Results 121 to 130 of about 2,218 (162)

Purification of endo‐polygalacturonase by affinity precipitation using alginate

Biotechnology and Applied Biochemistry, 1993
The precipitation of alginate by Ca2+ at pH 3.8 was found to occur concomitantly with the precipitation of endo‐polygalacturonase from Aspergillus niger. Under optimum conditions, 92% of the enzyme activity was precipitated. The enzyme could be recovered from the precipitate by washing with 0.5 M NaCl/0.2 M Ca2+.
MN Gupta, G. Dong, B. Mattiasson
openaire   +1 more source

On the simulation of enzymatic digest patterns: The fragmentation of oligomeric and polymeric galacturonides by endo-polygalacturonase II [PDF]

Biochimica Et Biophysica Acta - General Subjects, 2006
Preprint - has been accepted to Biochimica et Biophysica ...
Randall Cameron
exaly   +6 more sources

Crystallization and Preliminary Crystallographic Characterization of Endo-polygalacturonase II from Aspergillus niger

Journal of Molecular Biology, 1994
The endo-polygalacturonase II from Aspergillus niger has been crystallized from an ammonium sulfate solution by the hanging drop method. The crystals belong to the monoclinic space group P2(1), with cell dimensions a = 69.6 A, b = 152.6 A, c = 74.0 A and beta = 91.2 degrees with four molecules per asymmetric unit.
Bauke Dijkstra
exaly   +4 more sources

Isolation and genetic determination of a Saccharomyces cerevisiae mutant that produces an endo-polygalacturonase

Journal of Bioscience and Bioengineering, 1999
A Saccharomyces cerevisiae mutant that produces an endo-polygalacturonase (PGase) was isolated. The PGase gene was revealed to be located on chromosome X in both the mutant and its parental strain. The 5'-upstream region of the PGase gene in the mutant was entirely identical with that of its parent.
N, Hirose, M, Fujii, M, Kishida, H, Kawasaki, T, Sakai   +4 more
openaire   +2 more sources

Degradation of flax polysaccharides with purified endo-polygalacturonase

Carbohydrate Polymers, 1990
Abstract An endo-polygalacturonase was purified from a commercial preparation of Aspergillus by cation exchange and size exclusion chromatographies. It degraded a polysaccharide extracted from under-retted flax into three general size classes. The first product was a polysaccharide of high molecular weight (close to 100 000), enriched in galactose ...
openaire   +1 more source

Comprehensive glycan analysis of recombinant Aspergillus niger endo-polygalacturonase C

Analytical Biochemistry, 2006
The enzyme PGC is produced by the fungus Aspergillus niger during invasion of plant cell walls. The enzyme has been homologously overexpressed to provide sufficient quantities of purified enzyme for biological studies. We have characterized this enzyme in terms of its posttranslational modifications (PTMs) and found it to be both N- and O-glycosylated.
Bryan, Woosley, Min, Xie, Lance, Wells, Ron, Orlando, Derek, Garrison, Daniel, King, Carl, Bergmann   +6 more
openaire   +2 more sources

Characterization of some endo-polygalacturonases from Sclerotinia sclerotiorum

1996
Abstract The isolation and characterisation of an endo-polygalacturonase from S. sclerotiorum is reported. The purified glycoprotein has a molecular mass of 42 KDa and a pI of 4.8 and shows the enzymatic characteristics an endo-polygalacturonase.
M.B. Martel, R. Létoublon, M. Fèvre
openaire   +1 more source

Polygalacturonic Acid/endo-Polygalacturonase System: A Kinetic Study in Batch Reactors

Biotechnology Progress, 2004
The enzymatic depolymerization of the pectic substance polygalacturonic acid (PGA) is studied in batch reactor. The number-average molecular weight of native substrate is estimated, using a simple and quick technique, to be approximately 11.1 kDa, the polymeric chains consisting on average of 63 galacturonic acid units.
GALLIFUOCO, ALBERTO, CANTARELLA, Maria, VIPARELLI P., MARUCCI M.   +3 more
openaire   +3 more sources

Immobilization of endo-polygalacturonase from Aspergillus ustus on silica gel

Biotechnology Letters, 2000
Endo-polygalacturonase from Aspergillus ustus when immobilized on to modified silica gel retained 28% of its original activity. The immobilized enzyme could be re-used through 10 cycles of reaction with almost 90% retention of its original activity. It had increased thermostability over its soluble form: the half-life of the soluble enzyme at 40 °C was
M. Narsimha Rao, A.A. Kembhavi, A. Pant
openaire   +1 more source

PURIFICATION AND PARTIAL CHARACTERIZATION OF AN ENDO-POLYGALACTURONASE FROM ASPERGILLUS NIGER

Journal of Food Biochemistry, 2002
A pectinase was identified and isolated from a commercial Aspergillus niger pectinase preparation. The crude enzyme preparation, which was prepared by precipitation of the water extract of the culture of A. niger with ammonium sulfate, was further fractionated by three steps of chromatography, i.
Guo, C.T., Xue, W.M., Deng, W.H., Chen, Tianbao, Rao, P.F.   +4 more
openaire   +2 more sources