Isolation and Characterization of a Chlorogenic Acid Esterase from Aspergillus niger

Schobel, B; Pollmann, W.

doi:10.1515/znc-1980-3-407

Cited by 19 publications

(7 citation statements)

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“…Schöbel and Pollmann (1980a) isolated a tetrameric chlorogenic acid esterase (EC 3.1.1.42) from Aspergillus niger using a pectinolytic enzyme preparation. An hydroxycinnamic acid ester hydrolase was purified from A. japonicus (Okamura and Watanabe, 1982).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a chlorogenic acid hydrolase from Aspergillus niger catalysing the hydrolysis of chlorogenic acid

Asther¹,

Estrada‐Alvarado²,

Haon³

et al. 2005

Journal of Biotechnology

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Section: Introductionmentioning

confidence: 99%

Purification and characterization of a chlorogenic acid hydrolase from Aspergillus niger catalysing the hydrolysis of chlorogenic acid

Asther¹,

Estrada‐Alvarado²,

Haon³

et al. 2005

Journal of Biotechnology

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“…UmChlE retained Ͼ80% of its maximum activity between pH 4.5 and 10. The determined pH optima of the two previously reported chlorogenic acid esterases from A. niger (12,13) and of type B FAEs described previously by Koseki et al (36) were between pH 6 and 7. Especially, the pH stability of UmChlE was different from that of the characterized chlorogenic acid esterases from A. niger, which were more stable under acidic than under alkaline conditions.…”

Section: Characterization Of the Purified Chlorogenic Acid Esterasementioning

confidence: 60%

“…To date, only a few chlorogenic acid esterases (EC 3.1.1.42) have been well characterized (11)(12)(13)(14)(15), while numerous feruloyl esterases (FAEs) (EC 3.1.1.73), a subclass of the carboxylic ester hydrolases, from a wide range of bacteria and fungi have been purified and characterized (7)(8)(9)(10). Some feruloyl esterases showed the ability to hydrolyze chlorogenic acid, such as A. niger FAEB (34) and a type B feruloyl esterase from Neurospora crassa (35).…”

Section: Characterization Of the Purified Chlorogenic Acid Esterasementioning

confidence: 99%

“…To date, a small number of chlorogenic acid esterases have been reported, all from Aspergillus sp. In 1980, Schöbel and Pollmann (11,12) reported a specific chlorogenic acid esterase from a pectinolytic enzyme preparation of Aspergillus niger. More recently, Asther et al (13) demonstrated that another A. niger enzyme releases caffeic acid from industrial by-products such as coffee pulp (CP) and apple marc.…”

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confidence: 99%

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A Chlorogenic Acid Esterase with a Unique Substrate Specificity from Ustilago maydis

Nieter

Haase-Aschoff

Kelle

et al. 2015

Appl Environ Microbiol

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An extracellular chlorogenic acid esterase from Ustilago maydis (UmChlE) was purified to homogeneity by using three separation steps, including anion-exchange chromatography on a Q Sepharose FF column, preparative isoelectric focusing (IEF), and, finally, a combination of affinity chromatography and hydrophobic interaction chromatography on polyamide. SDS-PAGE analysis suggested a monomeric protein of ϳ71 kDa. The purified enzyme showed maximal activity at pH 7.5 and at 37°C and was active over a wide pH range (3.5 to 9.5). Previously described chlorogenic acid esterases exhibited a comparable affinity for chlorogenic acid, but the enzyme from Ustilago was also active on typical feruloyl esterase substrates. Kinetic , respectively. UmChlE released ferulic, p-coumaric, and caffeic acids from natural substrates such as destarched wheat bran (DSWB) and coffee pulp (CP), confirming activity on complex plant biomass. The full-length gene encoding UmChlE consisted of 1,758 bp, corresponding to a protein of 585 amino acids, and was functionally produced in Pichia pastoris GS115. Sequence alignments with annotated chlorogenic acid and feruloyl esterases underlined the uniqueness of this enzyme. P lant cell walls consist of a heterogeneous mixture of polymers, including cellulose, hemicellulose, pectin, and lignin. In addition to these main components, hydroxycinnamates play a key role in the formation of a complex network of these polymers. While hydroxycinnamates covalently cross-link plant cell wall polysaccharides to each other by ester bonds, links between polysaccharides and lignin are formed mainly by ether linkages (1). Thus, these phenolic acids (mainly ferulic, p-coumaric, and caffeic acids) not only influence the rigidity and mechanical properties of the cell wall but also play a role in plant defense (2). They are linked differently to sugar residues in plants: in grasses such as wheat, barley, or maize, ferulates and p-coumarates are mainly found esterified to the O-5 position of arabinose residues, whereas in pectin of dicotyledons, such as spinach or sugar beet, ferulic acid is esterified to the O-2 position of arabinose and the O-6 position of galactose residues (3). Furthermore, hydroxycinnamates also exist as soluble ester conjugates of quinic acid, the best-known example being chlorogenic acid [3-(3,4-dihydroxycinnamoyl)quinic acid] (4). Particularly high concentrations of chlorogenic acid are present in coffee, apple, pear, and potato tuber (4). The health, cosmetic, and pharmaceutical industries are especially interested in hydroxycinnamates due to their anticarcinogenic, anti-inflammatory, and antioxidant properties (5). Consequently, enzymes that are able to release these phenolic compounds are not only essential for the degradation of plant biomass but also of interest for potential food and medical applications of the released products.One group of these enzymes is the feruloyl esterases (FAEs) (EC 3.1.1.73), a subclass of the carboxylic ester hydrolases (EC 3.1.1). They hydrolyze the ester lin...

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“…Included in the chemical family of chlorogenates are additional esters of caffeate, and these compounds are hydrolyzed with various degrees of efficiency by an extracellular chlorogenate esterase (EC 3.1.1. 43) from Aspergillus niger (54,55) or Aspergillus japonicus (45,46). A preparation of the latter enzyme is commercially available (http://www.kikkoman.co.jp/bio/j/rinsyou/enzymes/) and is used to control bitterness and to prevent enzymatic browning in the preparation of juice, wine, and coffee.…”

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confidence: 99%

Genes for Chlorogenate and Hydroxycinnamate Catabolism ( hca ) Are Linked to Functionally Related Genes in the dca-pca-qui-pob-hca Chromosomal Cluster of Acinetobacter sp. Strain ADP1

Smith

Weaver

Young

et al. 2003

Appl Environ Microbiol

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Hydroxycinnamates are ubiquitous in the environment because of their contributions to the structure and defense mechanisms of plants. Additional plant products, many of which are formed in response to stress, support the growth of Acinetobacter sp. strain ADP1 through pathways encoded by genes in the dca-pca-qui-pob chromosomal cluster. In an appropriate genetic background, it was possible to select for an Acinetobacter strain that had lost the ability to grow with caffeate, a commonly occurring hydroxycinnamate. The newly identified mutation was shown to be a deletion in a gene designated hcaC and encoding a ligase required for conversion of commonly occurring hydroxycinnamates (caffeate, ferulate, coumarate, and 3,4-dihydroxyphenylpropionate) to thioesters. Linkage analysis showed that hcaC is linked to pobA. Downstream from hcaC and transcribed in the direction opposite the direction of pobA transcription are open reading frames designated hcaDEFG. Functions of these genes were inferred from sequence comparisons and from the properties of knockout mutants. HcaD corresponded to an acyl coenzyme A (acyl-CoA) dehydrogenase required for conversion of 3,4-dihydroxyphenylpropionyl-CoA to caffeoyl-CoA. HcaE appears to encode a member of a family of outer membrane proteins known as porins. Knockout mutations in hcaF confer no discernible phenotype. Knockout mutations in hcaG indicate that this gene encodes a membrane-associated esterase that hydrolyzes chlorogenate to quinate, which is metabolized in the periplasm, and caffeate, which is metabolized by intracellular enzymes. The chromosomal location of hcaG, between hcaC (required for growth with caffeate) and quiA (required for growth with quinate), provided the essential clue that led to the genetic test of HcaG as the esterase that produces caffeate and quinate from chlorogenate. Thus, in this study, organization within what is now established as the dca-pca-qui-pob-hca chromosomal cluster provided essential information about the function of genes in the environment.

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Isolation and Characterization of a Chlorogenic Acid Esterase from Aspergillus niger

Cited by 19 publications

References 0 publications

Purification and characterization of a chlorogenic acid hydrolase from Aspergillus niger catalysing the hydrolysis of chlorogenic acid

Purification and characterization of a chlorogenic acid hydrolase from Aspergillus niger catalysing the hydrolysis of chlorogenic acid

A Chlorogenic Acid Esterase with a Unique Substrate Specificity from Ustilago maydis

Genes for Chlorogenate and Hydroxycinnamate Catabolism ( hca ) Are Linked to Functionally Related Genes in the dca-pca-qui-pob-hca Chromosomal Cluster of Acinetobacter sp. Strain ADP1

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