Purification and Properties of a Feruloyl Esterase Involved in Lignocellulose Degradation by<i>Aureobasidium pullulans</i>

Rumbold, Karl; Biely, Peter; Mastihubová, Mária; Gudelj, Marinka; Gübitz, Georg; Robra, Karl‐Heinz; Prior, Bernard A.

doi:10.1128/aem.69.9.5622-5626.2003

Cited by 59 publications

(26 citation statements)

References 44 publications

(43 reference statements)

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“…the A. tubingensis strain was able to hydrolyse all the methyl esters evaluated in this study, except for Mca, indicating that it is a type a Fae, similar to those reported for A. niger, R. oryzae and A. awamori [14,33]. the R. oryzae strain was able to hydrolyse all the methyl esters, similar to the type c or D Fae reported for Clostridium stercorarium [36].…”

Section: Discussionsupporting

confidence: 79%

Overexpression of Aspergillus tubingensis faeA in protease-deficient Aspergillus niger enables ferulic acid production from plant material

Zwane

Rose

Zyl

et al. 2014

Journal of Industrial Microbiology and Biotechnology

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The production of ferulic acid esterase involved in the release of ferulic acid side groups from xylan was investigated in strains of Aspergillus tubingensis, Aspergillus carneus, Aspergillus niger and Rhizopus oryzae. The highest activity on triticale bran as sole carbon source was observed with the A. tubingensis T8.4 strain, which produced a type A ferulic acid esterase active against methyl p-coumarate, methyl ferulate and methyl sinapate. The activity of the A. tubingensis ferulic acid esterase (AtFAEA) was inhibited twofold by glucose and induced twofold in the presence of maize bran. An initial accumulation of endoglucanase was followed by the production of endoxylanase, suggesting a combined action with ferulic acid esterase on maize bran. A genomic copy of the A. tubingensis faeA gene was cloned and expressed in A. niger D15#26 under the control of the A. niger gpd promoter. The recombinant strain has reduced protease activity and does not acidify the media, therefore promoting high-level expression of recombinant enzymes. It produced 13.5 U/ml FAEA after 5 days on autoclaved maize bran as sole carbon source, which was threefold higher than for the A. tubingensis donor strain. The recombinant AtFAEA was able to extract 50 % of the available ferulic acid from non-pretreated maize bran, making this enzyme suitable for the biological production of ferulic acid from lignocellulosic plant material.

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Section: Discussionsupporting

confidence: 79%

Overexpression of Aspergillus tubingensis faeA in protease-deficient Aspergillus niger enables ferulic acid production from plant material

Zwane

Rose

Zyl

et al. 2014

Journal of Industrial Microbiology and Biotechnology

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“…A cinnamoyl esterase from Aspergillus niger CS 180 was reported to be a dimer and heavily glycosylated (Kroon et al 1996). A feruloyl esterase with 48% glycosylation from Aureobasidium pullulans was reported by Rumbold et al (2003). Both monomeric and dimeric feruloyl esterases have been purified from Aspergillus niger CBS 120.49 (Faulds and Williamson 1993).…”

Section: Enzyme Productionmentioning

confidence: 95%

Isolation and partial characterization of alkaline feruloyl esterases from Aspergillus niger CFR 1105 grown on wheat bran

Hegde

Muralikrishna

2009

World J Microbiol Biotechnol

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Feruloyl esterases (FAEs) of a strain of Aspergillus niger (CFR 1105) grown in solid state (ssf) and submerged fermentations (smf) using wheat bran both as carbon source and inducer of the enzyme were studied. The feruloyl esterase activity was maximum after 4 days in solid state as well as in submerged fermentations (32.5 and 31.5 U/g dry weight of wheat bran respectively) and the enzyme titers were comparable. The specific activity was maximum on day 2 in ssf (12.8 U/mg protein) and it decreased thereafter, whereas specific activity was maximum on day 3 (11.7 U/mg protein) in smf and it remained constant up to 5 days. Two isoenzymes of feruloyl esterases were isolated and purified to homogeneity by conventional protein purification methods from the day 5 culture filtrate of A. niger grown in smf. On a DEAEcellulose column, two enzyme activity peaks designated as FAE-1 and FAE-2 were eluted with 0.3 and 0.35 M NaCl, respectively. They were monomeric glycoproteins with approximate molecular weights of 50 kDa (FAE-1) and 55 kDa (FAE-2), respectively. FAE-1 showed a temperature optimum of 40°C whereas FAE-2 showed a wider temperature optimum of 40-50°C. FAE-1 and FAE-2 exhibited pH optima of 9 and 6, respectively, and both were stable over a pH range of 6-9. The ability of the enzyme to be active in alkaline pH may be advantageous in biotechnological applications.

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“…To our knowledge, not much work has been done to quantify esterase activities in A. pullulans especially not in the African tropics. We are aware of work carried out in South Africa on esterase activities from A. pullulans (Rumbold et al 2003). However, the strain used is from an American culture collection.…”

Section: Introduction *mentioning

confidence: 99%

Esterases and putative lipases from tropical isolates of Aureobasidium pullulans

Kudanga

Mwenje

Mandivenga

et al. 2007

J. Basic Microbiol.

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Esterases and lipases have been studied in a number of fungi, though very little is known about esterases from Aureobasidium pullulans especially from the African tropics. In this study, forty-two Zimbabwean isolates were screened for lipase activity on tributyrin agar. Extracellular esterase activities of seven selected isolates were studied under varying conditions using para-nitrophenol acetate as substrate. Twenty isolates (48%) showed lipolytic activity; sixteen showed negative results for lipase activity while the rest showed weak activities. Esterase activities in broth cultures ranged from 0.011-0.223 mmol/microg protein/min while activities ranged from 1.5-12.8 U/ml under solid state fermentation. The esterases were optimally active at pH 7.6-8.0, showed a temperature optimum of 35 degrees C and retained more than 50% activity at temperatures up to 60 degrees C and at pH 4.0-7.0 after 150 min. Enzyme production was optimal after 5-6 days with diammonium hydrogen phosphate as nitrogen source. Isolates showed variations in preference for carbon source for esterase production. The A. pullulans esterases differed from most fungal esterases in that they are optimally active in alkaline conditions and are active over a broad pH range.

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Purification and Properties of a Feruloyl Esterase Involved in Lignocellulose Degradation byAureobasidium pullulans

Cited by 59 publications

References 44 publications

Overexpression of Aspergillus tubingensis faeA in protease-deficient Aspergillus niger enables ferulic acid production from plant material

Overexpression of Aspergillus tubingensis faeA in protease-deficient Aspergillus niger enables ferulic acid production from plant material

Isolation and partial characterization of alkaline feruloyl esterases from Aspergillus niger CFR 1105 grown on wheat bran

Esterases and putative lipases from tropical isolates of Aureobasidium pullulans

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