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

wenzhu zhao, yuejiao Chen, siyu Xue, zhipeng Yu, hanjie Yu, Jingbo Liu, jianrong Li, Feng Chen

Index: 10.1039/C8FO00156A

Full Text: HTML

Abstract

The ability of ginger glycoproteins to inhibit the angiotensin-converting enzyme (ACE) was characterized. The activity was monitored by HPLC, and then the crude glycoproteins were enriched by lectin-microarray and magnetic microspheres. The N-linked glycan released from enriched glycoproteins by PNGase F was identified by MALDI-TOF-MS. The results suggested that crude ginger glycoproteins were active against ACE with an IC50 value of 0.83 ± 0.09 mg mL-1. The ginger glycoproteins were enriched by Con A and STL, and the structure of N-glycans released from ginger glycoproteins included high-mannose type glycans, fucosylated-type glycans, and hybrid-type glycans analyzed by the 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.