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

doi:10.1016/j.foodchem.2017.01.076

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 journal › Article › peer-review

12 Citations (Scopus)

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.

Original language	English
Pages (from-to)	149-157
Number of pages	9
Journal	Food Chemistry
Volume	227
DOIs	https://doi.org/10.1016/j.foodchem.2017.01.076
Publication status	Published - 2017 Jul 15

Bibliographical note

Funding Information:
This work was supported by the High Value-added Food Technology Development Program (111137-03-HD120), Ministry for Food, Agriculture, Forestry and Fisheries, Republic of Korea (iPET) and Korea Food Research Institute (Republic of Korea). The authors thank the Korea University-CJ Food Safety Center (Seoul, South Korea) for providing equipment and facilities.

Publisher Copyright:
© 2017 Elsevier Ltd

Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.

Keywords

Conjugate
Galactomannan
Lysozyme
Maillard reaction
Peptide

ASJC Scopus subject areas

Analytical Chemistry
Food Science

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10.1016/j.foodchem.2017.01.076

Cite this

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title = "Characterization of Maillard-type lysozyme-galactomannan conjugate having immune-enhancing effects",

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.",

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author = "Yang, {Jae Eon} and Chun, {Su Hyun} and Kim, {Ha Hyung} and Choi, {Hee Don} and Lee, {Kwang Won}",

note = "Funding Information: This work was supported by the High Value-added Food Technology Development Program (111137-03-HD120), Ministry for Food, Agriculture, Forestry and Fisheries, Republic of Korea (iPET) and Korea Food Research Institute (Republic of Korea). The authors thank the Korea University-CJ Food Safety Center (Seoul, South Korea) for providing equipment and facilities. Publisher Copyright: {\textcopyright} 2017 Elsevier Ltd Copyright: Copyright 2017 Elsevier B.V., All rights reserved.",

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AU - Yang, Jae Eon

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AU - Choi, Hee Don

AU - Lee, Kwang Won

N1 - Funding Information: This work was supported by the High Value-added Food Technology Development Program (111137-03-HD120), Ministry for Food, Agriculture, Forestry and Fisheries, Republic of Korea (iPET) and Korea Food Research Institute (Republic of Korea). The authors thank the Korea University-CJ Food Safety Center (Seoul, South Korea) for providing equipment and facilities. Publisher Copyright: © 2017 Elsevier Ltd Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

PY - 2017/7/15

Y1 - 2017/7/15

N2 - 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.

AB - 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.

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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