Chemical and thermal stability of ferulic acid (feruloyl) esterases from Aspergillus

Faulds, Craig B.; Aliwan, Fraj O; Vries, Ronald P. de; Pickersgill, Richard W.; Visser, Jaap; Williamson, Gary

doi:10.1016/s0921-0423(98)80007-5

Cited by 4 publications

(3 citation statements)

References 17 publications

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“…Chymotrypsin-like serine esterases have been histochemically demonstrated in the granules of intraepithelial mucosal mast cells of the gastrointestinal tract of rats and humans (34). Other cinnamoyl esterases such as FAEA from Aspergillus niger have been recognized as serine hydrolases (35) and, thus, it is possible that the intraepithelial serine hydrolases found in the mast cells may be responsible for the cinnamoyl esterase activity detected in the small intestine mucosa. Hydroxycinnamates are mostly ester-linked to hemicelluloses, forming large and complex molecules that cannot be absorbed through the mucosal barrier into the epithelial cells.…”

Section: Discussionmentioning

confidence: 99%

Esterase Activity Able To Hydrolyze Dietary Antioxidant Hydroxycinnamates Is Distributed along the Intestine of Mammals

Andreasen

Kroon

Williamson

et al. 2001

J. Agric. Food Chem.

270

176

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Hydroxycinnamic acids are effective antioxidants and are abundant components of plant cell walls, especially in cereal bran. For example, wheat and rye brans are rich sources of the hydroxycinnamates ferulic acid, sinapic acid, and p-coumaric acid. These phenolics are part of human and animal diets and may contribute to the beneficial effects derived from consumption of cereal bran. However, these compounds are ester linked to the main polymers in the plant cell wall and cannot be absorbed in this complex form. The present work shows that esterases with activity toward esters of the major dietary hydroxycinnamates are distributed throughout the intestinal tract of mammals. In rats, the cinnamoyl esterase activity in the small intestine is derived mainly from the mucosa, whereas in the large intestine the esterase activity was found predominantly in the luminal microflora. Mucosa cell-free extracts obtained from human duodenum, jejunum, and ileum efficiently hydrolyzed various hydroxycinnamoyl esters, providing the first evidence of human cinnamoyl esterase(s). This study first demonstrates the release by human colonic esterase(s) (mostly of microbial origin) of sinapic acid and p-coumaric acid from rye and wheat brans. Hydrolysis by intestinal esterase(s) is very likely the major route for release of antioxidant hydroxycinnamic acids in vivo.

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Section: Discussionmentioning

confidence: 99%

Esterase Activity Able To Hydrolyze Dietary Antioxidant Hydroxycinnamates Is Distributed along the Intestine of Mammals

Andreasen

Kroon

Williamson

et al. 2001

J. Agric. Food Chem.

270

176

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show abstract

“…The purified AtFAE displayed a 36 kDa protein species on SDS-PAGE (Fig. 1), similar to the A. niger FAEA (Faulds et al 1998), and peptide mass fingerprinting (PMF) confirmed the presence of AtFAEA with a protein score of 146 and a 100% confidence interval (data not shown).…”

Section: Purification and Characterisation Of Recombinant Atfaeamentioning

confidence: 73%

Enrichment of maize and triticale bran with recombinant Aspergillus tubingensis ferulic acid esterase

Zwane

Zyl²,

Duodu

et al. 2017

J Food Sci Technol

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Ferulic acid is a natural antioxidant found in various plants and serves as a precursor for various fine chemicals, including the flavouring agent vanillin. However, expensive extraction methods have limited the commercial application of ferulic acid, in particular for the enrichment of food substrates. A recombinant Aspergillus tubingensis ferulic acid esterase Type A (FAEA) was expressed in Aspergillus niger D15#26 and purified with anion-exchange chromatography (3487 U/mg, K m = 0.43 mM, K cat = 0.48/min on methyl ferulate). The 36-kDa AtFAEA protein showed maximum ferulic acid esterase activity at 50°C and pH 6, suggesting potential application in industrial processes. A crude AtFAEA preparation extracted 26.56 and 8.86 mg/g ferulic acid from maize bran and triticale bran, respectively, and also significantly increased the levels of p-coumaric and caffeic acid from triticale bran. The cost-effective production of AtFAEA could therefore allow for the enrichment of brans generally used as food and fodder, or for the production of fine chemicals (such as ferulic and p-coumaric acid) from plant substrates. The potential for larger-scale production of AtFAEA was demonstrated with the A. niger D15[AtfaeA] strain yielding a higher enzyme activity (185.14 vs.83.48 U/ml) and volumetric productivity (3.86 vs. 1.74 U/ ml/h) in fed-batch than batch fermentation.

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“…In addition, its expression was detected under wide range of NaCl concentrations when plants were treated with SA more than salinized-SA-untreated plants. Esterases can liberate ferulic acid from polysaccharides which form components of lignin in plant cell wall (Scalbert et al 1985;Faulds et al 1998;Faulds et al 2010). Dehydration stress was avoided when ferulic acid was used due to increase the activities of several antioxidant enzymes such as catalase, superoxide dismutase, and quaiacol peroxidase and it associated with increase transcripts of respective genes.…”

Section: Discussionmentioning

confidence: 99%

Salicylic acid-mediated salt stress tolerance by mitigation of the oxidative effects in Moringa

Hassanein¹,

El-nagish²,

Salem³

2020

Journal of Environmental Studies

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Chemical and thermal stability of ferulic acid (feruloyl) esterases from Aspergillus

Cited by 4 publications

References 17 publications

Esterase Activity Able To Hydrolyze Dietary Antioxidant Hydroxycinnamates Is Distributed along the Intestine of Mammals

Esterase Activity Able To Hydrolyze Dietary Antioxidant Hydroxycinnamates Is Distributed along the Intestine of Mammals

Enrichment of maize and triticale bran with recombinant Aspergillus tubingensis ferulic acid esterase

Salicylic acid-mediated salt stress tolerance by mitigation of the oxidative effects in Moringa

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