The structural and antimicrobial functions of lysozyme reduced with food-compatible
reducing agents cysteine (Cys) and glutathione (GSH) were investigated. The disulfide …

In recent years much attention and interest have been directed toward application of natural
antimicrobial agents in foods. Some naturally occurring proteins such as lactoperoxidase …

The structural changes and antimicrobial activity of hen lysozyme in which its disulfide
bonds were reduced to varying degrees, were investigated. Lysozyme was reduced with 2 …

Previously we reported that heat-treatment of lysozyme at 80° C for 20 min in pH 6.0
(HL80/6) greatly promoted its antimicrobial action to Gram-negative bacteria without …

It was recently found that partial denaturation of hen egg white lysozyme at 80° C for 20 min
at pH 6.0 produces a strong bactericidal lysozyme (HLz) not only against Gram-positive …

The structure and antimicrobial function of hen egg white lysozyme was investigated by
means of thermal denaturation at 80° C (pH 7.2), which leads to irreversible denaturation …

In order to broaden the antimicrobial action spectrum of lysozyme against Gram-negative
bacteria, different partially reduced lysozyme derivatives were obtained by reducing the …

Lysozyme, an important bacteriostatic protein, is widely distributed in nature. It is generally
believed that the high efficiency of lysozyme in inhibiting gram-positive bacteria is caused by …

The antimicrobial mechanism and structural changes of hen egg white lysozyme irreversibly
inactivated at 80° C and at different pHs were investigated. We found that heat denaturation …

The antimicrobial activity of heat-denatured and hydrolyzed hen egg white lysozyme against
oenological lactic acid and acetic acid bacteria was investigated. The lysozyme was …