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Selective Production of Xylooligosaccharides by Xylan Hydrolysis Using a Novel Recyclable and Separable Furoic Acid.

ABSTRACT: Xylooligosaccharides (XOS) have gained considerable attention worldwide as prebiotics due to their immune-strengthening activity and beneficial gut bacteria development and can be produced from xylan-rich resources by acid hydrolysis. The present study proved the organic acid hydrolysis to be beneficial for XOS yield. In this study, a recyclable and separable organic acid, i.e., furoic acid, was used for hydrolyzing xylan to produce XOS, and the response surface methodology design was applied to maximize the XOS yield; the results indicated that the quadratic model terms of the interaction between reaction temperature and hydrolysis time showed the most significant impact on XOS yields (P < 0.05). The predicted maximum yield of XOS was 49.0% with 1.2% furoic acid at 167°C for 33 min, being close to the experimental value (49.2%), indicating that the fitted models were in good agreement with the experimental results. Meanwhile, the primary byproducts, including xylose and furfural, were concurrently bio-oxidized into xylonic acid and furoic acid by Gluconobacter oxydans and separated by electrodialysis. Subsequently, the furoic acid with low solubility (<3.7%, 25°C) was recovered by natural crystallization. The above results indicate that the use of multi-steps contributes to sustainable XOS production by furoic acid.

SUBMITTER: Zhao J

PROVIDER: S-EPMC8062972 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:BackgroundXylan, the major constituent of hemicellulose, is composed of β-(1,4)-linked xylopyranosyl units that for the backbone, with side chains formed by other chemical moieties such as arabinose, galactose, mannose, ferulic acid and acetyl groups. Acetyl xylan esterases and α-L-arabinofuranosidases are two important accessory enzymes that remove side chain residues from xylan backbones and may act in synergy with other xylanolytic enzymes. Compared with enzymes possessing a single catalytic activity, multifunctional enzymes can achieve lignocellulosic biomass hydrolysis using a less complex mixture of enzymes.ResultsHere, we cloned an acetyl xylan esterase (PcAxe) from Penicillium chrysogenum P33 and expressed it in Pichia pastoris GS115. The optimal pH and temperature of the recombinant PcAxe (rPcAxe) for 4-nitrophenyl acetate were 7.0 and 40 °C, respectively. rPcAxe is stable across a broad pH range, retaining 100% enzyme activity om pH 6-9 after a 1 h incubation. The enzyme tolerates the presence of a wide range of metal ions. Sequence alignment revealed a GH62 domain exhibiting α-L-arabinofuranosidase activity with pH and temperature optima of pH 7.0 and 50 °C, in addition to the expected esterase domain. rPcAxe displayed significant synergy with a recombinant xylanase, with a degree of synergy of 1.35 for the hydrolysis of delignified corn stover. Release of glucose was increased by 51% from delignified corn stover when 2 mg of a commercial cellulase was replaced by an equivalent amount of rPcAxe, indicating superior hydrolytic efficiency.ConclusionsThe novel bifunctional enzyme PcAxe was identified in P. chrysogenum P33. rPcAxe includes a carbohydrate esterase domain and a glycosyl hydrolase family 62 domain. This is the first detailed report on a novel bifunctional enzyme possessing acetyl xylan esterase and α-L-arabinofuranosidase activities. These findings expand our current knowledge of glycoside hydrolases and pave the way for the discovery of similar novel enzymes.

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Selective Production of Xylooligosaccharides by Xylan Hydrolysis Using a Novel Recyclable and Separable Furoic Acid.

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