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Induction and characterization of chitinase in hyscinth pea pods

Xia Yuxian, Pei Yan, Li Xianbi, Zhang Lin

Southwest Agricultural University,Biotechanology Research Center.Chongqing 630716

Abstract

Chitinase (EC 3.2.1.14) was purified from the hulls of hyacinth pea pods by affinity chromatography on a column of regenerated chitin and by isoelectric focusing. The purified chitinase gave a single protein band on sodium dodecyl sulfate polyacrylamide gel electrophoresis with a molecular weight of 30 kD. The enzyme was proved to be endochitinase and the isoelectric point (pI) was pH 9.1. The specific activity of the chitinase in the hulls of hyacinth pea pods was about 17 times as high as that in the cotyledons and 11 times that in the embryo. The specific activity of chitinase in the hull increased with development and maturation of the pods. The time course of the change of chitinase activity had a single peak on the 13th day after anthesis. The results indicate that chitinase activity is in relationship with development. The chitinase activity in the hulls and in the seeds of the pods treated with HgCl_(2) was higher than in those of untreated ones. The chitinase activity increase induced by HgCl_(2) was larger in immature pods than in mature ones.

Key words: Hyacinth pea;Chitinase;Purification;Development;Induction

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Citing This Article：

Xia Yuxian, Pei Yan, Li Xianbi, Zhang Lin. Induction and characterization of chitinase in hyscinth pea pods. Acta Physiol Sin 1996; 48 (3): (in Chinese with English abstract).