Purification and properties of two pectate lyases produced by Erwinia carotovora.

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Abstract
Pectate lyase of E. carotovora Er was separated into 2 active protein fractions, pectate lyases I (pI 10.7) and II (pI 10.1), by electrofocusing. These enzymes could be distinguished by sodium dodecyl sulfate slab gel electrophoresis. Although they showed many similar properties, the optimal temperatures of pectate lyases I and II were 50.degree. and 60.degree. C respectively, and their Km values were 0.12 and 1.1 mg/ml. The amino acid composition was very similar in the 2 enzymes, but pectate lyase I contained a few more residues of lysine, valine, glycine and proline than pectate lyase II and fewer residues of isoleucine. The neutral sugar content of the lyses was 2.5 and 4.8%, respectively. Pectate lyases I and II seem to be different enzyme proteins, despite the fact that they have quite similar properties.