Purification and Properties of Soluble Chlorophyllase from Tea Leaf Sprouts

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Soluble chlorophyllase (chlorophyll-chlorophyllido-hydrolase, EC 3.1.1.14) was purified 650-fold from tea leafsprouts by ammonium sulfate fractionation and gel filtration through Sephadex G-200 and Sepharose CL-6B. The purified enzyme showed two bands on polyacrylamide gel electrophoresis and the specific activity was 2.6μmol chlorophyll a hydrolyzed min^<-1> mg^<-1> of protein. The molecular weights determined by Sepharose CL-6B were 910,000 and 350,000, indicating high molecular aggregates. The subunit molecular weight estimated by sodium lauryl sulfate-polyacrylamide gel electrophoresis was 38,000. The isoelectric point was 3.9. The optimum pH was 5.5 in acetate buffer and the K_m value for chlorophyll a was 10μM. This enzyme did not require a thiol compound nor metal ion such as Mg^<2+>.
日本植物生理学会の論文