Comparison of pectate hydrolases from parsley root cells

Comparison of pectate hydrolases from parsley root cells

Článek recenzovaný mimo WoS a Scopus

Pectate hydrolases of plants are generally supposed to be bound on primary cell wall where the catalysis of homogalacturonan as a side chain of pectin structure occures. These enzymes with terminal action pattern (exopolygalacturonases, EC 3.2.1.67) can be found in each plant species while the production of those with random action pattern (polygalacturonases, EC 3.2.1.15) indicates the requirement of plant tissue softening. Interestingly, while the function, structure and importance of plant polygalacturonases is widely known, the reseach of exopolygalacturonases is still on its beginning. References about the strict preference for polymeric substrates of these enzymes can be found unlike exopolygalacturonases produced by microorganisms which can prefer substrates with lower degree of polymerization, too. Five forms of pectate hydrolases purified from parsley roots cells are described in this work. Only one of them was strictly bound on the cell wall, enzyme with preference for decamer as the substrate. Other three forms, surprisingly with the preference for hexagalacturonate, were found in other cell structures. Only one typical form of exopolygalacturonase with preference for polymeric substrate was identified, partially bound on the cell wall and partially free in cytosole. The action pattern of individual forms for oligogalacturonides was evaluated using HPLC.

Pectate hydrolases of plants are generally supposed to be bound on primary cell wall where the catalysis of homogalacturonan as a side chain of pectin structure occures. These enzymes with terminal action pattern (exopolygalacturonases, EC 3.2.1.67) can be found in each plant species while the production of those with random action pattern (polygalacturonases, EC 3.2.1.15) indicates the requirement of plant tissue softening. Interestingly, while the function, structure and importance of plant polygalacturonases is widely known, the reseach of exopolygalacturonases is still on its beginning. References about the strict preference for polymeric substrates of these enzymes can be found unlike exopolygalacturonases produced by microorganisms which can prefer substrates with lower degree of polymerization, too. Five forms of pectate hydrolases purified from parsley roots cells are described in this work. Only one of them was strictly bound on the cell wall, enzyme with preference for decamer as the substrate. Other three forms, surprisingly with the preference for hexagalacturonate, were found in other cell structures. Only one typical form of exopolygalacturonase with preference for polymeric substrate was identified, partially bound on the cell wall and partially free in cytosole. The action pattern of individual forms for oligogalacturonides was evaluated using HPLC.

pectate hydrolases, exopolygalacturonase

pectate hydrolases, exopolygalacturonase

OMELKOVÁ, J.

2010

09.12.2008

1213-7103

CHEMICKE LISTY

102

15

Česká republika

630

632

3