Presentation Title

Qualitative MALDI Analysis of Lantibiotic Complexation with Major Whey Proteins in Milk

Format of Presentation

Poster to be presented the Friday of the conference

Abstract

The interaction of the lantibiotic nisin, a bio-preservative added to dairy products, with whey proteins in bovine milk products may hold significance in an immunological regard, as well as in the field of food chemistry. If the lantibiotic complexation site sterically hinders epitopes (antigenic determinant sites) on any of the major whey proteins, there is a potential for the interaction to affect the proteins ability to act as allergens. Furthermore, an interaction could also increase the solubility of the lantibioitic in dairy products, enhancing its anti-microbial properties. This research will seek to identify complexation between the lantibioitc, nisin, and three of the major whey proteins in milk – beta-lactoglobulin A (βLG -A), beta-lactoglobulin B (βLG-B), and alpha-lactalbumin (α-LA). The qualitative analysis will be performed with matrix assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Previous research has established a potential interaction between nisin and βLG-B using MALDI, but further determination is required for the other major whey proteins in bovine milk. However, It is expected that βLG-A will complex with nisin in a similar way as to βLG-B, as the proteins differ only at two residues (D64G and V118A from βLG-A to βLG-B, respectively) and it is unlikely the hydrophobic residues of glycine (G) or alanine (A) are involved in protein-peptide complexation.

Department

Chemistry

Faculty Advisor

Kingsley Donkor

This document is currently not available here.

Share

COinS
 

Qualitative MALDI Analysis of Lantibiotic Complexation with Major Whey Proteins in Milk

The interaction of the lantibiotic nisin, a bio-preservative added to dairy products, with whey proteins in bovine milk products may hold significance in an immunological regard, as well as in the field of food chemistry. If the lantibiotic complexation site sterically hinders epitopes (antigenic determinant sites) on any of the major whey proteins, there is a potential for the interaction to affect the proteins ability to act as allergens. Furthermore, an interaction could also increase the solubility of the lantibioitic in dairy products, enhancing its anti-microbial properties. This research will seek to identify complexation between the lantibioitc, nisin, and three of the major whey proteins in milk – beta-lactoglobulin A (βLG -A), beta-lactoglobulin B (βLG-B), and alpha-lactalbumin (α-LA). The qualitative analysis will be performed with matrix assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Previous research has established a potential interaction between nisin and βLG-B using MALDI, but further determination is required for the other major whey proteins in bovine milk. However, It is expected that βLG-A will complex with nisin in a similar way as to βLG-B, as the proteins differ only at two residues (D64G and V118A from βLG-A to βLG-B, respectively) and it is unlikely the hydrophobic residues of glycine (G) or alanine (A) are involved in protein-peptide complexation.