Results 171 to 180 of about 18,318 (222)

Polygalacturonase in strawberry fruit

Phytochemistry, 1993
Abstract A low level of exo- and endo-polygalacturonase has been found in strawberry fruit (Fragaria ananassa, Duch. cv. Toyonoka).
Nogota, Y., Ohta, H., Voragen, A.G.J.
exaly   +2 more sources

Strain and process for production of polygalacturonase

Enzyme and Microbial Technology, 1990
A process was developed for the production of polygalacturonase (poly-1,4-α-d-galacturonide glycanohydrolase, EC 3.2.1.15) by Aspergillus niger VTT-D-77050 and its mutant VTT-D-86267. High levels of production were obtained in laboratory fermentations on a beet extraction waste medium.
Pessa Erkki, Bailey Michael
exaly   +3 more sources

Inhibition of polygalacturonase from Verticillium dahliae by a polygalacturonase inhibiting protein from cotton

Phytochemistry, 2001
An extracellular endo-polygalacturonase (PGase) [E.C. 3.2.1.15] was isolated from 18-day-old culture filtrates of Verticillium dahliae and partially purified using gel permeation chromatography. The band responsible for PGase activity was electrophoretically characterized as having a molecular mass of approximately 29 500 and an isoelectric point of 5 ...
Ian A Dubery
exaly   +3 more sources

The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex

Journal of Molecular Biology, 2001
Polygalacturonases hydrolyze the alpha-(1-4) glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall. Crystal structures of polygalacturonase from Aspergillus aculeatus were determined at pH 4.5 and 8.5 both to 2.0 A resolution. A.
S W, Cho, S, Lee, W, Shin
exaly   +3 more sources

Properties of yeast polygalacturonase

Archives of Biochemistry and Biophysics, 1954
Abstract Various properties were studied of the exocellular polygalacturonase of the yeast Saccharomyces fragilis (strain #351). Yeast polygalacturonase (YPG) was partially purified, until the activity was 2.03 (PGu)mgTN. YPG is not accompanied by pectinesterase.
B S, LUH, H J, PHAFF
openaire   +2 more sources

Pectin-polygalacturonase in Citrus

Planta, 1976
Extracts from citrus [Citrus sinensis (L.) Osbeck] pedicles rated as containing polygalacturonase and cellulase gave activities both as measured with carboxymethylcellulose and with sodium polypectate. Gel electrophrosis of the extract demonstrated two region areas that contained cellulytic activity.
F M, Basiouny, R H, Biggs
openaire   +2 more sources

Polygalacturonases

2002
Polygalacturonases are enzymes that cleave the alpha-1,4-D-galacturonosidic linkage by ...
Benen, J.A.E., Visser, J.
openaire   +2 more sources

Polygalacturonases, polygalacturonase-inhibiting proteins and pectic oligomers in plant–pathogen interactions

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2004
Polygalacturonases (PGs) are produced by fungal pathogens during early plant infection and are believed to be important pathogenicity factors. Polygalacturonase-inhibiting proteins (PGIPs) are plant defense proteins which reduce the hydrolytic activity of endoPGs and favor the accumulation of long-chain oligogalacturonides (OGs) which are elicitors of ...
D'OVIDIO R, MATTEI, Maria Benedetta, ROBERTI S, BELLINCAMPI, Daniela   +3 more
openaire   +3 more sources

Two forms of polygalacturonase in tomatoes

Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
Abstract Two polygalacturonidases, (poly--1, 4-galacturonide glycanobydrolase, EC 3.2.1.15) (polygalacturonases I and II) have been separated from extracts of ripe tomatoes by chromatography on DEAE-Sephadex A-50. Polygalacturonase II was the predominant enzyme in all of the samples examined.
R, Pressey, J K, Avants
openaire   +2 more sources

A quantitative bioassay specific for polygalacturonases

Analytical Biochemistry, 1969
Abstract A bioassay for PG activity based on fresh weight loss of cucumber pericarp tissue is described which is specific, quantitative, sensitive and reproducible. The assay is at least 500 times more sensitive than previously described techniques.
H W, Mussell, D J, Morre
openaire   +2 more sources