Pectinase
Pectinase structure
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Common Name | Pectinase | ||
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| CAS Number | 9032-75-1 | Molecular Weight | 150.130 | |
| Density | 1.5±0.1 g/cm3 | Boiling Point | 415.5±38.0 °C at 760 mmHg | |
| Molecular Formula | C18H37N(CH3)2 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | 219.2±23.3 °C | |
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A Pectate Lyase-Coding Gene Abundantly Expressed during Early Stages of Infection Is Required for Full Virulence in Alternaria brassicicola.
PLoS ONE 10 , e0127140, (2015) Alternaria brassicicola causes black spot disease of Brassica species. The functional importance of pectin digestion enzymes and unidentified phytotoxins in fungal pathogenesis has been suspected but not verified in A. brassicicola. The fungal transcription f... |
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Low concentrations of the toxin ophiobolin A lead to an arrest of the cell cycle and alter the intracellular partitioning of glutathione between the nuclei and cytoplasm.
J. Exp. Bot. 66 , 2991-3000, (2015) Ophiobolin A, a tetracyclic sesterpenoid produced by phytopathogenic fungi, is responsible for catastrophic losses in crop yield but its mechanism of action is not understood. The effects of ophiobolin A were therefore investigated on the growth and redox met... |
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Polysaccharide-free nucleic acids and proteins of Abelmoschus esculentus for versatile molecular studies.
Mol. Biol. (Mosk.) 46(4) , 598-604, (2012) Abelmoschus esculentus (okra) is one of the polysaccharide rich crop plants. The polysaccharides interfere with nucleic acids and protein isolation thereby affecting the downstream molecular analysis. So, to understand the molecular systematics of okra, high ... |
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Grape marcs as unexplored source of new yeasts for future biotechnological applications.
World J. Microbiol. Biotechnol. 29(9) , 1551-62, (2013) In recent years the potential of using microbes as biotechnological sources of industrially relevant enzymes has stimulated a renewed interest in the exploration of new unconventional habitats like trove of natural biodiversity. In this work, grape marcs was ... |
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Synthesis and sensory evaluation of ent-kaurane diterpene glycosides.
Molecules 17(8) , 8908-16, (2012) Catalytic hydrogenation of the three ent-kaurane diterpene glycosides isolated from Stevia rebaudiana, namely rubusoside, stevioside, and rebaudioside-A has been carried out using Pd(OH)₂ and their corresponding dihydro derivatives have been isolated as the p... |
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Purification and physicochemical properties of polygalacturonase from Aspergillus niger MTCC 3323.
Protein Expr. Purif. 87(1) , 11-6, (2013) Polygalacturonases are the pectinolytic enzymes that catalyze the hydrolytic cleavage of the polygalacturonic acid chain. In the present study, polygalacturonase from Aspergillus niger (MTCC 3323) was purified. The enzyme precipitated with 60% ethanol resulte... |
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Pectinase hydrolysis of Dendrobium huoshanense polysaccharide and its effect on protein nonenzymatic glycation.
Int. J. Biol. Macromol. 61 , 439-47, (2013) The aim of this study was to investigate the inhibitory effects of molecular weight alteration of Dendrobium huoshanense polysaccharide on protein nonenzymatic glycation. For this purpose, one homogeneous active polysaccharide DHPD1 with molecular weight 3.2 ... |
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Production of polygalacturonases by Aspergillus section Nigri strains in a fixed bed reactor.
Molecules 18(2) , 1660-71, (2013) Polygalacturonases (PG) are pectinolytic enzymes that have technological, functional and biological applications in food processing, fruit ripening and plant-fungus interactions, respectively. In the present, a microtitre plate methodology was used for rapid ... |
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Functional properties of a manganese-activated exo-polygalacturonase produced by a thermotolerant fungus Aspergillus niveus.
Folia Microbiol. (Praha) 58(6) , 615-21, (2013) A thermotolerant fungus identified as Aspergillus niveus was isolated from decomposing materials and it has produced excellent levels of hydrolytic enzymes that degrade plant cell walls. A. niveus germinated faster at 40 °C, presenting protein levels almost t... |
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Validation of reference genes for gene expression analysis in Valsa mali var. mali using real-time quantitative PCR.
World J. Microbiol. Biotechnol. 29(9) , 1563-71, (2013) Valsa mali var. mali (Vmm), is the predominant species of apple valsa canker in China. Modern analysis of genes involved in virulence or pathogenicity usually implicate gene expression analysis most often performed using real-time quantitative polymerase chai... |