Characterization of Maillard-type lysozyme-galactomannan conjugate having immune-enhancing effects
- Authors
- Yang, Jae-Eon; Chun, Su-Hyun; Kim, Ha Hyung; Choi, Hee-Don; Lee, Kwang-Won
- Issue Date
- 15-7월-2017
- Publisher
- ELSEVIER SCI LTD
- Keywords
- Maillard reaction; Galactomannan; Lysozyme; Conjugate; Peptide
- Citation
- FOOD CHEMISTRY, v.227, pp.149 - 157
- Indexed
- SCIE
SCOPUS
- Journal Title
- FOOD CHEMISTRY
- Volume
- 227
- Start Page
- 149
- End Page
- 157
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/82826
- DOI
- 10.1016/j.foodchem.2017.01.076
- ISSN
- 0308-8146
- Abstract
- 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. (C) 2017 Elsevier Ltd. All rights reserved.
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