The Partial Purification and Properties of Endopolygalacturonase and  -L-Arabinofuranosidase secreted by Sclerotinia fructigena

Fielding, A. H.; Byrde, R. J. W.

doi:10.1099/00221287-58-1-73

Cited by 33 publications

(8 citation statements)

References 28 publications

(19 reference statements)

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“…The molecular masses of the two A. nMulans enzymes were slightly smaller than of those from A. niger. The optimal pH of the A. nidulans a-l.-arabinofuranosidase was higher than of the A. niger a-L-arabinofuranosidase B, but in the range of other fungal a-t.arabinofuranosidases [9]. The optimal pH for the A. nidulans endo-arabinase was slightly higher than that of the A. niger enzyme.…”

Section: Purification Of the Enzymes Induced By L-arabitolmentioning

confidence: 77%

“…We are particularly interested in the arabinandegrading enzymes. This class of hemicellulases has been isolated from a number of bacteria and fungi as Bacillus subtilis [3,4], Erwinia carotovora [5], Streptomyces purpurascens [6], A. niger [7,8], Sclerotinia fructigena [9] or Sclerotinia sclerotium [10]. Recently, we have studied the induction pattern of the arabinan-degrading enzymes of A. niger [11,12].…”

Section: Introductionmentioning

confidence: 99%

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Arabinan degrading enzymes from Aspergillus nidulans: Induction and purification

Ramón¹

1993

FEMS Microbiology Letters

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The presence in Aspergillus nidulans of two enzymes related to the Aspergillus niger endo-arabinase and alpha-L-arabinofuranosidase B has been established using antibodies against the purified A. niger enzymes. Moreover, the absence of an equivalent in A. nidulans to the alpha-L-arabinofuranosidase A of A. niger has been confirmed both at the protein and at the DNA level. Both A. nidulans arabinases have been purified and physico-chemically and kinetically characterized. They have a much higher temperature optimum than the corresponding A. niger enzymes. The pattern of induction has been studied on media containing different carbon sources showing an important role of L-arabitol in the induction of these enzymes.

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Section: Purification Of the Enzymes Induced By L-arabitolmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 99%

Arabinan degrading enzymes from Aspergillus nidulans: Induction and purification

Ramón¹

1993

FEMS Microbiology Letters

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“…[3][4][5][6][7][8][9] Phaff et al 10 ) reported on endopolygalacturonase from several yeasts. They found that Saccharomyces fragilis caused the most rapid clarification of the citrus pectin medium among yeasts investigated.…”

mentioning

confidence: 99%

Multiple Forms of Endo-Polygalacturonase fromSaccharomyces fragilis

Lim¹,

Yamasaki²,

Suzuki³

et al. 1980

Agricultural and Biological Chemistry

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Three forms of endopolygalacturonase from Saccharomyces ji-agilis (Kluyveromyces fragilis) were separated by a procedure induding adsorption on Amberlite IRC-50, CM Sephadex C-50 column chromatography and repeated preparative disc electrophoresis. Each endo-PG was almost homogenoeus as judged by polyacrylamide gel electrofocusing and disc electrophoresis. The three enzyme were designated as enzymes I, II and III. Enzymes I and II were similar but enzyme III different from I and II in isoelectric point. The three enzymes resembled one another in eznyme action on pectic acid and other properties. All the three enzymes showed macerating activity toward the potato and carrot tissues. 473

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“…Eluted fractions (3 ml) were collected and the absorbance was measured at 280 nm using a Camspec M330 (UV/visible) spectrophotometer. Peak fractions were pooled, freeze-dried and PG activity was verified individually for each pooled fraction by cup plate assay as described by Dingle et al (1953) and by the viscosity method (Fielding et al, 1969). The column was pre-calibrated with marker proteins such as cytochrome C horse heart, Bovine serum albumen, and carbonic-anhydrase (Sigma) by applying 2 mg of each marker protein dissolved in 2 ml eluting buffer (Andrews, 1964).…”

Section: Determination Of Molecular Weights Of Polygalacturonasementioning

confidence: 99%

“…Polygalacturonase (PG) activity in P. meadii isolates grown in liquid culture filtrates and obtained after different time intervals was determined according to Fielding and Byrde (1969) with modifications. The PG activity was measured arbitrarily in terms of reduction of viscosity of a 1.5 % sodium polypectate solution caused by disruption of polypectate.…”

Section: Polygalacturonase Assaymentioning

confidence: 99%

Effect of rubber petiole cell walls and virulence of strains on secretion of pectic enzymes by <i>Pytophthora meadii</i>

Jayasuriya

Wijesundera

Thennakoon

2009

Ceylon J. Sci. (Biol. Sci.)

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The characteristics of the pectic enzyme polygalacturonase (PG) of Phytophthora meadii isolates from petioles of rubber (Hevea brasiliensis) genotypes were compared in relation to (i) aggressiveness (virulence) in infecting detached petioles of a susceptible rubber genotype (PB86) or (ii) in relation to the availability of purified rubber petiole cell walls (obtained from a Phytophthora-resistant clone, RRIC100) in the growth medium, as the sole carbon source. The four most highly aggressive isolates produced PG forms varying within mw 48-60 kDa, while, the highly aggressive MAD86 isolate produced two PG forms of mw 48 and 70 kDa. Moderately or weakly aggressive isolates produced PG forms within the range of 62-66 kDa. With rubber petiole cell walls in the growth medium, the four most highly aggressive isolates produced PG forms of mw 42-62 kDa, while, MAD86 produced a much smaller PG form of 21 kDa. Weak or moderately aggressive isolates produced similar PG forms in both cell wall and pectin media. Quite smaller PG molecules produced in rubber cell wall medium could be due to elicitor molecular fragments bound to rubber cell walls, which may induce P. meadii to secret specific PG forms via signal transduction pathway. None of the isolates produced pectin lyase (PL) in any growth medium. Neither PG nor PL activity was detected in P. meadii-infected petioles.

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The Partial Purification and Properties of Endopolygalacturonase and -L-Arabinofuranosidase secreted by Sclerotinia fructigena

Cited by 33 publications

References 28 publications

Arabinan degrading enzymes from Aspergillus nidulans: Induction and purification

Arabinan degrading enzymes from Aspergillus nidulans: Induction and purification

Multiple Forms of Endo-Polygalacturonase fromSaccharomyces fragilis

Effect of rubber petiole cell walls and virulence of strains on secretion of pectic enzymes by <i>Pytophthora meadii</i>

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