Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis.

Abstract

We found two enzymes that solubilize pectin from protopectin, tentatively named protopectinase-N (PPase-N) and protopectinase-R (PPase-R), in a culture filtrate of Bacillus subtilis IFO 3134. These enzymes were purified to homogeneity by hydrophobic, cation exchange and size exclusion chromatographies. The molecular weights of PPase-N and PPase-R were estimated to be 43,000 and 35,000, respectively, by SDS-PAGE. Their pIs were 9.4 and 8.2, respectively. These enzymes were stable in a wide range of pH and temperature. PPase-N and -R released water-soluble pectin by transeliminative cleavage of protopectin. According to their substrate specificities and modes of action, PPase-N and PPase-R could be classified as endo-pectate transeliminase (pectate lyase; EC 4.2.2.2) and endo-pectin transeliminase (pectin lyase; EC 4.2.2.10), respectively. Both enzymes were produced in a simple medium containing defatted soybean flour and phosphates. Production of PPase-N was repressed by addition of glucose while that of PPase-R was enhanced by phosphate.

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@article{Sakamoto1994PurificationCA, title={Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis.}, author={Taro Sakamoto and Roque Alberto Hours and Tsutomu Sakai}, journal={Bioscience, biotechnology, and biochemistry}, year={1994}, volume={58 2}, pages={353-8} }