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The chitinase of <i>Serratia marcescens</i>
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1969
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BiologyIndustrial MycologyUnicellular OrganismBiomanufacturingBiosynthesisBiotransformationBiochemistryCellulase SystemNatural SciencesBiochemical TaxonomyBacteriologyBiotechnologyChitinolytic SystemsPolysaccharideMicrobiologyMedicineEnzymatic ModificationSerratia Marcescens
Serratia marcescens was found to be the most active organism of 100 tested for the production of chitinase. Enterobacter liquefaciens produced nearly as much enzyme. Under optimal conditions high yields of chitinase were obtained in 4–6 days. The S. marcescens enzyme system is extracellular and is composed of an endochitinase, a chitobiase, and a factor (CH 1 ) required for the hydrolysis of "crystalline" chitin. As such, it closely resembles the cellulase system of Trichoderma viride, and differs from those chitinolytic systems which act only on degraded forms of chitin. The absence of other hydrolytic enzymes in the S. marcescens filtrates makes this a useful system for determining the role of chitinase as a lytic agent.