, Volume 157, Issue 1, pp 22–31 | Cite as

Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function

  • T. Boller
  • A. Gehri
  • F. Mauch
  • U. Vögeli


Ethylene induced an endochitinase in primary leaves of Phaseolus vulgaris L. The enzyme formed chitobiose and higher chitin oligosaccharides from insoluble, colloidal or regenerated chitin. Less than 5% of the total chitinolytic activity was detected in an exochitinase assay proposed by Abeles et al. (1970, Plant Physiol. 47, 129–134) for ethylene-induced chitinase. In ethylene-treated plants, chitinase activity started to increase after a lag of 6 h and was induced 30 fold within 24 h. Exogenously supplied ethylene at 1 nl ml−1 was sufficient for half-maximal induction, and enhancement of the endogenous ethylene formation also enhanced chitinase activity. Cycloheximide prevented the induction. Among various hydrolases tested, only chitinase and, to a lesser extent, β-1,3-glucanase were induced by ethylene. Induction of chitinase by ethylene occurred in many different plant species. Ethylene-induced chitinase was purified by affinity chromatography on a column of regenerated chitin. Its apparent molecular weight obtained by sodium dodecyl sulfate-gel electrophoresis was 30,000; the molecular weight determined from filtration through Sephadex G-75 was 22,000. The purified enzyme attacked chitin in isolated cell walls of Fusarium solani. It also acted as a lysozyme when incubated with Micrococcus lysodeikticus. It is concluded that ethylene-induced chitinase functions as a defense enzyme against fungal and bacterial invaders.

Key words

Chitinase Defense (against bacteria, fungi) Enzyme induction Ethylene Lysozyme Phaseolus (chitinase) 



1-aminocyclopropane-1-carboxylic acid






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Copyright information

© Springer-Verlag 1983

Authors and Affiliations

  • T. Boller
    • 1
  • A. Gehri
    • 1
  • F. Mauch
    • 1
  • U. Vögeli
    • 1
  1. 1.Botanisches Institut der UniversitätBaselSwitzerland

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