Expression of a GDSL esterase from Pseudomonas sp. S9 in Pichiapastoris - Publikacja - MOST Wiedzy

Wyszukiwarka

Expression of a GDSL esterase from Pseudomonas sp. S9 in Pichiapastoris

Abstrakt

Cold active lipolytic enzymes are promising to replace the conventional enzymes processes of biotechnological industries. One of the most important feature of the cold-active lipases and esterases is that they offer economic benefits through energy saving. In general, they exhibit high activity at low temperatures and low thermostability at moderate temperatures. Lipolytic enzyme EstS9 was isolated from Pseudomonas sp. S9. A multiple sequence alignment identified EstS9 as belonging to clade II of the GDSL esterase family. The nucleotide sequence of the estS9 gene of Pseudomonas sp. S9 consists of 1,911 bp. The gene encodes for a protein of 636 amino acid residues with a molecular mass of ∼68.0 kDa. The enzyme is tolerant to alkaline pH and effective at medium to low temperatures (40–25 °C). In our previous study [1], the gene estS9 was expressed using pBAD system in E. coli TOP10 cells as His-tagged fusion protein. Like many other recombinant proteins, EstS9 was produced in E. coli in inclusion bodies. For these reason, there is interest in obtaining the extracellular active esterase which can be used for number of industrial application such as additives for laundry detergents. Therefore, during this study we constructed several recombinant P. pastoris designed for this purpose. Currently, these strains are tested for their ability to produce to the culture medium the active and soluble EstS9 esterase.

Cytowania

  • 0

    CrossRef

  • 0

    Web of Science

  • 0

    Scopus

Cytuj jako

Pełna treść

pełna treść publikacji nie jest dostępna w portalu

Słowa kluczowe

Informacje szczegółowe

Kategoria:
Inne
Typ:
suplement, wydanie specjalne, dodatek
Opublikowano w:
New Biotechnology nr 33, wydanie S, strony 198 - 198,
ISSN: 1871-6784
Tytuł wydania:
New Biotechnology strony 198 - 198
ISSN:
1871-6784
Język:
angielski
Rok wydania:
2016
DOI:
Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1016/j.nbt.2016.06.1404
Weryfikacja:
Politechnika Gdańska

wyświetlono 34 razy

Publikacje, które mogą cię zainteresować

Meta Tagi