Mycobiology.  2013 Sep;41(3):149-154. 10.5941/MYCO.2013.41.3.149.

Production and Characterization of a New alpha-Glucosidase Inhibitory Peptide from Aspergillus oryzae N159-1

• Kang MG
• Yi SH
• Lee JS

• KMID: 1964229
• DOI: http://doi.org/10.5941/MYCO.2013.41.3.149

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.

Keyword

alpha-Glucosidase inhibitory peptide; Anti-obesity; Aspergillus oryzae N159-1

MeSH Terms

alpha-Glucosidases*
Aspergillus oryzae*
Aspergillus*
Caseins
Chromatography, Gel
Chromatography, Liquid
Dextrans
Fungi
Inhibitory Concentration 50
Mass Spectrometry
Molecular Weight
Protein Hydrolysates
Solid Phase Extraction
Ultrafiltration
Caseins
Dextrans
Protein Hydrolysates
alpha-Glucosidases