Enzymes pectin methylesterase

Other polysaccharides of primary cell walls.-A complex mixture of enzymes including endopolygalacturonase, pectin methylesterase, and/or pectin lyase solubilizes a mixture of polysaccharides from the primary cell walls of fruits [57-64]. Food scientists have referred for some 15 years to this mixture of polysaccharides as the hairy region to describe the highly branched character of the polysaccharides in the fraction and to emphasize the contrast to unbranched homogalacturonan. The recent discovery of rhamnogalacturonan hydrolase [65,66], which selectively cleaves the backbone of RG-I, led to the realization that the hairy... 

Pitkanen, K., Heikinheimo, R. and Pakkanen, R. (1992) Purification and characterization of Erwinia chrysanthemi B374 pectin methylesterase produced by Bacillus subtilis. Enzyme Microb TechnoHA, 832-836. 

Among the five different species of Azospirillurn, only A. irakeme shows clearly pectinolytic activity on solid and in liquid medium. Moreover, this species can grow under non-diazotrophic as well as diazotrophic conditions when pectin is the sole carbon source (Khammas and Kaiser, 1991). Khammas and Kaiser (1991) analysed the pectinolytic activity of seven A. irakense isolates, and gave evidence for the presence of two types of pectinolytic enzymes. All strains tested have inducible Ca dependent pectate lyase activity. Six strains, showed also pectin methylesterase activity. So far, none of the corresponding enzymes have been purified. 

Figure 1 indicates that pectin methyltransferase (PMT) activity from freeze-thawed microsomes measured without exogenous substrate was maximal at neutral pH (6.5 to 7.5). When exogenous pectic substrates of various DE had been added, similar optimal neutral pH was observed, and the activity was slightly stimulated (1.2 to 1.8 times). A second optimal pH occured at pH 5.5, but in the presence of low methylated pectin (DE 0.1). As suggested by Lineweaver and Ballou [8] to explain the behaviour of another pectic enzyme -i.e. pectin methylesterase (PME), the mobility and the activity of PMT might be influenced by the presence of polyanionic substrates. On the other hand, the existence of several forms of pectin methyltransferase in flax microsomes might be responsible for such variations of the activity. 

According to the IUPAC-IUB Enzyme Nomenclature,11 pectinesterase belongs to the carboxyl ester hydrolases (EC 3.1.1.11) and has the systematic name pectin pectyl-hydrolase. The literature also contains the expressions pectin methylesterase, pectin demethoxylase, and pectin methoxylase for the same enzyme. The old name pectase,... 

These protruding structures may form catalytic sites or binding sites for small molecules. Remarkably, some polysaccharide modification enzymes of pathogenic bacteria are similar to enzymes of their host cells. For example, during cell development, pectin, a principal component in the primary cell wall of plants, is modified by its own pectin methylesterases that have /1-solenoid structures (Johansson et al, 2002) and in this respect, resemble pectin lyases secreted by bacteria to break down these structures (Lietzke et al., 1996). 

Pectin methylesterase (PM) is the enzyme which catalyzes the hydrolysis of the methyl ester groups in pectinic acids. In contrast to PG and protopectinase, a great deal of progress has been made during the past decade in our knowledge of PM. The older term pectase, 8 invented before the chemical action of the enzyme was understood, is now used by a decreasing number of workers while the name pectin-... 

Pectic enzymes are defined and classified on the basis of their action toward the galacturonan part of the pectins. Two main groups are distinguished pectin methylesterases (pectin esterase, PE EC 3.1.11.1), which split off methoxy groups from pectin, transforming... 

The enzymes are as follows A, lipase B, hemicellulase C, pectin methylesterase D, protease. Neutral guar used (Supercol from Hercules Incorporated). 

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