Publication detail

Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots

OMELKOVÁ, J. FLODROVÁ, D. STRATILOVÁ, E.

Original Title

Type

journal article - other

Language

English

Original Abstract

The main form of pectate hydrolases in the cell wall of parsley roots showed a unique substrate preference of a plant exopolygalacturonase because it clearly preferred the substrates with degree of polymerization about 10. This form was separated from the others, purified and characterized. Enzyme exhibited sharp pH optimum corresponding to pH 4.7, molecular mass 53.5 kDa, and isoelectric point 5.3. It was stable at 50A degrees C in 2-h assay and had optimum of temperature at 60A degrees C (activation energy being 37.0 kJ/mol). The interaction with concanavalin A indicated the glycosylation of enzyme. Substrates were cleaved from the non-reducing end.

Keywords

EXO-D-GALACTURONANASE; ASPERGILLUS-NIGER; GLYCOSIDE HYDROLASES; BIOCHEMICAL-CHARACTERIZATION; ENDOPOLYGALACTURONASE-I; CRYSTAL-STRUCTURE; EXOPOLYGALACTURONASE; POLYGALACTURONASE; CARROT; CHROMATOGRAPHY

Authors

OMELKOVÁ, J.; FLODROVÁ, D.; STRATILOVÁ, E.

RIV year

2009

Released

2. 4. 2009

ISBN

0006-3088

Periodical

Biológia

Year of study

2009 (64)

Number

State

United States of America

Pages from

228

Pages to

234

Pages count

BibTex

@article{BUT48997,
  author="Jiřina {Omelková} and Dana {Flodrová} and Eva {Stratilová}",
  title="Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots",
  journal="Biológia",
  year="2009",
  volume="2009 (64)",
  number="2",
  pages="228--234",
  issn="0006-3088"
}