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MALDI-TOF-MS characterization of N-linked glycoprotein derived from ginger with ACE inhibitory activity

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Abstract

Herein, the ability of ginger glycoproteins to inhibit the angiotensin-converting enzyme (ACE) is characterized. The activity is monitored via HPLC, and then the crude glycoproteins are enriched with lectin microarrays and magnetic microspheres. The N-linked glycans released from the enriched glycoproteins by PNGase F are identified by MALDI-TOF-MS. The results suggest that the crude ginger glycoproteins are active against ACE with an IC50 value of 0.83 ± 0.09 mg mL−1. The ginger glycoproteins are enriched by concanavalin A (Con A) and solanum tuberosum (Potato) lectin (STL), and the structures of the N-glycans released from the ginger glycoproteins include high-mannose type glycans, fucosylated-type glycans, and hybrid-type glycans, as analyzed by MALDI-TOF-MS. The results of this study are expected to provide a reference for the glycan structure of ginger glycoproteins with ACE-inhibitory activity.

Graphical abstract: MALDI-TOF-MS characterization of N-linked glycoprotein derived from ginger with ACE inhibitory activity

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Publication details

The article was received on 24 Jan 2018, accepted on 05 Apr 2018 and first published on 06 Apr 2018


Article type: Paper
DOI: 10.1039/C8FO00156A
Citation: Food Funct., 2018, Advance Article
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    MALDI-TOF-MS characterization of N-linked glycoprotein derived from ginger with ACE inhibitory activity

    W. Zhao, Y. Chen, S. Xue, Z. Yu, H. Yu, J. Liu, J. Li and F. Chen, Food Funct., 2018, Advance Article , DOI: 10.1039/C8FO00156A

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