A non-modular type B feruloyl esterase from Neurospora crassa exhibits concentration-dependent substrate inhibition

Crepin, Valérie F.; Faulds, Craig B.; Connerton, Ian F.

doi:10.1042/bj20020917

Cited by 84 publications

(37 citation statements)

References 54 publications

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“…FAEA was also produced in Pichia pastoris (23) at up to 300 mg liter Ϫ1 . FAEC from Talaromyces stipitatus was also produced in P. pastoris, and the secretion yield was within the 200-to-300-mg ml Ϫ1 range, depending on the nature of the signal peptide used (17).…”

Section: Discussionmentioning

confidence: 99%

Gene Overexpression and Biochemical Characterization of the Biotechnologically Relevant Chlorogenic Acid Hydrolase fromAspergillus niger

Benoit¹,

Asther²,

Bourne

et al. 2007

Appl Environ Microbiol

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The full-length gene that encodes the chlorogenic acid hydrolase from Aspergillus niger CIRM BRFM 131 was cloned by PCR based on the genome of the strain A. niger CBS 513.88. The complete gene consists of 1,715 bp and codes for a deduced protein of 512 amino acids with a molecular mass of 55,264 Da and an acidic pI of 4.6. The gene was successfully cloned and overexpressed in A. niger to yield 1.25 g liter ؊1 , i.e., 330-fold higher than the production of wild-type strain A. niger CIRM BRFM131. The histidine-tagged recombinant ChlE protein was purified to homogeneity via a single chromatography step, and its main biochemical properties were characterized. The molecular size of the protein checked by mass spectroscopy was 74,553 Da, suggesting the presence of glycosylation. ChlE is assembled in a tetrameric form with several acidic isoforms with pIs of around 4.55 and 5.2. Other characteristics, such as optimal pH and temperature, were found to be similar to those determined for the previously characterized chlorogenic acid hydrolase of A. niger CIRM BRFM 131. However, there was a significant temperature stability difference in favor of the recombinant protein. ChlE exhibits a catalytic efficiency of 12.5 ؋ 10 6 M ؊1 s ؊1 toward chlorogenic acid (CGA), and its ability to release caffeic acid from CGA present in agricultural by-products such as apple marc and coffee pulp was clearly demonstrated, confirming the high potential of this enzyme.

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Section: Discussionmentioning

confidence: 99%

Gene Overexpression and Biochemical Characterization of the Biotechnologically Relevant Chlorogenic Acid Hydrolase fromAspergillus niger

Benoit¹,

Asther²,

Bourne

et al. 2007

Appl Environ Microbiol

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“…So far, there has been no report concerning the primary structure of prokaryotic FAE in spite of the publication of some studies of the gene encoding the FAE from eukaryotic cells (8,10; GenBank accession no. AB032760).…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of a Feruloyl Esterase from the Intestinal BacteriumLactobacillus acidophilus

Wang

Geng

Egashira

et al. 2004

Appl Environ Microbiol

110

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Dietary ferulic acid (FA), a significant antioxidant substance, is currently the subject of extensive research. FA in cereals exists mainly as feruloylated sugar ester. To release FA from food matrices, it is necessary to cleave ester cross-linking by feruloyl esterase (FAE) (hydroxycinnamoyl esterase; EC 3.1.1.73). In the present study, the FAE from a human typical intestinal bacterium, Lactobacillus acidophilus, was isolated, purified, and characterized for the first time. The enzyme was purified in successive steps including hydrophobic interaction chromatography and anion-exchange chromatography. The purified FAE appeared as a single band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, with an apparent molecular mass of 36 kDa. It has optimum pH and temperature characteristics (5.6 and 37°C, respectively). Ferulic acid (FA) is a common component in plant cell walls and shows strong antioxidant potential by its radical-scavenging ability (16). In recent years, the results of many in vitro and in vivo studies have indicated that FA prevents low-density lipoprotein from oxidation (2, 27, 29, 31), exhibits inhibitory effects on tumor promotion (1, 17), and protects against certain chronic diseases such as coronary heart disease and some cancers (6,20,21,37).In cereals, FA is mainly ester linked with arabinose or galactose residues (which constitute side chains of cell wall polysaccharides) (15,18,19,28,34,38). Wende et al. showed that FA was released from 2-O-␤-D-xylopyranosyl-(5-O-feruloyl)-Larabinose by rat gut microorganisms quite quickly and presumed that feruloyl esterase (FAE) would be produced by microorganisms, with high-level activity which is closely related to the release (40). Subsequently, other in vitro observations confirmed the existence of FAE in animal and human intestines (3, 23). These results suggest that FAE plays an important role in releasing free FA from different feruloylated forms in foodstuff in the gut.Although FAEs from some eukaryotic cells (4,7,11,12,14,22,26,39) and from only one prokaryotic cell (13) have been purified and characterized to date, there is no information about FAE from intestinal bacteria. It is reported that FAEs from various sources show different properties with respect to such characteristics as optimal temperature and optimal pH. Therefore, it is necessary to purify the FAE from human gut bacteria to further study the mechanism of release of FA from complex food matrices in vitro. Nishizawa et al. studied the FAE activities of typical intestinal bacteria and found that among the intestinal bacteria tested, Lactobacillus acidophilus exhibited the highest level of activity with respect to feruloylated arabinose ester (30).Some investigations indicate that the presence of xylanase enhances FAE activity. In most of these studies, however, destarched wheat bran was used as a substrate; these experiments could not supply sufficiently detailed information to explain the releasing mechanism of dietary FA and the interaction between xylanase and FAE to ...

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“…This has stimulated great interests in developing enzymatic methods to recover ferulic acid from biomass (Bonnin et al, 2002;de Vries et al, 2000;Faulds et al, 2004Faulds et al, , 2005Saulnier et al, 2001;Yu et al, 2002). Consequent to these efforts, many novel ferulic acid esterases (FAEs) were discovered (Crepin et al, 2003GarciaConesa et al, 2004;Rumbold et al, 2003;Shin and Chen, 2006;Topakas et al, 2003aTopakas et al, ,b, 2004Topakas et al, , 2005Wang et al, 2004). Despite its importance, FAE alone is not sufficient to release ferulic acid from the biomass matrix.…”

Section: Introductionmentioning

confidence: 96%

A complete enzymatic recovery of ferulic acid from corn residues with extracellular enzymes fromNeosartorya spinosa NRRL185

Shin

McClendon

et al. 2006

Biotechnol. Bioeng.

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An economic ferulic acid recovery from biomass via biological methods is of interest for a number of reasons. Ferulic acid is a precursor to vanillin synthesis. It is also a known antioxidant with potential food and medical applications. Despite its universal presence in all plant cell wall material, the complex structure of the plant cell wall makes ferulic acid recovery from biomass a challenging bioprocess. Previously, without pretreatment, very low (3-13%) recovery of ferulic acid from corn residues was achieved. We report here the discovery of a filamentous fungus Neosartorya spinosa NRRL185 capable of producing a full complement of enzymes to release ferulic acid and the development of an enzymatic process for a complete recovery of ferulic acid from corn bran and corn fibers. A partial characterization of the extracellular proteome of the microbe revealed the presence of at least seven cellulases and hemicellulases activities, including multiple iso-forms of xylanase and ferulic acid esterase. The recovered ferulic acid was bio-converted to vanillin, demonstrating its potential application in natural vanillin synthesis. The enzymatic ferulic acid recovery accompanied a significant release of reducing sugars (76-100%), suggesting much broader applications of the enzymes and enzyme mixtures from this organism.

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A non-modular type B feruloyl esterase from Neurospora crassa exhibits concentration-dependent substrate inhibition

Cited by 84 publications

References 54 publications

Gene Overexpression and Biochemical Characterization of the Biotechnologically Relevant Chlorogenic Acid Hydrolase fromAspergillus niger

Gene Overexpression and Biochemical Characterization of the Biotechnologically Relevant Chlorogenic Acid Hydrolase fromAspergillus niger

Purification and Characterization of a Feruloyl Esterase from the Intestinal BacteriumLactobacillus acidophilus

A complete enzymatic recovery of ferulic acid from corn residues with extracellular enzymes fromNeosartorya spinosa NRRL185

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