Abstract
A continuous set of low molecular weight chitosan (LMWC) products was successfully made for this study by coordinating three enzymes (chitinase, lysozyme and cellulase) and two different deacetylated chitosan substrates (80% and 92%). It was observed that the intrinsic viscosity molecular weight ( M V ) and SEC-HPLC-determined M W distribution of LMWC were directed by both the used enzyme and the degree of chitosan substrate acetylation. LMWC prepared using lysozyme and 92%-deacetylated chitosan had larger M W and, therefore, possessed higher antibacterial activity, as compared to other combinations. LMWC enzyme-directed properties suggest chitinase is more predictable and flexible to produce the specified M V of LMWC. LMWC’s solubility and antibacterial activity, determined as minimum inhibitory concentration (MIC), against Escherichia coli exhibited a negative linear relationship with log M V . E. coli strains showed much higher susceptibility to LMWCs than Staphylococcus aureus strains did. Both species also showed intra-species sensitivity diversity toward LMWC.
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