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Manyattempts have been made to develop food preservatives with antimicrobial effects without any food toxicities.1'2* One of the most promising reagents is lytic enzymes such as egg white lysozyme. Lysozyme attacks only specific positions of glycosidic bonds between Nacetylhexosamines of the peptidoglycan layer in bacterial cell walls. The walls of Grampositive cells are generally quite sensitive to attack by lysozyme. However, Gram-negative bacteria are less susceptible to such attack, since the outer membraneexcludes lysozyme and prevents it from binding to its site of action on the peptidoglycan in cell walls. Surfactants solubilize outer membranesmainly consisting of lipopolysaccharide.3 "6) Therefore, if lysozyme is converted to an amphiphilic protein, it may attack to Gram-negative bacteria. Wehave reported7) that ovalbumin-dextran conjugate obtained by the naturally occurring Maillard reaction has excellent emulsifying properties superior to commercial emulsifiers. Strikingly, lysozyme-dextran conjugate obtained in a similar way showed greater emulsifying properties than ovalbumin-dextran conjugate. In addition, the lytic activity

Novel bifunctional lysozyme-dextran conjugate that acts on both Gram-negative and Grampositive bacteria.