Detail publikace

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

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

Originální název

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

Typ

článek v časopise - ostatní, Jost

Jazyk

angličtina

Originální abstrakt

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.

Klíčová slova

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

Autoři

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

Rok RIV

2009

Vydáno

2. 4. 2009

ISSN

0006-3088

Periodikum

Biológia

Ročník

2009 (64)

Číslo

2

Stát

Spojené státy americké

Strany od

228

Strany do

234

Strany počet

7

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"
}