Lignocellulose degradation for the bioeconomy: The potential of enzyme synergies between xylanases, ferulic acid esterase and laccase for the production of arabinoxylo-oligosaccharides

Schmitz, Eva; Leontakianakou, Savvina; Norlander, Siri; Karlsson, Eva Nordberg; Adlercreutz, Patrick

doi:10.1016/j.biortech.2021.126114

Cited by 30 publications

(24 citation statements)

References 32 publications

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“…During our previous study on synergistic enzymatic degradation of pre-treated complex carbohydrates originating from the agricultural side streams oat hull, oat bran and corn bran, the arabinoxylanase CtXyn5A in combination with a laccase resulted in a similar modification of the lignin fraction as the combination of a ferulic acid esterase (FAE) with the laccase [13] . This observation was only made for these two enzyme combinations, leading us to suspect an esterase side activity of CtXyn5A.…”

Section: Resultsmentioning

confidence: 99%

“…Two different complex carbohydrate as well as three different model substrates were used in this study. The complex carbohydrates originated from the highly feruloylated agricultural side streams corn bran and oat hull as described in Schmitz et al [13] . Details on their origin and pre-treatment are described in Table 2.…”

Section: Methodsmentioning

confidence: 99%

“…The imidazole and buffer salts were purchased from Sigma-Aldrich, while the organic solvents were obtained from VWR. [13,20] Ultrasound assisted alkali according to [20] Arabinoxylan Production and Purification of CtXyn5A-E279S. The truncated gene encoding the two-domain construct (GH5-CBM6) corresponding to CtXyn5A from A. thermocellus, with the catalytic nucleophile Glu279replaced by Ser (E279S) was chemically synthesized (GenScript USA Inc., Piscataway, NJ, USA) with native codons and cloned into the expression vector pET21b (+) with a His-tag introduced to the C-terminus.…”

Section: Methodsmentioning

confidence: 99%

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Novel Function of CtXyn5A from Acetivibrio thermocellus: Dual Arabinoxylanase and Feruloyl Esterase Activity Occur in the Same Active Site

Schmitz

Leontakianakou

Adlercreutz

et al. 2022

Preprint

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Uncharacterized side activities of enzymes can have significant negative effects on reaction products and yields. Hence, their identification and characterization is crucial for the development of successful reaction systems. Here, we report the presence of feruloyl esterase activity in CtXyn5A from Acetivibrio thermocellus besides its well-known arabinoxylanase activity for the first time. Both reaction types appear to be catalysed in the same active site in two subsequential steps. The ferulic acid substituent is cleaved off first, followed by the hydrolysis of the xylan backbone. The esterase activity on complex carbohydrates was found to be higher than the one of a designated ferulic acid esterase (E-FAERU). Therefore, we conclude that the enzyme exhibits a dual function rather than an esterase side activity.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Novel Function of CtXyn5A from Acetivibrio thermocellus: Dual Arabinoxylanase and Feruloyl Esterase Activity Occur in the Same Active Site

Schmitz

Leontakianakou

Adlercreutz

et al. 2022

Preprint

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“…The percentage of hydrolyzed beechwood xylan is higher than the reported with other xylanolytic enzymes, is typically lower than 20% [33,44]. This can be the consequence of the presence of a cocktail of hydrolytic enzymes in Depol 670L preparation, as the synergistic action of xylanolytic enzymes is demonstrated to increase the yield of XOS [50].…”

Section: Large-scale Purification Of Acidic Xosmentioning

confidence: 90%

Enzymatic bioconversion of beechwood xylan into the antioxidant 2′-O-α-(4-O-methyl-D-glucuronosyl)-xylobiose

Míguez

Fernandez-Polo

Santos-Moriano

et al. 2022

Biomass Conv. Bioref.

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Acidic xylooligosaccharides (XOS), also called aldouronics, are hetero-oligomers of xylose randomly branched with 4-O-methyl-D-glucuronic acid residues linked by α(1 → 2) bonds, which display bioactive properties. We have developed a simple and integrated method for the production of acidic XOS by enzymatic hydrolysis of a glucurono-xylan from beechwood. Among the enzymes screened, Depol 670L (a cellulolytic preparation from Trichoderma reesei) displayed the highest activity (70.3 U/mL, expressed in reducing xylose equivalents). High-performance anion-exchange chromatography coupled with pulsed amperometric detection (HPAEC-PAD) analysis revealed the formation of a neutral fraction (corresponding to linear XOS, mainly xylose and xylobiose) and a group of more retained products (acidic XOS), which were separated using strong anion-exchange cartridges. The acidic fraction contained a major product, characterized by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry and mono- and two-dimensional nuclear magnetic resonance spectroscopy (NMR) as 2′-O-α-(4-O-methyl-α-D-glucuronosyl)-xylobiose (X2_MeGlcA). Starting from 2 g of beechwood xylan, 1.5 g of total XOS were obtained, from which 225 mg (11% yield) corresponded to the aldouronic X2_MeGlcA. The acidic XOS exhibited higher antioxidant activity (measured by the ABTS·+ discoloration assay) than xylan, whilst neutral XOS displayed no antioxidant activity. This work demonstrates that it is possible to obtain a safe and natural antioxidant by enzymatic biotransformation of hardwood hemicellulose.

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“…Corn bran (or corn bre) is an agricultural by-product obtained from corn processing. It was well recognized that corn bran polysaccharides were very di cult to be decomposed by enzymatic hydrolysis (51)(52)(53)(54). Its recalcitrance was regarded due to the rich content of glucuronoarabinoxylan which was extensively decorated with variations of both monomeric and oligomeric substitutions (55).…”

Section: Hydrolysis Action Of Ttgh74 or Ttgh74δcbm On Pretreated Corn...mentioning

confidence: 99%

Comparison of a GH74 xyloglucanase and its CBM-deleted variant from Thielavia terrestris and their roles in xyloglucan-rich biomass degradation

Wang

Chen

Zhang

et al. 2022

Preprint

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Background The hydrolysis of lignocellulose was greatly hindered by the associated hemicellulose. Xyloglucan (XG) is a major complex hemicellulose in the primary plant cell wall, however, the blocking effect of xyloglucan on lignocellulose biodegradation was still less understood compared with xylan and mannan. Glycoside hydrolase family 74 (GH74) enzymes are specific xyloglucanases widely distributed in bacteria and fungi. Fungal GH74 xyloglucanases generally contains family 1 carbohydrate binding module (CBM1), but its effect on the enzymatic properties of GH74 xyloglucanases and its roles in xyloglucan-rich biomass degradation has not been investigated in depth. Results TtGH74 and CBM-deleted variant (TtGH74ΔCBM) from Thielavia terrestris had the same optimum temperature and pH, but TtGH74ΔCBM had higher thermostability. TtGH74 displayed high binding affinity on xyloglucan and cellulose, while TtGH74ΔCBM almost completely lost the adsorption capacity on cellulose. Their hydrolysis action alone or combined with other glycoside hydrolases on the free XG, xyloglucan-coated phosphoric acid swollen cellulose or pretreated corn bran and apple pomace was compared in this study. CBM1 might not be essential for hydrolysis of free XG, but effective for the associated XG to some extent. TtGH74 was more effective in hydrolysis of xyloglucan in corn bran, while TtGH74ΔCBM showed relatively higher catalytic activity on apple pomace. Similar phenomenon was also observed when TtGH74 or TtGH74ΔCBM synergistically acting with CBH1/EG1 mixture. The addition of TtGH74 or TtGH74ΔCBM in CBH1/EG1 mixture significantly facilitated the overall hydrolysis of pretreated corn bran and apple pomace by 1.22–2.02 folds in terms of the degree of synergy. The extra addition of GH10 xylanase in TtGH74 or TtGH74ΔCBM /CBH1/EG1 mixture further improved the overall hydrolysis efficiency, and the degree of synergy was up to 1.50–2.16 because of co-existence of xyloglucan and xylan in pretreated corn bran and apple pomace. Conclusions TtGH74 can remove the bound xyloglucan on cellulose, therefore efficiently boost the hydrolysis of the pretreated lignocellulosic biomass by synergistic action with cellulase and xylanase. The presence of CBM1 in TtGH74 is conducive to enzymatic hydrolysis, but its role and significance is substrate-specific due to the differences of xyloglucan contents and structure in various biomasses.

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Lignocellulose degradation for the bioeconomy: The potential of enzyme synergies between xylanases, ferulic acid esterase and laccase for the production of arabinoxylo-oligosaccharides

Cited by 30 publications

References 32 publications

Novel Function of CtXyn5A from Acetivibrio thermocellus: Dual Arabinoxylanase and Feruloyl Esterase Activity Occur in the Same Active Site

Novel Function of CtXyn5A from Acetivibrio thermocellus: Dual Arabinoxylanase and Feruloyl Esterase Activity Occur in the Same Active Site

Enzymatic bioconversion of beechwood xylan into the antioxidant 2′-O-α-(4-O-methyl-D-glucuronosyl)-xylobiose

Comparison of a GH74 xyloglucanase and its CBM-deleted variant from Thielavia terrestris and their roles in xyloglucan-rich biomass degradation

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