These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Biochemical Characterization of a Psychrophilic Phytase from an Artificially Cultivable Morel Morchella importuna.
    Author: Tan H, Tang J, Li X, Liu T, Miao R, Huang Z, Wang Y, Gan B, Peng W.
    Journal: J Microbiol Biotechnol; 2017 Dec 28; 27(12):2180-2189. PubMed ID: 29017237.
    Abstract:
    Psychrophilic phytases suitable for aquaculture are rare. In this study, a phytase of the histidine acid phosphatase (HAP) family was identified in Morchella importuna, a psychrophilic mushroom. The phytase showed 38% identity with Aspergillus niger PhyB, which was the closest hit. The M. importuna phytase was overexpressed in Pichia pastoris, purified, and characterized. The phytase had an optimum temperature at 25°C, which is the lowest among all the known phytases to our best knowledge. The optimum pH (6.5) is higher than most of the known HAP phytases, which is fit for the weak acidic condition in fish gut. At the optimum pH and temperature, MiPhyA showed the maximum activity level (2,384.6 ± 90.4 μmol·min⁻¹·mg⁻¹, suggesting that the enzyme possesses a higher activity level over many known phytases at low temperatures. The phytate-degrading efficacy was tested on three common feed materials (soybean meal/rapeseed meal/corn meal) and was compared with the well-known phytases of Escherichia coli and A. niger. When using the same amount of activity units, MiPhyA could yield at least 3× more inorganic phosphate than the two reference phytases. When using the same weight of protein, MiPhyA could yield at least 5× more inorganic phosphate than the other two. Since it could degrade phytate in feed materials efficiently under low temperature and weak acidic conditions, which are common for aquacultural application, MiPhyA might be a promising candidate as a feed additive enzyme.
    [Abstract] [Full Text] [Related] [New Search]