Degradation of Muskmelon Cell Wall by the Xylanases of <i>Colletotrichum lagenarium</i>

Doux‐Gayat, A.; Auriol, P.; Joseleau, J.P.; Touzé, A.

doi:10.1111/j.1399-3054.1978.tb04086.x

Cited by 9 publications

(3 citation statements)

References 27 publications

(17 reference statements)

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“…Highly and minimally branched xylans are observed that vary in structure between plant species. Unbranched xylan has been found in the tobacco pith cell wall (Eda et al 1976), muskmelon (Doux‐Gayat et al 1978) and ‘Barlett’ pear (Ahmed and Labavitch 1980).…”

Section: Introductionmentioning

confidence: 99%

Papaya fruit softening, endoxylanase gene expression, protein and activity

Manenoi

Paull

2007

Physiologia Plantarum

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Papaya (Carica papaya L.) cell wall matrix polysaccharides are modified as the fruit starts to soften during ripening and an endoxylanase is expressed that may play a role in the softening process. Endoxylanase gene expression, protein amount and activity were determined in papaya cultivars that differ in softening pattern and in one cultivar where softening was modified by the ethylene receptor inhibitor 1-methylcyclopropene (1-MCP). Antibodies to the endoxylanase catalytic domain were used to determine protein accumulation. The three papaya varieties used in the study, 'Line 8', 'Sunset', and 'Line 4-16', differed in softening pattern, respiration rate, ethylene production and showed similar parallel relationships during ripening and softening in endoxylanase expression, protein level and activity. When fruit of the three papaya varieties showed the respiratory climacteric and started to soften, the level of endoxylanase gene expression increased and this increase was related to the amount of endoxylanase protein at 32 kDa and its activity. Fruit when treated at less than 10% skin yellow stage with 1-MCP showed a significant delay in the respiratory climacteric and softening, and reduced ethylene production, and when ripe was firmer and had a 'rubbery' texture. The 1-MCP-treated fruit that had the 'rubbery' texture showed suppressed endoxylanase gene expression, protein and enzymatic activity. Little or no delay occurred between endoxylanase gene expression and the appearance of activity during posttranslational processing from 65 to 32 kDa. The close relationship between endoxylanase gene expression, protein accumulation and activity in different varieties and the failure of the 1-MCP-treated fruit to fully soften, supported de novo synthesis of endoxylanase, rapid posttranslation processing and a role in papaya fruit softening.

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Section: Introductionmentioning

confidence: 99%

Papaya fruit softening, endoxylanase gene expression, protein and activity

Manenoi

Paull

2007

Physiologia Plantarum

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“…The procedure described by Doux-Gayat et al (1978) with some modifications was used to isolate hemicelluloses from cucumber cell walls. About 0.7 g of pure celi walls was mixed with O.I M KOH for 12 h in a shaker.…”

Section: Isolation Of Hemicelluloses From Cucumher Ceii Wallsmentioning

confidence: 99%

“…In Cucumis melo. Fraction 2 is a xylan-rich fraction (Doux-Gayat et al 1978). The ability of cucumber endo-xylanase to utilize Fraction 2 poiysaccharides suggests the presence of an in vivo substrate in the cell walls of cucumber seeds.…”

Section: Activity Towards Other Substratesmentioning

confidence: 99%

Partial purification and properties of an endo-xylanase from cucumber seeds

Mujer¹,

Kretchman²,

Miller³

1991

Physiol Plant

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1991. Partial purification and properties of an endo-xylanase from cucumber seeds. -Physio!. Plant. 81: 327-334.An endo-xylanase. 1.4-^-D-xylan xylanohydrolase (EC 3.2.1.8) from immature cucumber (Cucumis sativus L. cv. Heinz 3534) seeds was partially purified using ammonium sulfate fractionation and chromatography on SP-Sephadex and Sephadex G-100 in order to determine its role in xylan metabolism during development. Attempts to further purify the enzyme using chromatography on DEAE-Sephadex, Bio-Gel HTP hydroxylapatite, Sephadex G-200 and con A-Sepharose 4B and native polyacrylamide ge! electrophoresis resulted in a significant decrease or complete loss of enzyme activity. Endo-xylanase had a native molecular weight of 96 kDa as determined by gel filtration, exhibited optimal activity ai pH 5.0 and 48°C, and was most stable from pH 4.0 to 5.0. Using beechwood 4-o-methyl-t)-glucurono-D-xylan dyed with Remazol Brilliant Blue R as substrate, the K^ was estimated to be 0.70 mg ml '. HgCI, at i mM inhibited endo-xylanase completely. Other metal ions inhibited the enzyme in the order Cu^* > Fe'* > Zn'+ > Ca-+ > Mn'*. The eihanol-soluble products of endo-xylanase action on beechwood xylan were isolated and characterized by consecutive chromatography on Bio-Gel PIO and P-2. The major reaction products were xylo-oligosaccharides [degree of polymerization (dp) > 10] but traces of xylobiose and free xylose were also isolated. The formation of xylo-oligosaccharides indicated that the reaction was catalyzed primarily by an endo-xylanase. The partially pure enzyme had no activity towards other cell wall polysaccharides such as cellulose, carboxymethyl cellulose, sodium carboxyi cellulose, potato starch, orange pectin, polygalacturonic acid, arabinogalactan and /J-giucan. However, it was able to hydrolyze larchwood and oat spelts xylan and a polysaccharide component from purified cucumber cell walls. The ability to utilize a substrate from cucumber cell walls supports the hypothesis that endo-xylanase is involved in the development of cucumber seeds.

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Pathogens of Cucurbit Crops

Dixon¹

1981

Vegetable Crop Diseases

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Degradation of Muskmelon Cell Wall by the Xylanases of Colletotrichum lagenarium

Cited by 9 publications

References 27 publications

Papaya fruit softening, endoxylanase gene expression, protein and activity

Papaya fruit softening, endoxylanase gene expression, protein and activity

Partial purification and properties of an endo-xylanase from cucumber seeds

Pathogens of Cucurbit Crops

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