Partial purification and properties of extracellular chitinase produced by Acremonium obclavatum, an antagonist to the groundnut rust, Puccinia arachidis

1994 ◽  
Vol 10 (3) ◽  
pp. 342-345 ◽  
Author(s):  
K. R. Gunaratna ◽  
R. Balasubramanian
2000 ◽  
Vol 78 (2) ◽  
pp. 168-174 ◽  
Author(s):  
M Sathiyabama ◽  
R Balasubramanian

Apoplastic β-1,3 glucanases (G1, G2) of Arachis hypogaea L. (peanut) leaves treated with glucan have been partially purified by ammonium sulphate precipitation, sephadex G-100, CM-Sephadex, DEAE-Sephadex chromatography, and preparative native PAGE electrophoretic techniques. The pI values of purified enzymes G1 and G2 were near 8 and 4, respectively. The apparent molecular masses of purified glucanases G1 and G2 from glucan-treated peanut leaves were 36 and 34 kDa, respectively. Both isoforms (G1 and G2) showed their pH optimum of 5.0 and temperature optimum of 40°C. The partially purified enzymes hydrolysed laminarin better than other substrates and inhibited uredospore germination of Puccinia arachidis. Both isoforms (G1 and G2) inhibited spore germination of some biocontrol agents such as Acremonium obclavatum W. Gams, Myrothecium verrucaria (Alb. Schw.) Ditmer, Fusarium solani (Mart.) Sacc., and Trichoderma harzianum Rifai.Key words: Acremonium obclavatum, Arachis hypogaea, β-1,3 glucanase, glucan, inhibition, Puccinia arachidis.


1991 ◽  
Vol 81 (3) ◽  
pp. 327-334 ◽  
Author(s):  
Cesar V. Mujer ◽  
Dale W. Kretchman ◽  
A. Raymond Miller

1995 ◽  
Vol 94 (4) ◽  
pp. 629-634 ◽  
Author(s):  
Mohamed Benichou ◽  
Gracia Martinez-Reina ◽  
Felix Romojaro ◽  
Jean-Claude Pech ◽  
Alain Latche

1985 ◽  
Vol 260 (2) ◽  
pp. 1096-1102
Author(s):  
P R DiMaria ◽  
G Kaltwasser ◽  
C J Goldenberg

1985 ◽  
Vol 45 (6) ◽  
pp. 1903-1910 ◽  
Author(s):  
Jacques-Andre Maring ◽  
Richard A. Deitrich ◽  
Roger Little

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