In plant bacterial pathogens such as " Erwinia carotovora " and in fungal pathogens such as " Aspergillus niger ", pectinesterase is involved in maceration and soft-rotting of plant tissue.
22.
These include alpha-amylase from bacteria, which converts starch to simple sugars, chymosin from bacteria or fungi, which clots milk protein for cheese making, and pectinesterase from fungi, which improves fruit juice clarity.
23.
In plants, pectinesterase plays a role in the modulation of cell wall mechanical stability during fruit ripening, cell wall extension during pollen germination and pollen tube growth, abscission, stem elongation, tuber yield and root development.
24.
A cell wall-associated pectinesterase of " Nicotiana tabacum " is involved in host cell receptor recognition for the tobacco mosaic virus movement protein and it has been shown that this interaction is required for cell-to-cell translocation of the virus.
25.
It has now been shown that some plant pectinesterase isoforms may exhibit both mechanisms and that such mechanisms are driven by alterations in pH . The optimal pH of higher plants is usually between pH 7 and pH 8 although the pH of pectinesterase from fungi and bacteria is usually much lower than this.
26.
It has now been shown that some plant pectinesterase isoforms may exhibit both mechanisms and that such mechanisms are driven by alterations in pH . The optimal pH of higher plants is usually between pH 7 and pH 8 although the pH of pectinesterase from fungi and bacteria is usually much lower than this.
27.
The first three-dimensional structure solved for a plant pectinesterase was for an isoform from carrot ( " Daucus carota " ) root and consists of a right-handed parallel ?-helix as seen in all the carbohydrate esterase family CE-8, a transmembrane domain and a pectin binding cleft . Similarly several pectinesterase structures have been elucidated in fungi and " E . coli " and share most of the structural motifs seen in plants.
28.
The first three-dimensional structure solved for a plant pectinesterase was for an isoform from carrot ( " Daucus carota " ) root and consists of a right-handed parallel ?-helix as seen in all the carbohydrate esterase family CE-8, a transmembrane domain and a pectin binding cleft . Similarly several pectinesterase structures have been elucidated in fungi and " E . coli " and share most of the structural motifs seen in plants.
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