All eight C6-aliphatic alcohol and aldehyde compounds in naturally occurring green leaves showed bacteriostatic effects against Staphylococcus aureus IFO 12732, methicillin-resistant S. aureus, Escherichia coli IFO 3301, E. coli O157:H7, and Salmonella enteritidis, with bacteriostatic activities of less than 12.5 microg mL(-1). In this study, the susceptibility of Gram-positive bacteria tested was observed to be greater than that of Gram-negative bacteria. The bactericidal action of the aldehyde compounds was found to be much stronger than that of the alcohol compounds under both liquid and gaseous conditions. The most effective compound was (3E)-hexenal at concentrations of 0.1 and 1 microg mL(-1), which killed 2.1 x 10(5) cfu mL(-1) of S. aureus IFO 12732 and 1.4 x 10(5) cfu mL(-1) of E. coli IFO 3301, respectively, by direct contact with the compound. Lethality of (3E)-hexenal against S. aureus IFO 12732 and E. coli IFO 3301 was also observed as a result of gaseous contact at concentrations of 3 and 30 microg mL(-1), respectively. The bactericidal effects of 30 microg mL(-1) (3E)-hexenal were thoroughly maintained throughout periods of 2 days and 1 day against S. aureus IFO 12732 and E. coli IFO 3301, respectively, by a complex formation with alpha-cyclodextrin.
The effect of the length of polysaccharide chains on the functional
properties of Maillard-type
protein−polysaccharide conjugates was investigated using the lysozyme
as a model protein, various
sizes of galactomannan as a polysaccharide, and xyloglucan as an
oligosaccharide. The emulsifying
properties of the lysozyme−galactomannan conjugates increased in
proportion to the length of
polysaccharide chains. On the other hand, the heat stability of
the lysozyme−galactomannan
conjugates greatly increased in the range of 3.5−24 kDa
galactomannan, regardless of its molecular
mass. In addition, the effects of the binding number of
polysaccharide to lysozyme on the emulsifying
properties of the lysozyme−galactomannan conjugates were further
investigated using 1 and 2 mol
of the galactomannan (24 kDa)-attached lysozyme. The 2 mol of the
polysaccharide-attached
lysozyme showed better emulsifying properties than 1 mol of the
polysaccharide-attached protein.
The residue most sensitive to the Maillard reaction in a lysozyme
was identified as the 97-lysine
using the lysozyme−xyloglucan conjugate.
Keywords: Lysozyme; Maillard-type protein−polysaccharide conjugate;
galactomannan; xyloglucan
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.