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Journal articles on the topic 'Oligogalacturonic Acid'

Author: Grafiati

Published: 24 June 2021

Last updated: 3 February 2022

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1

Fan, Hong-Ni, Mei-Zheng Liu, and Yuan C. Lee. "Large-scale preparation of α-D-(14)-oligogalacturonic acids from pectic acid." Canadian Journal of Chemistry 80, no. 8 (August 1, 2002): 900–903. http://dx.doi.org/10.1139/v02-055.

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An efficient and inexpensive method for large-scale preparation of α-D-(1[Formula: see text]4)-oligogalacturonic acids (oligo-GalA), up to DP 5, from pectic acid is described. Pectic acid was digested with a commercially available pectinase to yield a mixture of oligo-GalA, which was effectively separated by a combination of low-pressure size-exclusion chromatography based on ion-exchange chromatography to obtain pure oligo-GalA of DP 2-5. Key words: pectic acid, galacturonic acid, galabiose, galatriose, pectinase.

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2

Hodroge, Ahmed, Eric Trécherel, Marjorie Cornu, Walaa Darwiche, Ali Mansour, Katia Ait-Mohand, Thomas Verissimo, et al. "Oligogalacturonic Acid Inhibits Vascular Calcification by Two Mechanisms." Arteriosclerosis, Thrombosis, and Vascular Biology 37, no. 7 (July 2017): 1391–401. http://dx.doi.org/10.1161/atvbaha.117.309513.

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3

Hu, Xiangyang, Steven Neill, Weiming Cai, and Zhangcheng Tang. "Hydrogen peroxide and jasmonic acid mediate oligogalacturonic acid-induced saponin accumulation in suspension-cultured cells of Panax ginseng." Physiologia Plantarum 118, no. 3 (June 17, 2003): 414–21. http://dx.doi.org/10.1034/j.1399-3054.2003.00124.x.

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4

Lion, Jean-Marc, Romuald Mentaverri, Stéphanie Rossard, Nathalie Jullian, Bernard Courtois, Josiane Courtois, Michel Brazier, Jean-Claude Mazière, and Said Kamel. "Oligogalacturonic acid inhibit bone resorption and collagen degradation through its interaction with type I collagen." Biochemical Pharmacology 78, no. 12 (December 2009): 1448–55. http://dx.doi.org/10.1016/j.bcp.2009.07.014.

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5

Huang, Jie-Hong, Edwin J. Bakx, Harry Gruppen, and Henk A. Schols. "Characterisation of 3-aminoquinoline-derivatised isomeric oligogalacturonic acid by travelling-wave ion mobility mass spectrometry." Rapid Communications in Mass Spectrometry 27, no. 20 (September 10, 2013): 2279–85. http://dx.doi.org/10.1002/rcm.6692.

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6

Zhao, Yan, Ye Yuan, Xinyu Zhang, Yumei Li, Qiang Li, Yifa Zhou, and Juan Gao. "Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from Paenibacillus polymyxa KF-1: Cloning, Expression and Characterization." Molecules 23, no. 11 (October 26, 2018): 2774. http://dx.doi.org/10.3390/molecules23112774.

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Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of Paenibacillus polymyxa KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from P. polymyxa KF-1 genomic DNA and expressed in Escherichia coli. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and pI of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The Km, vmax and kcat values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s−1, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (Boehmeria nivea) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing.

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7

Stoll, Thomas, Andreas Schieber, and Reinhold Carle. "Quantitative determination of saturated oligogalacturonic acids in enzymatic digests of polygalacturonic acid, pectin and carrot pomace by on-line LC-ESI-MS." Analytical and Bioanalytical Chemistry 377, no. 4 (October 1, 2003): 655–59. http://dx.doi.org/10.1007/s00216-003-2138-0.

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8

Nakahara, Yoshiaki, and Tomoya Ogawa. "A highly stereocontrolled synthesis of the propyl glycoside of a decagalacturonic acid, a model compound for the endogenous phytoalexin elicitor-active oligogalacturonic acids." Carbohydrate Research 194 (December 1989): 95–114. http://dx.doi.org/10.1016/0008-6215(89)85010-4.

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9

HU, Xiang Yang, Steven J. NEILL, Wei Ming CAI, and Zhang Cheng TANG. "Induction of defence gene expression by oligogalacturonic acid requires increases in both cytosolic calcium and hydrogen peroxide in Arabidopsis thaliana." Cell Research 14, no. 3 (June 2004): 234–40. http://dx.doi.org/10.1038/sj.cr.7290224.

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10

Zhang, Ying, Chengjian Wang, Yang Liu, Weinan Yao, Yujiao Sun, Ping Zhang, Linjuan Huang, and Zhongfu Wang. "Fluorescein-5-thiosemicarbazide (FTSC) labeling for fluorescent imaging of pectin-derived oligogalacturonic acid transported in living cells by confocal microscopy." European Food Research and Technology 239, no. 5 (July 10, 2014): 867–75. http://dx.doi.org/10.1007/s00217-014-2283-z.

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11

Hu, Xiangyang, Steven J. Neill, Weiming Cai, and Zhangcheng Tang. "Nitric oxide mediates elicitor-induced saponin synthesis in cell cultures of Panax ginseng." Functional Plant Biology 30, no. 8 (2003): 901. http://dx.doi.org/10.1071/fp03061.

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The elicitor oligogalacturonic acid (OGA) stimulated nitric oxide (NO) accumulation in the growth medium of ginseng suspension cultures and induced increased nitric oxide synthase (NOS) activity in ginseng cells. OGA also stimulated accumulation of saponin, transcription of genes encoding squalene synthase (sqs) and squalene epoxidase (sqe), two early enzymes of saponin synthesis, and the accumulation of β-amyrin synthase protein (β-AS). Saponin accumulation, sqs and sqe gene expression, and increases in β-AS content were also induced by exposure to NO via the NO donor sodium nitroprusside (SNP). Inhibitors of mammalian nitric oxide synthase reduced both OGA-induced NO accumulation and NOS activity, suggesting that OGA-induced NO production occurs via a NOS-like enzyme. OGA-induced accumulation of β-AS and saponin, and transcription of sqs and sqe, were suppressed by treatments that removed NO or inhibited its production, indicating a role for NO in mediating OGA effects on these defence responses. NO accumulation and increased NOS activity were inhibited by calcium channel inhibitors and a protein kinase inhibitor, but not by a protein phosphatase inhibitor, indicating the requirement for calcium and protein phosphorylation during OGA-induced NO production. Saponin production and transcription, and accumulation of saponin biosynthetic genes and enzymes were also suppressed by these treatments, as well as by the protein phosphatase inhibitor okadaic acid.

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12

Kajsheva, N. Sh, and A. Sh Kajshev. "DEVELOPMENT OF MEDICAL PRODUCTS ON THE BASIS OF OLIGOGALACTURONIC ACID, AS CARRIERS OF BIOGENIC METALS (II) AND HEAVY METAL (II) ANTIDOTES." Trace Elements in Medicine (Moscow) 17, no. 3 (2016): 41–47. http://dx.doi.org/10.19112/2413-6174-2016-17-3-41-47.

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13

Lee, Sumin, Hyunjung Choi, SuJeoung Suh, In-Suk Doo, Ki-Young Oh, Eun Jeong Choi, Ann T. Schroeder Taylor, Philip S. Low, and Youngsook Lee. "Oligogalacturonic Acid and Chitosan Reduce Stomatal Aperture by Inducing the Evolution of Reactive Oxygen Species from Guard Cells of Tomato and Commelina communis." Plant Physiology 121, no. 1 (September 1, 1999): 147–52. http://dx.doi.org/10.1104/pp.121.1.147.

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14

Dongowski, Gerhard, Angelika Lorenz, and Horst Anger. "Degradation of Pectins with Different Degrees of Esterification by Bacteroides thetaiotaomicron Isolated from Human Gut Flora." Applied and Environmental Microbiology 66, no. 4 (April 1, 2000): 1321–27. http://dx.doi.org/10.1128/aem.66.4.1321-1327.2000.

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ABSTRACT A complete human fecal flora and cultures of defined species obtained from fecal flora were investigated in vitro to determine their ability to ferment the dietary fiber pectin. Bacteroides thetaiotaomicron was tested as a pectin-degrading microorganism alone and in coculture with Escherichia coli. Macromolecular pectins with different degrees of esterification were used as substrates in microbial degradation studies. The levels of oligogalacturonic acids formed in batch cultures were estimated during a 24- or 48-h incubation period by using high-performance thin-layer chromatography and high-performance anion-exchange chromatography. The spectrum and the amount of unsaturated oligogalacturonic acids formed as intermediate products of pectin fermentation changed permanently in the culture media during incubation with the complete fecal flora. After 24 h, no oligogalacturonic acids were detected. The pectin-degrading activities of pure cultures of B. thetaiotaomicron were lower than the pectin-degrading activity of a complete fecal flora. Cocultures of B. thetaiotaomicronand E. coli exhibited intermediate levels of degradation activity. In pure cultures of E. coli no pectin-degrading activity was found. Additionally, the rate of pectin degradation was affected by the degree of esterification of the substrate. Saturated oligogalacturonic acids were not found during pectin fermentation. The disappearance of oligogalacturonic acids in the later stages of fermentation with both the complete fecal flora and B. thetaiotaomicron was accompanied by increased formation of short-chain fatty acids.

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15

Doner, Landis W., Peter L. Irwin, and Michael J. Kurantz. "Preparative chromatography of oligogalacturonic acids." Journal of Chromatography A 449 (January 1988): 229–39. http://dx.doi.org/10.1016/s0021-9673(00)94382-6.

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16

Nikolic, Milos, and Ljiljana Mojovic. "Characterization and degradation of pectin derived from Budimka apple." Journal of the Serbian Chemical Society 73, no. 2 (2008): 157–67. http://dx.doi.org/10.2298/jsc0802157n.

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The characterization of apple pectin and its oligogalacturonic fractions derived from the autochthones apple variety Budimka, characteristic for central Serbia, is described in this paper. After extraction, the apple pectin was subjected to controlled enzymatic hydrolysis by polygalacturonase (PG) and pectin lyase (PL) from Aspergillus niger and then fractionated by ion-exchange column chromatography on Dowex 1X-8 (200-400 mesh). Saturated oligo?galacturonic acids, obtained by controlled hydrolysis with PG, were efficiently separated by elution with a gradient of Na acetate buffer (pH 6.0), while unsaturated oligogalacturonic acids, obtained by controlled hydrolysis with PL, were separated on the same resin, using a gradient of Na formate buffer (pH 4.7) as the eluent. The yields of the fractions with the particular degree of polymerization (DP) were also determined. The total content of neutral saccharides in the original Budimka apple pectin was detected by HPLC analysis of the 4-nitrobenzoyl derivatives of the sugar, and amounted to 5.31%. Among the neutral saccharides, contents of galactose, glucose, rhamnose, arabinose, xylose and mannose were detected.

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17

Doner, Landis W., Peter L. Irwin, and Michael J. Kurantz. "High-performance thin-layer chromatographic resolution of oligogalacturonic acids." Carbohydrate Research 172, no. 2 (February 1988): 292–96. http://dx.doi.org/10.1016/s0008-6215(00)90863-2.

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18

Versari, A. "HPAEC–PAD analysis of oligogalacturonic acids in strawberry juice." Food Chemistry 66, no. 2 (August 1999): 257–61. http://dx.doi.org/10.1016/s0308-8146(98)00264-7.

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19

Aoki, Takayoshi, Yuko Hiidome, Yasushi Sugimoto, Hisham R. Ibrahim, and Yasuko Kato. "Modification of ovalbumin with oligogalacturonic acids through the Maillard reaction." Food Research International 34, no. 2-3 (2001): 127–32. http://dx.doi.org/10.1016/s0963-9969(00)00140-x.

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20

Hotchkiss, Arland T., Kevin B. Hicks, Landis W. Doner, and Peter L. Irwin. "Isolation of oligogalacturonic acids in gram quantities by preparative h.p.l.c." Carbohydrate Research 215, no. 1 (August 1991): 81–90. http://dx.doi.org/10.1016/0008-6215(91)84009-4.

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21

Cook, B. J., R. P. Clay, C. W. Bergmann, P. Albersheim, and A. G. Darvill. "Fungal Polygalacturonases Exhibit Different Substrate Degradation Patterns and Differ in Their Susceptibilities to Polygalacturonase-Inhibiting Proteins." Molecular Plant-Microbe Interactions® 12, no. 8 (August 1999): 703–11. http://dx.doi.org/10.1094/mpmi.1999.12.8.703.

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Polygalacturonic acid (PGA) was hydrolyzed by polygalacturonases (PGs) purified from six fungi. The oligogalacturonide products were analyzed by HPAEC-PAD (high performance anion exchange chromatography-pulsed amperimetric detection) to assess their relative amounts and degrees of polymerization. The abilities of the fungal PGs to reduce the viscosity of a solution of PGA were also determined. The potential abilities of four polygalacturonase-inhibiting proteins (PGIPs) from three plant species to inhibit or to modify the hydrolytic activity of the fungal PGs were determined by colorimetric and HPAEC-PAD analyses, respectively. Normalized activities of the different PGs acting upon the same substrate resulted in one of two distinct oligogalacturonide profiles. Viscometric analysis of the effect of PGs on the same substrate also supports two distinct patterns of cleavage. A wide range of susceptibility of the various PGs to inhibition by PGIPs was observed. The four PGs that were inhibited by all PGIPs tested exhibited an endo/exo mode of substrate cleavage, while the three PGs that were resistant to inhibition by one or more of the PGIPs proceed by a classic endo pattern of cleavage.

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22

Lieker, Heinz-Peter, Klaus Thielecke, Klaus Buchholz, and Peter J. Reilly. "High-performance anion-exchange chromatography of saturated and unsaturated oligogalacturonic acids." Carbohydrate Research 238 (January 1993): 307–11. http://dx.doi.org/10.1016/0008-6215(93)87021-j.

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23

Xie, Mei, Denis Giraud, Patrick Arpino, Yves Bertheau, and Bruno Casetta. "Analysis of linear oligogalacturonic acids by negative-ion electrospray ionization mass spectrometry." Rapid Communications in Mass Spectrometry 9, no. 15 (1995): 1572–75. http://dx.doi.org/10.1002/rcm.1290091521.

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24

Dongowski, Gerhard. "Determination of saturated and unsaturated oligogalacturonic acids by means of thin-later chromatography." Journal of Chromatography A 756, no. 1-2 (December 1996): 211–17. http://dx.doi.org/10.1016/s0021-9673(96)00637-1.

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25

Zhu, Liang, and Hian Kee Lee. "Preliminary study of the analysis of oligogalacturonic acids by electrospray ionization mass spectrometry." Rapid Communications in Mass Spectrometry 15, no. 12 (2001): 975–78. http://dx.doi.org/10.1002/rcm.326.

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26

Hosseini-Abari, Afrouzossadat, Giti Emtiazi, Mahboubeh Jazini, Joonwon Kim, and Byung Gee Kim. "LC/MS detection of oligogalacturonic acids obtained from tragacanth degradation by pectinase producing bacteria." Journal of Basic Microbiology 59, no. 3 (December 13, 2018): 249–55. http://dx.doi.org/10.1002/jobm.201800332.

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27

WILLIAMS, Martin A. K., and Jacques A. E. BENEN. "A novel enzyme activity involving the demethylation of specific partially methylated oligogalacturonides." Biochemical Journal 367, no. 2 (October 15, 2002): 511–15. http://dx.doi.org/10.1042/bj20020796.

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Studies of the enzymic digestion of pectic substrates using different polygalacturonase (PG) preparations have revealed evidence for a previously unreported enzyme activity carried out by a contaminating enzyme in one of the preparations. This observed activity involves the demethylation of specific oligogalacturonides, namely 2-methyltrigalacturonic acid and 2,3-dimethyltetragalacturonic acid. However, no large-scale demethylation of highly methylated polymeric substrates is found, demonstrating that the enzyme responsible is not a conventional pectin methylesterase (PME). Furthermore, it has been shown that a commercial sample of fungal PME from Aspergillus niger demethylates all of the oligogalacturonides present as primary products of endo-PG digestion, in contrast with the activity observed here. On the basis of the known methyl ester distribution of the endo-PG-generated fragments and knowledge of which of these oligogalacturonides are demethylated, it is concluded that the observed activity can be explained by the existence of an exo-acting methylesterase that attacks the non-reducing end of the oligogalacturonide molecules.

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28

Dongowski, Gerhard, and Angelika Lorenz. "Unsaturated oligogalacturonic acids are generated by in vitro treatment of pectin with human faecal flora." Carbohydrate Research 314, no. 3-4 (December 1998): 237–44. http://dx.doi.org/10.1016/s0008-6215(98)00304-8.

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29

Simms, Peter J., Arland T. Hotchkiss, Peter L. Irwin, and Kevin B. Hicks. "High-performance liquid chromatographic separation of oligogalacturonic acids on a cyclomaltoheptaose (β-cyclodextrin) bonded-phase column." Carbohydrate Research 278, no. 1 (November 1995): 1–9. http://dx.doi.org/10.1016/0008-6215(95)00228-x.

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30

Suzuki, T., K. Tomita-Yokotani, S. Yoshida, Y. Takase, I. Kusakabe, and K. Hasegawa. "Preparation and Isolation of Oligogalacturonic Acids and Their Biological Effects in Cockscomb (Celosia argentea L.) Seedlings." Journal of Plant Growth Regulation 21, no. 3 (September 2002): 209–15. http://dx.doi.org/10.1007/s003440010060.

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31

Naohara, J., and M. Manabe. "Separation of oligogalacturonic acids by high-performance gel filtration chromatography on silica gel with diol radical." Journal of Chromatography A 603, no. 1-2 (June 1992): 139–43. http://dx.doi.org/10.1016/0021-9673(92)85354-v.

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32

Stoll, Thomas, Andreas Schieber, and Reinhold Carle. "High-performance liquid chromatographic separation and on-line mass spectrometric detection of saturated and unsaturated oligogalacturonic acids." Carbohydrate Research 337, no. 24 (November 2002): 2481–86. http://dx.doi.org/10.1016/s0008-6215(02)00348-8.

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33

Hotchkiss, Arland T., and Kevin B. Hicks. "Analysis of pectate lyase-generated oligogalacturonic acids by high-performance anion-exchange chromatography with pulsed amperometric detection." Carbohydrate Research 247 (September 1993): 1–7. http://dx.doi.org/10.1016/0008-6215(93)84236-y.

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34

Cano, María Emilia, Alberto García-Martín, Miguel Ladero, David Lesur, Serge Pilard, and José Kovensky. "A simple procedure to obtain a medium-size oligogalacturonic acids fraction from orange peel and apple pomace wastes." Food Chemistry 346 (June 2021): 128909. http://dx.doi.org/10.1016/j.foodchem.2020.128909.

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35

Hotchkiss, Arland T., Stephanie L. Lecrinier, and Kevin B. Hicks. "Isolation of oligogalacturonic acids up to DP 20 by preparative high-performance anion-exchange chromatography and pulsed amperometric detection." Carbohydrate Research 334, no. 2 (August 2001): 135–40. http://dx.doi.org/10.1016/s0008-6215(01)00170-7.

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36

Xu, Yuxia, Qun Dong, Hong Qiu, Chung-Wah Ma, and Kan Ding. "A homogalacturonan from the radix of Platycodon grandiflorum and the anti-angiogenesis activity of poly-/oligogalacturonic acids derived therefrom." Carbohydrate Research 346, no. 13 (September 2011): 1930–36. http://dx.doi.org/10.1016/j.carres.2011.05.011.

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37

Hotchkiss, Arland T., and Kevin B. Hicks. "Analysis of oligogalacturonic acids with 50 or fewer residues by high-performance anion-exchange chromatography and pulsed amperometric detection." Analytical Biochemistry 184, no. 2 (February 1990): 200–206. http://dx.doi.org/10.1016/0003-2697(90)90669-z.

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38

Zhu, Ru-Gang, Yan-Di Sun, Yu-Ting Hou, Jun-Gang Fan, Gang Chen, and Tuo-Ping Li. "Pectin penta-oligogalacturonide reduces cholesterol accumulation by promoting bile acid biosynthesis and excretion in high-cholesterol-fed mice." Chemico-Biological Interactions 272 (June 2017): 153–59. http://dx.doi.org/10.1016/j.cbi.2017.05.018.

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39

Deconinck, Thomas J. M., Antoine Ciza, Georges M. Sinnaeve, Jean T. Laloux, and Philippe Thonart. "High-performance anion-exchange chromatography — DAD as a tool for the identification and quantification of oligogalacturonic acids in pectin depolymerisation." Carbohydrate Research 329, no. 4 (December 2000): 907–11. http://dx.doi.org/10.1016/s0008-6215(00)00253-6.

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40

Mata, Georgina Hernández, Baldemar Sepúlveda, Alan Richards, and Eva Soriano. "The architecture of Phaseolus vulgaris root is altered when a defense response is elicited by an oligogalacturonide." Brazilian Journal of Plant Physiology 18, no. 2 (June 2006): 351–55. http://dx.doi.org/10.1590/s1677-04202006000200012.

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Phytoalexin accumulation is one of a myriad of plant defense responses; these responses can be elicited by pathogens or molecules such as oligogalacturonides (OGAs). Phytoalexin production has been considered a vital component of the resistance mechanisms that determine the outcome of many plant-microbe interactions. Besides inducing defense responses, OGAs have been shown to affect plant development, which normally is controlled by plant hormones, particularly auxin. In this work we measured phytoalexin accumulation in roots of bean (Phaseolus vulgaris L.) seedlings grown in the presence or absence of the auxin 3-naphtalenacetic acid (NAA) and treated with a decagalacturonide (OGA10). We found that OGA10 (0.01 mM) caused phytoalexin production and also inhibited main root elongation and the formation of secondary roots by ca. 33%. Expression of Cycb 2-2 was also inhibited, while pal and chs were highly expressed. The root growth inhibition was not overcome by the addition of a stimulatory concentration of auxin (NAA 0.1 µM). The data suggests that elicitation of defense responses in the root alters metabolism in such a way that results in the modification of the architecture of bean roots.

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41

Riou, Chantal, Christine Hervé, Valérie Pacquit, Patrick Dabos, and Bernard Lescure. "Expression of an Arabidopsis lectin kinase receptor gene, lecRK-a1, is induced during senescence, wounding and in response to oligogalacturonic acids." Plant Physiology and Biochemistry 40, no. 5 (May 2002): 431–38. http://dx.doi.org/10.1016/s0981-9428(02)01390-6.

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42

Zhu, Rugang, Yuting Hou, Yandi Sun, Tuoping Li, Jungang Fan, Gang Chen, and Junxiu Wei. "Pectin Penta-Oligogalacturonide Suppresses Intestinal Bile Acids Absorption and Downregulates the FXR-FGF15 Axis in High-Cholesterol Fed Mice." Lipids 52, no. 6 (May 4, 2017): 489–98. http://dx.doi.org/10.1007/s11745-017-4258-x.

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43

Norman, Cecilia, Sabina Vidal, and E. Tapio Palva. "Oligogalacturonide-Mediated Induction of a Gene Involved in Jasmonic Acid Synthesis in Response to the Cell-Wall-Degrading Enzymes of the Plant Pathogen Erwinia carotovora." Molecular Plant-Microbe Interactions® 12, no. 7 (July 1999): 640–44. http://dx.doi.org/10.1094/mpmi.1999.12.7.640.

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Identification of Arabidopsis thaliana genes responsive to plant cell-wall-degrading enzymes of Erwinia carotovora subsp. carotovora led to the isolation of a cDNA clone with high sequence homology to the gene for allene oxide synthase, an enzyme involved in the biosynthesis of jasmonates. Expression of the corresponding gene was induced by the extracellular enzymes from this pathogen as well as by treatment with methyl jasmonate and short oligogalacturonides (OGAs). This suggests that OGAs are involved in the induction of the jasmonate pathway during plant defense response to E. carotovora subsp. carotovora attack.

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44

Nakahara, Yoshiaki, and Tomoya Ogawa. "Stereocontrolled, total synthesis of α-d-GalA-[1→4)-α-d-GalA]8-(1→4)-β-d-GalA-1→OPr, a synthetic model for phytoalexin elicitor-active oligogalacturonic acids." Carbohydrate Research 167 (September 1987): C1—C7. http://dx.doi.org/10.1016/0008-6215(87)80292-6.

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45

Wan, Jiangxue, Min He, Qingqing Hou, Lijuan Zou, Yihua Yang, Yan Wei, and Xuewei Chen. "Cell wall associated immunity in plants." Stress Biology 1, no. 1 (August 18, 2021). http://dx.doi.org/10.1007/s44154-021-00003-4.

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AbstractThe plant cell wall is the first physical and defensive barrier against pathogens. The plant cell wall usually undergoes dynamic remodeling as an immune response to prevent infection by pathogens. In this review, we summarize advances on relationship between cell wall and immunity in plants. In particular, we outline current progresses regarding the regulation of the cell wall components, including cellulose, hemicellulose, pectin and lignin, on plant disease resistance. We also discuss the impacts of cell wall-derived cellodextrin, oligogalacturonic acid and xyloglucan/xylan oligosaccharides as potent elicitors or signal molecules to trigger plant immune response. We further propose future studies on dissecting the molecular regulation of cell wall on plant immunity, which have potentials in practical application of crop breeding aiming at improvement of plant disease resistance.

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Ma, Yingxuan, Leilei Zhou, Zhichao Wang, Jianting Chen, and Guiqin Qu. "Oligogalacturonic acids promote tomato fruit ripening through the regulation of 1-aminocyclopropane-1-carboxylic acid synthesis at the transcriptional and post-translational levels." BMC Plant Biology 16, no. 1 (January 9, 2016). http://dx.doi.org/10.1186/s12870-015-0634-y.

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Keggi, Christian, and Joy Doran-Peterson. "The Homogalacturonan Deconstruction System of Paenibacillus amylolyticus 27C64 Requires No Extracellular Pectin Methylesterase and Has Significant Industrial Potential." Applied and Environmental Microbiology 86, no. 12 (April 17, 2020). http://dx.doi.org/10.1128/aem.02275-19.

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Abstract:

ABSTRACT Paenibacillus amylolyticus 27C64, a Gram-positive bacterium with diverse plant cell wall polysaccharide deconstruction capabilities, was isolated previously from an insect hindgut. Previous work suggested that this organism’s pectin deconstruction system differs from known systems in that its sole pectin methylesterase is cytoplasmic, not extracellular. In this work, we have characterized the specific roles of key extracellular pectinases involved in homogalacturonan deconstruction, including four pectate lyases and one pectin lyase. We show that one newly characterized pectate lyase, PelC, has a novel substrate specificity, with a lower Km for highly methylated pectins than for polygalacturonic acid. PelC works synergistically with PelB, a high-turnover exo-pectate lyase that releases Δ4,5-unsaturated trigalacturonate as its major product. It is likely that PelC frees internal stretches of demethylated homogalacturonan which PelB can degrade. We also show that the sole pectin lyase has a high kcat value and rapidly depolymerizes methylated substrates. Three cytoplasmic GH105 hydrolases were screened for the ability to remove terminal unsaturated galacturonic acid residues from oligogalacturonide products produced by the action of extracellular lyases, and we found that two are active on demethylated oligogalacturonides. This work confirms that efficient homogalacturonan deconstruction in P. amylolyticus 27C65 does not require extracellular pectin methylesterase activity. Three of the extracellular lyases studied in this work are also thermostable, function well over a broad pH range, and have significant industrial potential. IMPORTANCE Pectin is an important structural polysaccharide found in most plant cell walls. In the environment, pectin degradation is part of the decomposition process that turns over dead plant material and is important to organisms that feed on plants. Industrially, pectinases are used to improve the quality of fruit juices and can also be used to process coffee cherries or tea leaves. These enzymes may also prove useful in reducing the environmental impact of paper and cotton manufacturing. This work is significant because it focuses on a Gram-positive bacterium that is evolutionarily distinct from other well-studied pectin-degrading organisms and differs from known systems in key ways. Most importantly, a simplified extracellular deconstruction process in this organism is able to break down pectins without first removing the methyl groups that inhibit other systems. Moreover, some of the enzymes described here have the potential to improve industrial processes that rely on pectin deconstruction.

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