Production and Characterization of a New alpha-Glucosidase Inhibitory Peptide from Aspergillus oryzae N159-1.
10.5941/MYCO.2013.41.3.149
- Author:
Min Gu KANG
1
;
Sung Hun YI
;
Jong Soo LEE
Author Information
1. Department of Biomedicinal Science and Biotechnology, Paichai University, Daejeon 302-735, Korea. biotech8@pcu.ac.kr
- Publication Type:Original Article
- Keywords:
alpha-Glucosidase inhibitory peptide;
Anti-obesity;
Aspergillus oryzae N159-1
- MeSH:
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
- From:Mycobiology
2013;41(3):149-154
- CountryRepublic of Korea
- Language:English
-
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.
