Interaction of ε-Poly-L-lysine with Ovalbumin and Its Influence on Antibacterial Activity

doi:10.7506/spkx1002-6630-201801011

Abstract

Abstract: The purpose of this study was to characterize the interaction of cationic ε-poly-L-lysine (ε-PL) with anionic ovalbumin and investigate the influence of this interaction on the antimicrobial efficacy of ε-PL. The interaction was characterized by measuring the ζ-potential and turbidity of ovalbumin-ε-PL complex solution. The results showed that ovalbumin interacted with ε-PL molecules, forming complexes with different electrical charges. In addition, the antimicrobial efficacy of ε-PL against Escherichia coli decreased, likely due to strong electrostatic binding of ε-PL to ovalbumin molecules and consequently reducing its interaction with the negative charge on the of microbial surface. The model of ε-PL interaction with ovalbumin and bacteria proposed in this study helps further reveal the interaction of ε-PL with protein and the influence of this interaction on the antimicrobial efficacy of ε-PL in complex food systems.

Key words: ε-poly-L-lysine, ovalbumin, electrostatic binding, antibacterial activity, protein

CLC Number:

TS201.3

TAN Zhilei, WU Yanan, FANG Siqi, SUN Xiaoguang, LIANG Li, GUO Fengzhu, JIA Shiru, ZHOU Bin. Interaction of ε-Poly-L-lysine with Ovalbumin and Its Influence on Antibacterial Activity[J]. FOOD SCIENCE, 2018, 39(1): 73-77.

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Interaction of ε-Poly-L-lysine with Ovalbumin and Its Influence on Antibacterial Activity

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