Erwinia aroideae

By separation Irom bacterial culture such as Escherichia coli, Serratia marcescens, Erwinia aroideae, Erwinia atroseptica, Erwinia carotovora. 

The pH optimum of both exopectate lyases lies in the alkaline region. The pH optimum of exopectate lyase of Erwinia aroideae is influenced by univalent cations. The enzyme activated by K+ and NH4+ has its pH optimum at 8.0, but, in the presence of Na+ ions, it is shifted towards the alkaline region. 

Hatanaka and Ozawa17 purified, from the cell extract of Erwinia aroideae, an enzyme preferring the unsaturated disaccharide as substrate, and classified it as an unsaturated oligo-D-galac-tosiduronate lyase. ... 

Hatanaka and Ozawa studied oligogalacturonate lyases from Erwinia aroideae (54) and a Pseudomonas species (55), which are apparently similar to the one described by Moran et al. (53). With the Erwinia enzyme polygalacturonic acid was degraded more slowly than oligogalacturonate, and unsaturated oligogalacturonates were attacked the most rapidly. The unsaturated dimer forms two molecules of 4-deoxy-5-keto-D-fructuronic acid. The process by which the unsaturated monomer is converted to this product is not known. Ca was not required for activity. 

Okamoto et al, (46, 47, 48, 49) isolated a polygalacturonate lyase from Erwinia aroideae. Since an acid soluble pectic acid was degraded to unsaturated digalacturonic acid and continually shortening chains, these authors also concluded that the attack was from the reducing end. 

Cytochrome 6-562 of E. coli has been highly purified and well characterized 172,173,201). It has also been purified from Erwinia aroideae, Erwinia carotovoro, and Serratia marcescens 202). Spectrally similar cytochromes are also found in Xanthomonas phaseoli 114) and Bacterium anitratum 174)- The Serratia and Bacterium cytochromes have been established to react as an electron acceptor of dehydrogenases 173,174,203). 

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