Clostridium felsineum

Characteristic properties of endopectate lyases are the high pH optimum, and a requirement for Ca2+ ions in order to maintain catalytic activity. The pH optimum of various endopectate lyases ranges from 8.0 to 9.5 (Refs. 4, 178, 234, 236, 243). Besides activation by Ca2+ ions, the optimal concentration of which is 1 mM,234,236,244 strontium salts were also considered in the case of Bacillus sp. lyase.234 The enzyme from Pseudomonas sp. was also partly activated by magnesium chloride,178 and for the lyase of Clostridium felsineum, salts of other bivalent cations had an activating effect as well.245 (Ethylenedinitrilo)tetraacetic acid completely inactivated all of the lyases mentioned. The activity of endopectate lyase from Pseudomonas was also lessened in the presence of sodium chloride, potassium chloride, and dipotassium hydrogen phosphate (K2HP04). 

Type of material Clostridium felsineum Clostridium butylicum ... 

Endo-L-arabinanase activity was found for the first time26 in the culture of Clostridium felsineum var. sikokianum in 1963. Then, in 1975, it was found that B. subtilis F-ll produces this enzyme well,4 and, in 1982, that B. subtilis IFO 3022 is also a producer.44... 

Through the centuries man has used pectic enzymes produced by microorganisms in natural fermentations to modify plant tissue to produce more useful products. One of the oldest fermentations is the process of retting, in which textile fibers, such as flax, hemp, and jute are loosened from their plant stems. Clostridium felsineum, one of the organisms involved in anaerobic retting, produced endopolygalacturonase and endopolygalacturonate lyase but not pectinesterase 178, 179). 

The pectic enzymes of six strains of pigmented, pectolytic Clostridia isolated from potatoes have been examined and compared with those of strains of Clostridium felsineum and C. aurantibutyricum using cup-plate assays. All the organisms were found to produce pectate lyase activity. 

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