Pectic Enzymes

Rexová-Benková, Ľubomíra; Markovič, Oskar

doi:10.1016/s0065-2318(08)60285-1

Cited by 306 publications

(157 citation statements)

References 213 publications

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“…Pectate hydrolases with terminal action pattern preferring oligomeric substrates were described as typical enzymes produced by various microorganisms (Rexová -Benková and Markovič, 1976). To prevent misinterpretation of results obtained with roots cropped from the field (possibility of contamination) sterile cell cultures from these roots growing on solid and liquid medium were prepared.…”

Section: Resultsmentioning

confidence: 99%

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Pectate Hydrolases of Parsley (Petroselinum crispum) Roots

Flodrová

Dzúrovä

Lišková

et al. 2007

Zeitschrift Für Naturforschung C

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The presence of various enzyme forms with terminal action pattern on pectate was evaluated in a protein mixture obtained from parsley roots. Enzymes found in the soluble fraction of roots (juice) were purified to homogeneity according to SDS-PAGE, partially separated by preparative isoelectric focusing and characterized. Three forms with pH optima 3.6, 4.2 and 4.6 clearly preferred substrates with a lower degree of polymerization (oligogalacturonates) while the form with pH optimum 5.2 was a typical exopolygalacturonase [EC 3. 2.1.67] with relatively fast cleavage of polymeric substrate. The forms with pH optima 3.6, 4.2 and 5.2 were released from the pulp, too. The form from the pulp with pH optimum 4.6 preferred higher oligogalacturonates and was not described in plants previously. The production of individual forms in roots was compared with that produced by root cells cultivated on solid medium and in liquid one.

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Section: Resultsmentioning

confidence: 99%

“…Substrates for these enzymes are polygalacturonic and oligogalacturonic acids and, in contrast to polygalacturonases [EC 3.2.1.15], also di-d-(galactosiduronic) acid (Rexová -Benková and Markovič, 1976). The particular enzymes differ from each other by the range and rate of the effects on substrate in relation to the chain length.…”

Section: Introductionmentioning

confidence: 99%

Pectate Hydrolases of Parsley (Petroselinum crispum) Roots

Flodrová

Dzúrovä

Lišková

et al. 2007

Zeitschrift Für Naturforschung C

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“…It catalyzes the deesterification of galactosyluronate methyl esters of pectin to their free carboxyl groups. PME activity has been detected in most plant tissues; however, the enzyme is particularly associated with ripening fruit, abscission zones, and maturing cell walls (Rexova-Benkova and Markovic, 1976;Sexton and Roberts, 1982;Huber, 1983a;Northcote, 1986). lncreases in PME enzyme activity have been reported during ripening of several fruits, including tomato (Tucker et al, 1982;Harriman et al, 1991).…”

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confidence: 99%

An Antisense Pectin Methylesterase Gene Alters Pectin Chemistry and Soluble Solids in Tomato Fruit.

et al. 1992

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Pectin methylesterase (PME, EC 3.1.11) demethoxylates pectins and is believed to be involved in degradation of pectic cell wall components by polygalacturonase in ripening tomato fruit. We have introduced antisense and sense chimeric PME genes into tomato to elucidate the role of PME in fruit development and ripening. Fruits from transgenic plants expressing high levels of antisense PME RNA showed

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“…In contrast, the PGs exhibited a much longer lag time, although fairly high levels of ethylene were eventually produced by both enzymes. The difference in response time for the lyases and hydrolases may be due to highly esterified pectin in citrus which would be less susceptible to degradation by PGs (17). The enzyme-treated oranges developed areas of Chl breakdown around the injection sites which increased with time.…”

Section: Effects Of the Enzymes On Ethylene Productionmentioning

confidence: 99%

Pectic Enzymes in Pectolyase

Baldwin¹,

Pressey²

1989

Plant Physiol.

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The pectic enzymes in Pectolyase were separated by ion exchange chromatography on Q-Sepharose. Three pectin lyases, two polygalacturonases, and a pectinmethylesterase were resolved. The enzymes were further purified on Mono 0 and/or Mono S columns to remove traces of cellulase. The enzymes had molecular weights ranging from 25,000 to 36,000 daltons. They were optimally active between pH 4.0 and 6.2 and were not greatly affected by ions. The pectin lyases and polygalacturonases were endo-enzymes. They solubilized uronic acids from washed cell wall fragments, but the lyases were much more effective than the polygalacturonases. The mixture of enzymes constituting Pectolyase increased ethylene production 15-to 25-fold when introduced into tomato and orange fruits. The enzymes purified from Pectolyase all increased ethylene production in the fruits but the lyases were generally more effective than the hydrolases.Pectolyase is a commercially available enzyme mixture prepared from culture filtrates of Aspergillus japonicus (8,13). These enzymes in combination with cellulases are very effective in degrading cell walls and thereby liberating protoplasts. For this reason, Pectolyase is widely used to generate protoplasts in cell culture research. There have been several attempts to identify the cell wall degrading enzymes in Pectolyase to explain the effectiveness of this preparation. Ishii and coworkers (10, 11) separated an endo-PG' (EC 3.2.1.15) and an endo-PL (EC 4.2.2.3) from the culture filtrates. They also obtained evidence that the solutions contained a maceration stimulation factor which enhanced the action of both enzymes on cell walls (9). The combination of enzymes able to degrade pectate and pectin plus the enzyme activator appeared to be the basis for the potency of Pectolyase in liberating protoplasts.Our interest in the pectic enzymes in Pectolyase stems from the observation that purified tomato PG induced ethylene production and accelerated ripening when infiltrated into green tomato fruit (4). We wanted to expand these studies to microbial pectic enzymes and selected Pectolyase as a source. Attempts to separate the PL and PG (10, 11) revealed that the Pectolyase contained several isoenzymes of each. This ' Abbreviations: PG, polygalacturonase; PL, pectin lyase; PME, pectinmethylesterase.paper describes the separation and properties of the enzymes and their effectiveness in inducing ethylene production in tomato and orange fruit. MATERIALS AND METHODS SubstratesCitrus pectin (Sigma Chemical Co.) was purified by precipitation from a 1% aqueous solution by the addition of two volumes of ethanol, followed by washing with ethanol and acetone. Polygalacturonic acid was prepared from pectate (Sigma Chemical Co.) by partial hydrolysis as described earlier (15). Cell walls were prepared from the fruits of apple, nectarine, cucumber, and tomato and the roots of carrot and radish by homogenizing 100 g of tissue with 200 mL of0.5 M sodium phosphate (pH 7.0). The insoluble material was collected by centrifuga...

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Pectic Enzymes

Cited by 306 publications

References 213 publications

Pectate Hydrolases of Parsley (Petroselinum crispum) Roots

Pectate Hydrolases of Parsley (Petroselinum crispum) Roots

An Antisense Pectin Methylesterase Gene Alters Pectin Chemistry and Soluble Solids in Tomato Fruit.

Pectic Enzymes in Pectolyase

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