Production of xylan-hydrolyzing enzymes by Aureobasidium pullulans

Myburgh, Jacobus; Prior, Bernard A.; Kilian, S. G.

doi:10.1016/0922-338x(91)90325-b

Cited by 17 publications

(5 citation statements)

References 21 publications

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“…: Fr., Streptomyces spp. and Aureobasidium pullulans (de Bary) Arnaud (MacKenzie et al, 1987;Biely et al, 1988;MacKenzie and Bilous, 1988;Myburgh et al, 1991). These enzymes are considered to act in the cooperative degradation of the isolated acetylated xylan (Biely et al, 1986).…”

Section: Discussionmentioning

confidence: 96%

Production of acetyl esterase during wood biodegradation by Coriolus versicolor

1998

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A role of acetyl esterase in wood biodegradation by Coriolus versicolor was examined by the assay of enzyme production and the chemical analysis of decayed wood meal of Japanese beech (Fagus crenata). Enzyme assay demonstrated that the degradation proceeded in two stages and acetyl esterase production was correlated with the cellulolytic and xylanolytic enzyme production in the second stage, not with the production of phenol-oxidizing enzymes. From the results of chemical analysis, acetyl and xylose contents in wood meal were observed to decrease simultaneously in the second stage. In contrast, rapid decrease of lignin was recognized during the initial three wk of incubation, and it was closely related with the production of phenol-oxidizing enzymes in the first stage. These results show that acetyl esterase of C. versicolor participates in the degradation of acetylxylan and acts with the cellulolytic and xylanolytic systems, not with the ligninolytic system.

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Section: Discussionmentioning

confidence: 96%

Production of acetyl esterase during wood biodegradation by Coriolus versicolor

1998

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“…Brightly pigmented, so‐called color variant strains of Aureobasidium are good sources of endoxylanase with a high specific activity [7–9]. Color variant strains overproduce xylanase at 10–100 times levels of typically pigmented strains.…”

Section: Saccharification Of Corn Fibermentioning

confidence: 99%

Bioconversions of maize residues to value-added coproducts using yeast-like fungi

Leathers

2003

FEMS Yeast Research

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Agricultural residues are abundant potential feedstocks for bioconversions to industrial fuels and chemicals. Every bushel of maize (approximately 25 kg) processed for sweeteners, oil, or ethanol generates nearly 7 kg of protein- and fiber-rich residues. Currently these materials are sold for very low returns as animal feed ingredients. Yeast-like fungi are promising biocatalysts for conversions of agricultural residues. Although corn fiber (pericarp) arabinoxylan is resistant to digestion by commercially available enzymes, a crude mixture of enzymes from the yeast-like fungus Aureobasidium partially saccharifies corn fiber without chemical pretreatment. Sugars derived from corn fiber can be converted to ethanol or other valuable products using a variety of naturally occurring or recombinant yeasts. Examples are presented of Pichia guilliermondii strains for the conversion of corn fiber hydrolysates to the alternative sweetener xylitol. Corn-based fuel ethanol production also generates enormous volumes of low-value stillage residues. These nutritionally rich materials are prospective substrates for numerous yeast fermentations. Strains of Aureobasidium and the red yeast Phaffia rhodozyma utilize stillage residues for production of the polysaccharide pullulan and the carotenoid astaxanthin, respectively.

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“…On the other hand, a band around 46 kDa became more evident after the partial purification. The previous works reporting the production of esterases by A. pullulans are mainly focused on specific enzymatic activities such as feruloyl esterase (molecular weight of 210 kDa) [54], acetyl esterase (molecular weight not reported) [55] or acetyl xylan esterase (molecular weight not reported) [56]. Nevertheless, esterases from yeast-like organisms (including other Aureobasidium sp.)…”

Section: Partial Purification Of Esterasementioning

confidence: 99%

Integrated strategy for purification of esterase from Aureobasidium pullulans

Lemes

Silvério

Rodrigues

et al. 2019

Separation and Purification Technology

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Esterases catalyze the cleavage and formation of ester bonds of a broad range of substrates presenting a widespread spectrum of industrial applications. This work aimed to partially purify and characterize an esterase from Aureobasidium pullulans LABIOTEC 01 produced in a culture medium containing olive mill wastewater. Esterase purification was evaluated using different strategies, namely the enzyme recovery by PEG-salt aqueous twophase systems (ATPSs); and the enzyme precipitation with ammonium sulfate, acetone, and ethanol. The best purification factor (18 ± 2) was obtained when the ATPS composed of 20% (w/w) polyethylene glycol (PEG) 6000 and 5.8% (w/w) potassium phosphate buffer (PPB) pH 8.0 was combined with acetone precipitation. The partially purified enzyme presented an optimum pH of 5.0, although it remained active in the pH range of 4.5 to 7.5 (≥ 50% relative activity). The optimum temperature was found to be 60°C. Furthermore, the addition of salts such as FeCl 3 , CuSO 4 and MnCl 2 promoted an increase in the enzymatic activity (above 100%). The enzyme was found to be stable and showed high activity when exposed to polar solvents such as dimethyl sulfoxide, dimethylformamide, and methanol. The use of an integrated strategy of purification combining simple purification methods such as ATPS and precipitation was herein reported for the first time for esterase. This strategy proved to be an interesting approach to partially purify the esterase produced under submerged fermentation by A. pullulans. Furthermore, the enzyme showed potential to be applied in industrial biocatalytic processes using high temperature and different salts or solvents. Also, the production of esterase using olive mill wastewater as substrate demonstrated to be a suitable alternative to reduce and valorize agro-industrial residues.

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Production of xylan-hydrolyzing enzymes by Aureobasidium pullulans

Cited by 17 publications

References 21 publications

Production of acetyl esterase during wood biodegradation by Coriolus versicolor

Production of acetyl esterase during wood biodegradation by Coriolus versicolor

Bioconversions of maize residues to value-added coproducts using yeast-like fungi

Integrated strategy for purification of esterase from Aureobasidium pullulans

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