pgaD encodes a new type of endopolygalacturonase from Aspergillus niger

We isolated and characterized a new type of endopolygalacturonase (PG)-encoding gene, pgaD, from Aspergillus niger. The primary structure of PGD differs from that of other A. niger PGs by a 136 amino acid residues long N-terminal extension. Biochemical analysis demonstrated extreme processive behavior of the enzyme on oligomers longer than five galacturonate units. Furthermore, PGD is the only A. niger PG capable of hydrolyzing di-galacturonate. It is tentatively concluded that the enzyme is composed of four subsites. The physiological role of PGD is discussed.

Bibliographic Details

Main Authors:	Parenicova, L., Kester, H.C.M., Benen, J.A.E., Visser, J.
Format:	Article/Letter to editor biblioteca
Language:	English
Subjects:	Aspergillus niger, Endopolygalacturonase, Methylated oligogalacturonate, Processivity,
Online Access:	https://research.wur.nl/en/publications/pgad-encodes-a-new-type-of-endopolygalacturonase-from-aspergillus
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