Multiple forms of polygalacturonase from banana fruits

Pathak, Neelam; Sanwal, G.G.

doi:10.1016/s0031-9422(98)00005-3

Cited by 112 publications

(59 citation statements)

References 33 publications

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“…Polygalacturonase activity was assayed according to the method described by Pathak and Sanwal (1998). The reaction mixture contained 0.2 ml sodium acetate buffer (200 mM, pH 4.5), 0.1 ml NaCl (200 mM), and 0.3 ml Polygalacturonic Acid (PGA, 1% aqueous solution adjusted to pH 4.5) and 0.05 ml of enzyme extract in a total volume of 1.0 ml.…”

Section: Assay Of Polygalacturonase (Pg)mentioning

confidence: 99%

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Gum Ghatti Based Edible Coating Emulsion with an Additive of Clove Oil Improves the Storage Life and Maintains the Quality of Papaya (Carica papaya L., cv. Madhu bindu)

Joshi¹,

Baraiya²,

Vyas³

et al. 2017

Int.J.Curr.Microbiol.App.Sci

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Section: Assay Of Polygalacturonase (Pg)mentioning

confidence: 99%

“…Cellulase activity was assayed by the method described by Pathak and Sanwal (1998) cited by Lohani et al, (2004). The reaction mixture contained 0.25 ml sodium acetate buffer (100 mM, pH 5.0), 0.5 ml Carboxy Methyl Cellulase (CMC, 1.5%), and 0.25 ml of enzyme extract in total volume of 1.0 ml.…”

Section: Assay Of Cellulasementioning

confidence: 99%

Gum Ghatti Based Edible Coating Emulsion with an Additive of Clove Oil Improves the Storage Life and Maintains the Quality of Papaya (Carica papaya L., cv. Madhu bindu)

Joshi¹,

Baraiya²,

Vyas³

et al. 2017

Int.J.Curr.Microbiol.App.Sci

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“…ExoPG attacks HG from the nonreducing end and removes terminally (1→)-linked GalA residues. PG has been found in some fungi, bacteria, yeasts, and in several higher plants such as apple (Wu and others 1993), avocado (Wakabayashi and Huber 2001), banana (Pathak and Sanwal 1998), cucumber (Pressey and Avants 1975;MacFeeters and others 1980), Jamaica cherry (Gayathri and others 2007), mango (Chaimanee 1992;Ketsa and others 1998;Prasanna and others 2006;Singh and Dwivedi 2008), papaya (Chan and Tam 1982), pear (Pressey and Avants 1976), peach (Pressey and others 1971a), strawberry (Nogata and others 1993), and tomato (Pressey and Avants 1971b;Ali and Brady 1982;Moshrefi and Luh 1984;Pressey 1987). Most of the PGs found in higher plants are endo-acting enzymes.…”

Section: Polygalacturonase (Pg)mentioning

confidence: 99%

Pectins in Processed Fruit and Vegetables: Part I—Stability and Catalytic Activity of Pectinases

Duvetter¹,

Sila²,

Buggenhout³

et al. 2009

Comp Rev Food Sci Food Safe

113

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Pectinases catalyze numerous pectin conversion reactions strongly impacting on the quality of fruits, vegetables, and the related intermediate and end products. The effect of processing on the stability and catalytic activity of pectinases is of prime importance to food processors since desirable and/or deleterious reactions can be tailored (accelerated or inhibited) meeting specific quality targets. Of the multiple endogenous enzymes involved in the modification and degradation of pectin, pectinmethylesterase (PME), and polygalacturonase (PG) have been widely investigated in the context of fruit and vegetable processing. This review covers the stability and catalytic activity of endogenous plant PME and PG including the quantitative approaches applied in inactivating and/or boosting the catalytic activity of the enzymes in purified and real food systems. This will be discussed in the context of both traditional and novel food processing technologies.

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“…For instance, both banana and tomato PGs were reported to have specific activities 100-fold lower than that of FmPG (ref. 36 and references therein). We hypothesize that the big indolic side chain of the added tryptophan may constitute a considerable steric hindrance inside the active site cleft and form a favorable stacking interaction with the conserved residue Tyr-302, as shown in the model of the S270insW structure superimposed with that of the wild-type enzyme (Fig.…”

Section: Fmpg Modified With Residues Typical Of Plant-derived Pgs Is Notmentioning

confidence: 99%

Structural requirements of endo polygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)

Federici

Caprari

Mattei

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

135

129

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To invade a plant tissue, phytopathogenic fungi produce several cell wall-degrading enzymes; among them, endopolygalacturonase (PG) catalyzes the fragmentation and solubilization of homogalacturonan. Polygalacturonase-inhibiting proteins (PGIPs), found in the cell wall of many plants, counteract fungal PGs by forming specific complexes with them. We report the crystal structure at 1.73 Å resolution of PG from the phytopathogenic fungus Fusarium moniliforme (FmPG). The structure of FmPG was useful to study the mode of interaction of the enzyme with PGIP-2 from Phaseolus vulgaris. Several amino acids of FmPG were mutated, and their contribution to the formation of the complex with PGIP-2 was investigated by surface plasmon resonance. The residues Lys-269 and Arg-267, located inside the active site cleft, and His-188, at the edge of the active site cleft, are critical for the formation of the complex, which is consistent with the observed competitive inhibition of the enzyme played by PGIP-2. The replacement of His-188 with a proline or the insertion of a tryptophan after position 270, variations that both occur in plant PGs, interferes with the formation of the complex. We suggest that these variations are important structural requirements of plant PGs to prevent PGIP binding.

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Multiple forms of polygalacturonase from banana fruits

Cited by 112 publications

References 33 publications

Gum Ghatti Based Edible Coating Emulsion with an Additive of Clove Oil Improves the Storage Life and Maintains the Quality of Papaya (Carica papaya L., cv. Madhu bindu)

Gum Ghatti Based Edible Coating Emulsion with an Additive of Clove Oil Improves the Storage Life and Maintains the Quality of Papaya (Carica papaya L., cv. Madhu bindu)

Pectins in Processed Fruit and Vegetables: Part I—Stability and Catalytic Activity of Pectinases

Structural requirements of endo polygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)

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