Substrate Specificity of Chlorophyllase from Different Plants

Siegrid Schoch3 and M onica Ihl a Botanisches Institut, Universität München, D-80638 München, Menzingerstr. 67, Germany b Departamento de Ingeniena Quimica, Universidad de La Frontera, cas. 54-D, Temuco, Chile Z. Naturforsch. 53c, 21-26 (1998); received September 19/October 11, 1997 Chlorophyll, Chlorophyllase, Substrates Specificity, Vegetables, Zn pheophytin The activity of chlorophyllase (chlorophyll-chlorophyllido-hydrolase, EC 3.1.1.14) ex­ tracted from six different species was compared with enzyme extracted from leaves of Tree of Heaven. The chlorophyllase activity from Swiss chard was similar to the Tree of Heaven enzyme, all the others were less active or inactive. We tested the substrate specificity with bacteriochlorophyll a, chlorophylls a and b. pheophytins a and b and also the synthetic pig­ ments Zn pheophytins a and b and Zn pyropheophytin a. The natural pigments were the best substrates, but the Zn derivatives were also hydrolysed, except Zn pyropheophytin a which was accepted only by the enzyme extracted from the leaves of Tree of Heaven.