Production and Characterization of a New alpha-Glucosidase Inhibitory Peptide from Aspergillus oryzae N159-1
Mycobiology
;
: 149-154, 2013.
Article
Dans Anglais
| WPRIM
| ID: wpr-729421
ABSTRACT
An alpha-glucosidase inhibitor was developed from Aspergillus oryzae N159-1, which was screened from traditional fermented Korean foods. The intracellular concentration of the inhibitor reached its highest level when the fungus was cultured in tryptic soy broth medium at 27degrees C for five days. The inhibitor was purified using a series of purification steps involving ultrafiltration, Sephadex G-25 gel permeation chromatography, strong cation exchange solid phase extraction, reverse-phase high performance liquid chromatography, and size exclusion chromatography. The final yield of the purification was 1.9%. Results of the liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis indicated that the purified alpha-glucosidase inhibitor was a tri-peptide, Pro-Phe-Pro, with the molecular weight of 360.1 Da. The IC50 value of the peptide against alpha-glucosidase activity was 3.1 mg/mL. Using Lineweaver-Burk plot analysis, the inhibition pattern indicated that the inhibitor acts as a mixed type inhibitor.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Hydrolysats de protéines
/
Aspergillus
/
Aspergillus oryzae
/
Spectrométrie de masse
/
Ultrafiltration
/
Caséines
/
Chromatographie sur gel
/
Chromatographie en phase liquide
/
Dextrane
/
Concentration inhibitrice 50
langue:
Anglais
Texte intégral:
Mycobiology
Année:
2013
Type:
Article
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