Depolymerization with endolytic

The pectate lyase activities secreted by Clostridium populeti, isolated from a poplar based methane digestor (28), were compared with those secreted by E. chrysanthemi and L. multiparus. Isoelectric focusing followed by overlay and activity analysis revealed the presence of one or two activity bands with pi values from 4.5 to 4.7 for both the C. populeti and the L. multiparus. The kinetic depolymerization profiles of C. populeti also revealed an exolytic/endolytic mechanism, typified by the high ratio of trimer and/or dimer to hexamer in the early stages of the reaction (Table I). 

Saprophytic anaerobic bacteria, e.g. the ruminant bacterium Lachnospira multiparus and the methane digestor isolate, Clostridium populeti, secrete only acidic pectate lyases that exhibit an exolytic/endolytic depolymerization toward polygalacturonate. It will be important to determine if this acidic property contributes to the adsorption of these enzymes to the secreting bacterium, perhaps contributing to the efficiency with which the bacteria are able to assimilate the products generated by these enzymes. 

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