Characterization of Maillard-type lysozyme-galactomannan conjugate having immune-enhancing effects

Jae Eon Yang, Su Hyun Chun, Ha Hyung Kim, Hee Don Choi, Kwang Won Lee

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


In the present study, lysozyme-galactomannan conjugate (LGC) was fractionated by ion-exchange chromatography, the immune activity of the fractions was confirmed, and a structural analysis of the glycoprotein was performed. A high-molecular-weight fraction of LGC (H-LGC), was characterized by using a method using matrix-assisted laser desorption/ionization time of flight mass spectrometry. The glycated site of H-LGC was determined to be the lysine (Lys)115 residue. In addition, about 1 mol of galactomannan (G) was linked to 1 mol of lysozyme (L) in LGC based on the binding weight ratio. Conjugation of L and G reduced the aggregation of particles, resulting in a monodispersion based on measurement of dynamic light scattering. LGC in solution showed heterogeneous shapes with a mean size of 337 nm. Therefore, we suggest that LGC improves the immune-enhancing activity as G conjugates the site of Lys115 on L, and provides higher solubility with reduced aggregation for the industrial use of LGC as a food constituent.

Original languageEnglish
Pages (from-to)149-157
Number of pages9
JournalFood Chemistry
Publication statusPublished - 2017 Jul 15


  • Conjugate
  • Galactomannan
  • Lysozyme
  • Maillard reaction
  • Peptide

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science


Dive into the research topics of 'Characterization of Maillard-type lysozyme-galactomannan conjugate having immune-enhancing effects'. Together they form a unique fingerprint.

Cite this