Rhamnogalacturonase B from Aspergillus aculeatus Is a Rhamnogalacturonan [alpha]-L-Rhamnopyranosyl-(1-&gt;4)-[alpha]-D-Galactopyranosyluronide Lyase

Mutter, M.; Colquhoun, Ian J.; Schols, Henk A.; Beldman, G.; Voragen, A.G.J.

doi:10.1104/pp.110.1.73

Cited by 83 publications

(47 citation statements)

References 13 publications

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“…This enzyme has a higher molecular mass than the pectin and pectate lyases and was positively influenced by Ca 2ϩ but did not require Ca 2ϩ ions for catalysis (266). The activity of the enzyme was positively affected by the presence of galactose side chains and negatively affected by the presence of arabinose side chains and acetyl residues (266).…”

Section: Degradation Of the Pectin Backbonementioning

confidence: 99%

“…The A. niger pectin lyases characterized (A, B, and II) prefer substrates with a high degree of esterification. Only one rhamnogalacturonan lyase has been identified in aspergilli (203,266). This enzyme has a higher molecular mass than the pectin and pectate lyases and was positively influenced by Ca 2ϩ but did not require Ca 2ϩ ions for catalysis (266).…”

Section: Degradation Of the Pectin Backbonementioning

confidence: 99%

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AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

886

585

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SUMMARY Degradation of plant cell wall polysaccharides is of major importance in the food and feed, beverage, textile, and paper and pulp industries, as well as in several other industrial production processes. Enzymatic degradation of these polymers has received attention for many years and is becoming a more and more attractive alternative to chemical and mechanical processes. Over the past 15 years, much progress has been made in elucidating the structural characteristics of these polysaccharides and in characterizing the enzymes involved in their degradation and the genes of biotechnologically relevant microorganisms encoding these enzymes. The members of the fungal genus Aspergillus are commonly used for the production of polysaccharide-degrading enzymes. This genus produces a wide spectrum of cell wall-degrading enzymes, allowing not only complete degradation of the polysaccharides but also tailored modifications by using specific enzymes purified from these fungi. This review summarizes our current knowledge of the cell wall polysaccharide-degrading enzymes from aspergilli and the genes by which they are encoded.

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Section: Degradation Of the Pectin Backbonementioning

confidence: 99%

Section: Degradation Of the Pectin Backbonementioning

confidence: 99%

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

886

585

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“…Breakdown of rhamnogalacturonan is mainly mediated by two rhamnogalacturonan-degrading enzymes, rhamnogalacturonan hydrolase (RGaseA) and rhamnogalacturonan lyase (RGaseB). The rhamnogalacturonandegrading system of Aspergillus aculeatus has been well characterized, and three-dimensional structures of RGaseA and RGaseB have been elucidated, contributing toward the understanding of their structure-function relationship (Kofod et al, 1994, Mutter et al, 1994, Mutter et al, 1996a, Mutter et al, 1996b, Mutter et al, 1998, McDonough et al, 2004, Jensen et al, 2010. Furthermore, the usefulness of these enzymes in the processing of food has been confirmed.…”

Section: Introductionmentioning

confidence: 91%

Sequence Analysis and Heterologous Expression of Rhamnogalacturonan Lyase A Gene (AsrglA) from Shoyu Koji Mold, Aspergillus sojae KBN1340

Yoshino-Yasuda¹,

Karita²,

Kato³

et al. 2012

FSTR

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The rhamnogalacturonan lyase A gene, designated AsrglA, was isolated from a shoyu koji mold, Aspergillus sojae KBN1340, and characterized. The structural gene comprised 2,245 bp with 11 introns. The open reading frame encoded a 528-residue protein with a signal peptide of 20 residues. AsrglA shared a high degree of sequence identity with Aspergillus oryzae rhamnogalacturonate lyase A and Aspergillus flavus rhamnogalacturonase B. Utilizing the promoter of the A. oryzae taaG2 gene, AsRglA was successfully expressed in A. oryzae and secreted into the culture medium. AsRglA had a molecular mass of 55.0 kDa, a pH optimum of 4.5, and a temperature optimum of 50℃.Keywords: shoyu koji mold, Aspergillus sojae, rhamnogalacturonan lyase gene, heterologous expression *To whom correspondence should be addressed. E-mail: shiyouko_yasuda@pref.aichi.lg.jp IntroductionThe filamentous fungus Aspergillus sojae is used for the production of fermented soy sauce (shoyu), a traditional Japanese food. A. sojae, when grown on a shoyu koji composed of soybean and wheat, secretes a large variety of carbohydrases and proteases. These enzymes are essential for the efficient maceration and hydrolysis of soybean and wheat. Among these enzymes, pectinolytic enzymes are the most important in soy sauce production as they improve the filtration efficiency of soy sauce mash and decrease the amount of the pressed cake (Kikuchi, 1977). Pectinolytic enzymes play a key role in the complete degradation of the plant cell wall, as the depolymerization of pectin exposes other cell wall components to degradation and leads to further cell wall breakdown. Pectin is one of the most complex polysaccharides with a backbone composed of homogalacturonan "smooth" regions and highly rhamnified "hairy" regions of rhamnogalacturonan (Willats et al., 2001). The canonical pectinolytic enzymes such as polygalacturonases and pectin lyases can fragment homogalacturonan but cannot degrade rhamnogalacturonan. Breakdown of rhamnogalacturonan is mainly mediated by two rhamnogalacturonan-degrading enzymes, rhamnogalacturonan hydrolase (RGaseA) and rhamnogalacturonan lyase (RGaseB). The rhamnogalacturonandegrading system of Aspergillus aculeatus has been well characterized, and three-dimensional structures of RGaseA and RGaseB have been elucidated, contributing toward the understanding of their structure-function relationship (Kofod et al., 1994, Mutter et al., 1994, Mutter et al., 1996a, Mutter et al., 1996b, Mutter et al., 1998, McDonough et al., 2004, Jensen et al., 2010. Furthermore, the usefulness of these enzymes in the processing of food has been confirmed. The solubilization of soybean cell wall material (CWM) by RGaseA and RGaseB in combination with other pectinolytic enzymes was compared in order to identify enzymes for new soybean processes or products (Heldt-Hansen et al., 1996). RGaseA was only able to solubilize 7% of the CWM, whereas addition of rhamnogalacturonan acetyl esterase and galactanase increased the solubilization to 17% and 44%, respectively. On the ot...

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“…This family contains two other proteins. Only one of them, produced by A. aculeatus, has been biochemically characterized as a rhamnogalacturonate lyase (18). Homology between these proteins was restricted to their C-terminal parts.…”

Section: E Chrysanthemi Secretes a Rhamnose-inducible Proteinmentioning

confidence: 99%

“…Only a few enzymes that are able to cleave the RG-I backbone have so far been characterized, mostly in Aspergillus aculeatus. A rhamnogalacturonate lyase (18) cleaves inside the chain between a rhamnose and a galacturonate, creating an unsaturation on the galacturonate at the nonreducing end. A rhamnogalacturonate rhamnohydrolase (17) and a rhamnogalacturonate galacturonohydrolase (16) cleave the rhamnose and galacturonate residues, respectively, present at the nonreducing end of the rhamnogalacturonate chain.…”

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confidence: 99%

Rhamnogalacturonate Lyase RhiE Is Secreted by the Out System in Erwinia chrysanthemi

Laatu

Condemine

2003

J Bacteriol

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Supernatants of rhamnose-induced Erwinia chrysanthemi strain 3937 cultures contain a principal secreted protein named RhiE. A rhiE mutant has been found among a set of rhamnose-induced MudI1681 lacZ fusions. RhiE is a 62-kDa protein that has rhamnogalacturonate lyase activity on rhamnogalacturonan I (RG-I). It does not require a divalent cation for its activity and has an optimal pH of 6.0. rhiE expression is strongly induced in the presence of rhamnose but is also regulated by PecT and Crp, two regulators of the transcription of pectinolytic enzyme genes. RhiE is secreted through the type II Out secretion pathway. RhiE has no disulfide bond. The absence of RhiE secretion in a dsb mutant indicated that disulfide bond formation is required for the biogenesis of the secretion apparatus. RhiE was searched for in several E. chrysanthemi strains by using antibodies, and it was found to be present in one-third of the strains tested. However, the reduced virulence of the rhiE mutant indicates that degradation of the RG-I region of pectin is important for full virulence of E. chrysanthemi.Pectin is one of the main components present in plant cell walls. The pectin molecule can have three types of backbone: homogalacturonan, rhamnogalacturonan I (RG-I), and RG-II. Homogalacturonan (polygalacturonate [PGA]) is a polymer of galacturonic acid residues linked by ␣ 1-4 bonds which are partially methylated and acetylated. Homogalacturonan forms the smooth regions of pectin which are interspersed with hairy regions of RG-I and RG-II. RG-I has a backbone composed of as many as 100 repeats of the disaccharide ␣-L-rhamnose-␣-1,4-galacturonic acid. Side chains of arabinan or galactan are attached to O-4 of the rhamnosyl residues. RG-II is a complex polysaccharide with a short homogalacturonan backbone to which are linked side chains containing more than 10 different types of sugars (1).Plant-pathogenic microorganisms often secrete enzymes that are able to degrade the polysaccharides of cell walls in order to disorganize the plant tissue and obtain carbon sources for their growth. The enzymes that degrade the smooth regions of pectin have been extensively studied (26). The action of pectin methylesterases and of pectin acetylesterases liberates PGA. PGA is then degraded by pectate lyases or polygalacturonases that cleave either in an endo or in an exo mode. These enzymes have been characterized in bacteria as well in fungi. Much less is known about the enzymes degrading RG-I and RG-II. It seems that the presence of side chains prevents the degradation of the homogalacturonan backbone of RG-II by polygalacturonase and pectate lyases, and the debranching enzymes have not yet been characterized. Only a few enzymes that are able to cleave the RG-I backbone have so far been characterized, mostly in Aspergillus aculeatus. A rhamnogalacturonate lyase (18) cleaves inside the chain between a rhamnose and a galacturonate, creating an unsaturation on the galacturonate at the nonreducing end. A rhamnogalacturonate rhamnohydrolase (17) and a rha...

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Rhamnogalacturonase B from Aspergillus aculeatus Is a Rhamnogalacturonan [alpha]-L-Rhamnopyranosyl-(1->4)-[alpha]-D-Galactopyranosyluronide Lyase

Cited by 83 publications

References 13 publications

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Sequence Analysis and Heterologous Expression of Rhamnogalacturonan Lyase A Gene (AsrglA) from Shoyu Koji Mold, Aspergillus sojae KBN1340

Rhamnogalacturonate Lyase RhiE Is Secreted by the Out System in Erwinia chrysanthemi

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