Results 131 to 140 of about 6,645 (176)
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2002
In this chapter the differences and similarities between pectate lyases and pectin lyases are ...
Benen, J.A.E., Visser, J.
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In this chapter the differences and similarities between pectate lyases and pectin lyases are ...
Benen, J.A.E., Visser, J.
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Evolutionary Analysis of Pectin Lyases of the Genus Colletotrichum
Journal of Molecular Evolution, 2017Pectin lyases (PNLs) are important enzymes that are involved in plant cell wall degradation during the infection process. Colletotrichum is a diverse genus of fungi, which allows the study of the evolution of PNLs and their possible role in pathogen-host interactions and lifestyle adaptations. The phylogenetic reconstruction of PNLs from Colletotrichum
Alicia, Lara-Márquez +5 more
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In silico analysis of pectin lyase and pectinase sequences
Biochemistry (Moscow), 2009A total of 48 full-length protein sequences of pectin lyases from different source organisms available in NCBI were subjected to multiple sequence alignment, domain analysis, and phylogenetic tree construction. A phylogenetic tree constructed on the basis of the protein sequences revealed two distinct clusters representing pectin lyases from bacterial ...
P K, Yadav +4 more
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Current Genetics, 1990
Using the previously cloned Aspergillus niger N756 pectin lyase D gene as a probe, the corresponding pelD gene has been isolated from a genomic library of the laboratory strain A. niger N400. This gene encodes PLD, previously described as PLI, which is one of the two major pectin lyases isolated from the commercial pectinase preparation Ultrazym ...
Harmsen, J.A.M. +2 more
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Using the previously cloned Aspergillus niger N756 pectin lyase D gene as a probe, the corresponding pelD gene has been isolated from a genomic library of the laboratory strain A. niger N400. This gene encodes PLD, previously described as PLI, which is one of the two major pectin lyases isolated from the commercial pectinase preparation Ultrazym ...
Harmsen, J.A.M. +2 more
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Partial purification and properties of pectin lyase from Penicillium expansum
World Journal of Microbiology and Biotechnology, 1993A pectin lyase, poly(methoxygalacturonide) lyase, EC 4.2.2.10, from a culture filtrate of Penicillium expansum was partially purified 33-fold with 7.3% yield. The enzyme was monomeric with a molecular mass of 36.5 kDa. The enzyme did not contain pectate lyase activity and degraded citrus and apple pectin best at pH 7.0 and 40 to 45°C.
Tempest D W, M M Attwood, D W Tempest
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Pectin lyase is a key enzyme in the maceration of potato tuber
Journal of the Science of Food and Agriculture, 1997The maceration of potato tuber (Solanum tuberosum cv Bintje) by technical enzyme preparations was examined with the aid of fluorescence microscopy using fluorescein diacetate as a dye. Treatment with Pectinex Ultra-SP-L from Aspergillus aculeatus resulted in a higher release of single viable cells and smaller clumps of cells than treatment with ...
van den Broek, L.A.M. +4 more
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Purification and characterization of pectin lyase secreted by Penicillium citrinum
Biochemistry (Moscow), 2009The importance of various parameters such as sugarcane juice concentration, pH of the medium, and effects of different solid supports for maximum secretion of pectin lyase from Penicillium citrinum MTCC 8897 has been studied. The enzyme was purified to homogeneity by Sephadex G-100 and DEAE-cellulose chromatography. The molecular mass determined by SDS-
S, Yadav +3 more
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Yeast, 1994
AbstractThe catalytic capacity of several excreted pectinolytic enzymes obtained from various yeast strains was examined using in vivo and biochemical techniques. Of the 33 yeast strains studied, 30 were isolated from champagne wine during alcoholic fermentation.
A, Gainvors +5 more
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AbstractThe catalytic capacity of several excreted pectinolytic enzymes obtained from various yeast strains was examined using in vivo and biochemical techniques. Of the 33 yeast strains studied, 30 were isolated from champagne wine during alcoholic fermentation.
A, Gainvors +5 more
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Isolation and characterization of extracellular pectin lyase from Penicillium canescens
Biochemistry (Moscow), 2007Pectin lyase A (molecular weight 38 kD by SDS-PAGE, pI 6.7) was purified to homogeneity from culture broth of the mycelial fungus Penicillium canescens using chromatographic techniques. During genomic library screening, the gene encoding pectin lyase A from P.
Alexander Gusakov +2 more
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Analytical Biochemistry, 2001
Several methods have been described for the detection and quantification of polygalacturonase (PG) and pectin lyase (PL) activities. The most frequently used tests are the Nelson method using copper(II) and an arsenomolybdate reagent to detect PG activity, and the colorimetric method using thiobarbituric acid (TBA) to detect PL activity.
M, Nedjma, N, Hoffmann, A, Belarbi
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Several methods have been described for the detection and quantification of polygalacturonase (PG) and pectin lyase (PL) activities. The most frequently used tests are the Nelson method using copper(II) and an arsenomolybdate reagent to detect PG activity, and the colorimetric method using thiobarbituric acid (TBA) to detect PL activity.
M, Nedjma, N, Hoffmann, A, Belarbi
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