Lysozyme-catalyzed degradation

Nakamura, F., et al. 1992. Lysozyme-catalyzed degradation properties of the conjugates between chitosans having some deacetylation degrees and methotrexate. Yakuzaigaku 52 59. 

The data shown in Figure 12 indicate that the rate of glucose oxidase released from the hydrogel is directly proportional to the concentration of the protein in the hydrogel, suggesting that lysozyme catalyzed degradation of the hydrogel occurs predominantly by surface erosion process. 

DGBP Lactalbumins Lysozymes Galactose activation (369) Lactose biosynthesis Catalyze degradation of peptidoglycan, e.g. of bacterial cell walls (370,371)... 

The values for chymotrypsin and acetylcholinesterase are within the range for normal metabolic enzymes. Lysozyme is an enzyme that degrades certain polysaccharide components of bacterial cell walls. It is present in many body tissues. Its low catalytic efficiency indicates that it operates well enough to catalyze polysaccharide degradation under normal conditions. 

As described in the previous section, the addition of a surfactant produced remarkable stimulation during the synthesis of CoA. In the immobilized cell system, some surfactants showed similar stimulative effects. When the gel in which intact cells were trapped was treated with sodium laurylsulfate before the reaction, it was remarkably activated. An addition of sodium laurylsulfate to the reaction mixture with trapped Intact cells caused an increased accumulation of CoA. Similar observations have been reported by other workers. Franks (M) has reported that polyacrylamide gel-entrapped Streptococcus faecalls, which catalyzes the degradative conversion of arginine to putrescine, was activated by treating it with lysozyme. Chlbata l. (15) activated Escherichia coll cells with aspartase activity, which was trapped in polyacrylamide gel, by autolysis. 

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