Effect of tannic acid on lysozyme activity through intermolecular noncovalent binding
作者： Junmei Su , Yuan Sun , Zhenshun Li , Yang Chen , Baomiao Ding
DOI: 10.1016/J.JAFR.2019.100004
关键词:
摘要: Abstract Lysozyme (Ly) is a good natural food preservative. However, its enzyme activity easily influenced by components, such as tannins. the specific mechanism still unknown. In this study, tannic acid (TA) was used model tannin to bind with Ly. The interactional properties of Ly-TA complexes were characterized intrinsic fluorescence intensity, fourier transform infrared spectroscopy, circular dichroism and dynamic light scattering. activities Ly analyzed lysis rate Micrococcus lysodeikticus. results indicated that TA can well through hydrophobic, hydrogen electrostatic interactions, which induced unfolding molecule. Consequently, inhibited for conformational changes masking active sites TA, stability further declined in pH changes, thermal treatments high salt concentrations. Our findings shed some on possible explanation negative effects from tannins plant foods.
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