proteins showed that the four blocks characteristic of this type of phospholipases and the amino acids representing the catalytic dyad are conserved in this protein. PLP_2.9 was overexpressed in Escherichia coli and the purified enzyme was characterized biochemically. PLP_2.9 hydrolyzed p-nitrophenyl palmitate at alkaline pH over a wide range of temperatures (55–80°C), showing high thermostability. PLP_2.9 displayed phospholipase A and acyltransferase activities on egg yolk phosphatidylcholine. Due to its high thermostability, PLP_2.9 has potential applications as a catalyst in several industrial processes. |
| تدمد: | 2673-1673 2673-1665 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_________::2065d765a128e71fb0e8a37cbf17727c https://doi.org/10.1159/000491698 |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi...........2065d765a128e71fb0e8a37cbf17727c |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 26731673 26731665 |
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