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Biological and biochemical studies on the ‘basic’ isoenzyme of endo-polygalacturonase secreted by Monilinia fructigena

Published online by Cambridge University Press:  01 October 1997

M. M. SNAPE ,
A. H. FIELDING  and
R. J. W. BYRDE
M. M. SNAPE
Affiliation:
Present address: Ms M. M. Brown, 5 Merstow Place, Evesham, Worcs WR11 4AZ. IACR–Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS18 9AF, U.K.
A. H. FIELDING
Affiliation:
Present address: 9 Beaufort Road, Clifton, Bristol BS8 2JU. IACR–Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS18 9AF, U.K.
R. J. W. BYRDE
Affiliation:
IACR–Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS18 9AF, U.K.
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Abstract

Monilinia fructigena secretes one molecular form of endo-polygalacturonase (PG) in apple fruits infected by it. This PG, purified from culture filtrate to homogeneity, had an Mr of ca 33000 (SDS electrophoresis) and a pI value of ca 9·75. It had little or no effect on the structural integrity of potato tuber tissues, nor on the viability of apple callus cells in suspension. Modification of the lysine units of the purified enzyme by pyridoxal phosphate resulted in ca 50% decrease in PG activity. PG thus modified appeared to bind to an apple fibre preparation less than did PG not treated with pyridoxal phosphate. Lysine residues may thus be involved in subsites binding this PG to carboxyl groups in the polygalacturonate.

Type
Research Article
Information
Mycological Research , Volume 101 , Issue 10 , October 1997 , pp. 1183 - 1189
Copyright
The British Mycological Society 1997

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