Open AccessBiochemical characterization of MI‐ENG1, a family 5 endoglucanase secreted by the root‐knot nematode Meloidogyne incognita
Author(s) -
BéraMaillet Christel,
Arthaud Laury,
Abad Pierre,
Rosso MarieNoëlle
Publication year - 2000
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2000.01356.x
Subject(s) - meloidogyne incognita , nematode , cellulase , root knot nematode , enzyme , glycoside hydrolase , biology , biochemistry , microbiology and biotechnology , ecology
A β‐1,4‐endoglucanase named MI‐ENG1, homologous to the family 5 glycoside hydrolases, was previously isolated from the plant parasitic root‐knot nematode Meloidogyne incognita . We describe here the detection of the enzyme in the nematode homogenate and secretion and its complete biochemical characterization. This study is the first comparison of the enzymatic properties of an animal glycoside hydrolase with plant and microbial enzymes. MI‐ENG1 shares many enzymatic properties with known endoglucanases from plants, free‐living or rumen‐associated microorganisms and phytopathogens. In spite of the presence of a cellulose‐binding domain at the C‐terminus, the ability of MI‐ENG1 to bind cellulose could not be demonstrated, whatever the experimental conditions used. The biochemical characterization of the enzyme is a first step towards the understanding of the molecular events taking place during the plant–nematode interaction.