Hairy plant polysaccharides: a close shave with microbial esterases

Williamson, Gary; Kroon, Paul A.; Faulds, Craig B.

doi:10.1099/00221287-144-8-2011

Cited by 199 publications

(106 citation statements)

References 84 publications

(117 reference statements)

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“…Efficient breakdown of plant cell wall material by microorganisms requires not only glycosidase activities that cleave polysaccharide chains, but also activities that remove groups that are connected by ester linkages to polysaccharides (Christov & Prior, 1993 ;Williamson et al, 1998). Xylans are often heavily substituted with acetyl groups and can also be connected to phenolic acids, and hence to lignin, via ester linkages involving arabinose substituents (Iiyama et al, 1994), while pectins carry esterified methyl and acetyl groups The GenBank accession numbers for the sequences reported in this paper are AJ238716 (cesA) and AJ272430 (xynE).…”

Section: Introductionmentioning

confidence: 99%

Three multidomain esterases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that carry divergent dockerin sequences The GenBank accession numbers for the sequences reported in this paper are AJ238716 (cesA) and AJ272430 (xynE).

Aurilia¹,

Martin²,

McCrae³

et al. 2000

Microbiology

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Three enzymes carrying esterase domains have been identified in the rumen cellulolytic anaerobe Ruminococcus flavefaciens 17. The newly characterized CesA gene product (768 amino acids) includes an N-terminal acetylesterase domain and an unidentified C-terminal domain, while the previously characterized XynB enzyme (781 amino acids) includes an internal acetylesterase domain in addition to its N-terminal xylanase catalytic domain. A third gene, xynE, is predicted to encode a multidomain enzyme of 792 amino acids including a family 11 xylanase domain and a C-terminal esterase domain. The esterase domains from CesA and XynB share significant sequence identity (44 %) and belong to carbohydrate esterase family 3 ; both domains are shown here to be capable of deacetylating acetylated xylans, but no evidence was found for ferulic acid esterase activity. The esterase domain of XynE, however, shares 42 % amino acid identity with a family 1 phenolic acid esterase domain identified from Clostridum thermocellum XynZ. XynB, XynE and CesA all contain dockerin-like regions in addition to their catalytic domains, suggesting that these enzymes form part of a cellulosome-like multienzyme complex. The dockerin sequences of CesA and XynE differ significantly from those previously described in R. flavefaciens polysaccharidases, including XynB, suggesting that they might represent distinct dockerin specificities.

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Section: Introductionmentioning

confidence: 99%

Three multidomain esterases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that carry divergent dockerin sequences The GenBank accession numbers for the sequences reported in this paper are AJ238716 (cesA) and AJ272430 (xynE).

Aurilia¹,

Martin²,

McCrae³

et al. 2000

Microbiology

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“…15) Moreover, ferulic acid has several potential applications: it may be useful as an anti oxidizing agent, 16,17) an anti inflammatory drug, 18,19) and a food preservative that inhibits microbial growth. 20,21) Enzymatic extraction of ferulic acid from industrial wastes has been studied. Penicillium funiculosum FAEB releases 98% of esterified ferulic acid from wheat bran in the presence of xylanase and releases 35% of esterified ferulic acid from sugar beet pulp in the presence of a mixture of endo arabinanase and L arabinofuranosidase.…”

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confidence: 99%

Efficient Extraction of Ferulic Acid from Sugar Beet Pulp Using the Culture Supernatant of Penicillium chrysogenum

et al. 2005

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Ferulic acids have been found in the cell walls of many plant products including maize bran, 1) sugar cane bagasse,2) wheat bran, 3) sugar beet pulp, 4,5) and spinach. 6) In the three former tissues, ferulic acid is esterified to the C 5 of arabinose in arabinoxylan, a 1,4 D xylan to which L arabinofuranosyl residues are attached at position 2 or 3. In contrast, ferulic acids mainly attach to the C 2 position of 1,5 linked arabinofuranose residues or the C 6 of 1,4 linked galactopyranose residues in the hairy region of pectins of sugar beet and spinach. 7,8) Recently, Levigne et al. demonstrated that ferulic acid is also linked to the C 5 position of arabinofuranose residues in sugar beet pectin by analysis of the structures of feruloylated oligosaccharides obtained by treating sugar beets with a commercial enzyme preparation (Driselase). 9) Furthermore, some ferulic acids exist as dehydrodimers (e.g. 5 5 dehydrodiferulic acid) in the cell walls of several plant species, which are formed through an oxidation reaction catalyzed by peroxidases.10,11) Possible roles of ferulic acid in plant cell walls are to decrease the digestibility of the cell wall by microorganisms 12) and to regulate cell growth 13) by cross linking cell wall polysaccharides.Ferulic acid esterases (FAEs) are enzymes that catalyze the hydrolysis of ester linkages between ferulic acids and sugars or alcohols. The number of studies concerning microbial FAEs has been increasing in the last ten years and many FAEs have been isolated and characterized. In the utilization of agro industrial wastes such as sugar beet pulp, effective degradation of plant cell walls requires FAEs for the release of ferulic acid as well as polysaccharidases such as xylanases 14) and arabinanases. 15) Moreover, ferulic acid has several potential applications: it may be useful as an anti oxidizing agent, 16,17) an anti inflammatory drug, 18,19) and a food preservative that inhibits microbial growth. 20,21) Enzymatic extraction of ferulic acid from industrial wastes has been studied. Penicillium funiculosum FAEB releases 98% of esterified ferulic acid from wheat bran in the presence of xylanase and releases 35% of esterified ferulic acid from sugar beet pulp in the presence of a mixture of endo arabinanase and L arabinofuranosidase. 22) To the best of our knowledge, that releases more ferulic acid from sugar beet pulp than any other enzyme.In this paper we describe the screening of microorganisms that can achieve high yield extraction of free ferulic acid from sugar beet pulp. In addition, we describe the isolation and some of the characteristics of a novel FAE, termed FAE 1, produced by P. chrysogenum 31B. MATERIALS AND METHODS Chemicals and reagents.ResourceQ 6 mL, ResourceS 6 mL, MonoQ HR 5 5, MonoS HR 5 5 and HiLoad 16 60 Superdex 75 columns were purchased from Amersham Biosciences. All other chemicals were from Wako Pure Chemical Industries, Ltd. (Osaka) unless otherwise stated, and were of certified reagent grade.Organism and cultivation conditions. The microorganisms...

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“…Recent research shows that cleavage of esterified linkages by purified cinnamoyl esterases such as ferulic acid esterase within the plant cell wall matrix may be the key to improving digestion of complex plant cell wall materials (Williamson et al 1998a, b;Wang and McAllister 2002) Ferulic Acid in Plant Cell Walls and the Association between Ferulic Aicd and Lignin/ Polysaccharides In complex plant cell walls, ferulic acid is ubiquitous (Brézillon et al 1996), and is particularly high in the cell walls of cereal grains Brézillon et al 1996;Bartolomé et al 1997a, b). The levels of ferulic acid in the cell walls of several plants are as follows: barley hull 1.4 µg mg -1 (Tenkanen et al 1991), oat hulls 2.2 to 3.8 µg mg -1 (Garleb et al 1988(Garleb et al , 1991Yu et al 2002a, b), barley spent grain 3.2 µg mg -1 (Bartolomé et al 1997a(Bartolomé et al , 1997b(Bartolomé et al and 1999, wheat bran (de-starched) 5.0 to 7.3 µg mg -1 (Bartolomé et al 1995;Faulds and Williamson 1995), maize bran 32 µg mg -1 (de-starched and de-proteined) ) and sugar beet pulp 8.7 µg mg -1 .…”

Section: Complex Plant Cell Wallsmentioning

confidence: 99%

“…Ferulic acid esterase has been found to break the ester linkage between ferulic acid and the attached sugar, and so liberate ferulic acid from chemical model compounds -isolated feruloylated oligosaccharides Faulds et al 1995a, b;Williamson et al 1998a;Sancho et al 1999;Ferreira et al 1999) and from complex plant cell walls such as coastal bermudagrass ), wheat bran (Mackenzie and Bilous 1988;Williamson 1993, 1995;Relat et al 1994;Bartolomé et al 1995Bartolomé et al , 1997aFaulds et al 1995a;Kroon et al 1999), maize bran (Faulds et al 1995b), barley spent grain (Moore et al 1996;Bartolomé et al 1997a, b;Bartolomé and Gómez-Cordovés 1999;Sancho et al 1999), sugar beet pulp (Brézillon et al 1996;Ferreira et al 1999) and oat hulls (Yu et al 2000;2002a, b). Certain ferulic acid esterases have also been reported to be able to release ferulate dimers (Bartolomé et al 1997a), which play an important structural role in strengthening and cross-linking primary plant cell walls (Ishii 1997;Iiyama and Lam 2001).…”

Section: Function Of Ferulic Acid Esterasementioning

confidence: 99%

Hydroxycinnamic acids and ferulic acid esterase in relation to biodegradation of complex plant cell walls

Yu¹,

McKinnon²,

Christensen³

2005

Can. J. Anim. Sci.

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. 2005. Hydroxycinnamic acids and ferulic acid esterase in relation to biodegradation of complex plant cell walls. Can. J. Anim. Sci. 85: 255-267. Ferulic acid (3-methoxy-4-hydroxycinnamic acid), present in complex plant cell walls, is covalently cross-linked to polysaccharides by ester bonds and to components of lignin mainly by ether bonds. Ferulic acid has also been shown to occur in dimer-and trimerized forms through oxidative coupling between esterified and/or etherified ferulic acid residues. These cross-links are among the factors most inhibitory to digestion of complex plant cell walls in ruminants. Recently obtained information on ferulic acid and ferulic acid esterases in relation to complex plant cell wall biodegradation is reviewed. A focus of the review is on structural characteristics of plant cell walls associated with ferulic acid, physicochemical properties of ferulic acid esterase and synergistic interaction between ferulic acid esterase and other accessary cell wall degrading enzymes on the release of ferulic acid and plant cell wall biodegradation. L'acide férulique (acide 3-méthoxy-4-hydroxycinnamique) présent dans la paroi cellulosique des plantes évoluées, se lie par covalence aux polysaccharides grâce à des ponts ester ainsi qu'aux composantes de la lignine principalement grâce à des ponts éther. On sait aussi que l'acide férulique se rencontre sous la forme de dimères et de trimères consécutivement à un couplage oxydatif entre ses résidus estérifiés ou éthérifiés. Ces liens croisés figurent parmi les facteurs qui entravent le plus la digestion de la paroi cellulosique des plantes complexes par les ruminants. Les auteurs passent en revue des données récentes sur l'acide férulique et ses estérases, et sur la digestion de la paroi cellulosique des plantes évoluées. Ils insistent en particulier sur les caractéristiques structurales de la paroi cellulosique associées à l'acide férulique, sur les propriétés physicochimiques de l'estérase de l'acide férulique et sur l'action synergique de l'estérase de l'acide férulique et des enzymes accessoires à la dégradation de la paroi cellulosique sur la libération de l'acide férulique et la digestion de la paroi cellulosique par les ruminants.

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Hairy plant polysaccharides: a close shave with microbial esterases

Cited by 199 publications

References 84 publications

Three multidomain esterases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that carry divergent dockerin sequences The GenBank accession numbers for the sequences reported in this paper are AJ238716 (cesA) and AJ272430 (xynE).

Three multidomain esterases from the cellulolytic rumen anaerobe Ruminococcus flavefaciens 17 that carry divergent dockerin sequences The GenBank accession numbers for the sequences reported in this paper are AJ238716 (cesA) and AJ272430 (xynE).

Efficient Extraction of Ferulic Acid from Sugar Beet Pulp Using the Culture Supernatant of Penicillium chrysogenum

Hydroxycinnamic acids and ferulic acid esterase in relation to biodegradation of complex plant cell walls

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