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231223s2010 xx |||||o 00| ||eng c |
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|a 10.1016/j.jplph.2010.03.017
|2 doi
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|a pubmed24n0661.xml
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|a (DE-627)NLM198169787
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|a (NLM)20478643
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Wei, Wei
|e verfasserin
|4 aut
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| 245 |
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|a Synergism between cucumber alpha-expansin, fungal endoglucanase and pectin lyase
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|c 2010
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 04.11.2010
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright 2010 Elsevier GmbH. All rights reserved.
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|a Several recombinant fungal enzymes (endoglucanase and pectinase) were studied for their interactions with alpha-expansin in cell wall extension and polysaccharide degradation. Both Cel12A and Cel5A were able to hydrolyze cellulose CMC-Na and mixed-linkage beta-glucan. In contrast to Cel5A, Cel12A could also hydrolyze xyloglucan and induce wall extension of cucumber hypocotyls in an in vitro assay. Combining alpha-expansin, even at high concentrations, with Cel12A did not enhance the maximum/final wall extension rate induced by Cel12A alone. These results strongly suggest that modification/degradation of the xyloglucan molecule/network is the key for cell wall extension, and alpha-expansin and Cel12A may share the same acting site in the substrate. Pectinase (Pel1, a pectin lyase) enhanced alpha-expansin-induced wall extension in a concentration-dependent manner, suggesting that the pectin network may normally regulate accessibility of expansin to the xyloglucan-cellulose complex. alpha-Expansin enhanced Cel12A's hydrolytic activity on cellulose CMC-Na but not on xyloglucan and beta-glucan. Expansin did not affect Cel5A's hydrolytic activity. Interestingly, expansin also enhanced Pel1's activity on degrading high esterified pectin. A potential explanation for why expansin could synergistically interact with only certain enzymes on specific polysaccharides is discussed. Additional results also suggested that cell wall swelling may not be a significant event during the action of expansin and hydrolases
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Fungal Proteins
|2 NLM
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|a Glucans
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Polysaccharides
|2 NLM
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|a Xylans
|2 NLM
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|a expansin protein, plant
|2 NLM
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|a xyloglucan
|2 NLM
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|a 37294-28-3
|2 NLM
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|a Cellulase
|2 NLM
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|a EC 3.2.1.4
|2 NLM
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|a Polysaccharide-Lyases
|2 NLM
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|a EC 4.2.2.-
|2 NLM
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|a pectin lyase
|2 NLM
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|a EC 4.2.2.10
|2 NLM
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| 700 |
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|a Yang, Chun
|e verfasserin
|4 aut
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| 700 |
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|a Luo, Jun
|e verfasserin
|4 aut
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| 700 |
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|a Lu, Changmei
|e verfasserin
|4 aut
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|a Wu, Yajun
|e verfasserin
|4 aut
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| 700 |
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|a Yuan, Sheng
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 167(2010), 14 vom: 15. Sept., Seite 1204-10
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
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|g volume:167
|g year:2010
|g number:14
|g day:15
|g month:09
|g pages:1204-10
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|u http://dx.doi.org/10.1016/j.jplph.2010.03.017
|3 Volltext
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|d 167
|j 2010
|e 14
|b 15
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|h 1204-10
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