Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds

Hüttner, Silvia; Klaubauf, Sylvia; Vries, Ronald P. de; Olsson, Lisbeth

doi:10.1007/s00253-017-8266-9

Cited by 29 publications

(29 citation statements)

References 45 publications

(69 reference statements)

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“…Feruloyl esterases are also applied for improving the quality of bread, preparation and clarification of juices, synthesis of oligosaccharides and production of medicinal compounds (Fazary and Ju 2013). Glucuronoyl esterases are active against a wide range of natural and synthetic lignin-carbohydrate complexes (Hüttner et al 2017). Specifically, glucuronoyl esterases cleave ester linkages between the lignin and glucuronoxylan complexes (Arnling Bååth et al 2016).…”

Section: Commercial Significance Of Pectin and Lignin De-esterasesmentioning

confidence: 99%

Structural and functional properties of pectin and lignin–carbohydrate complexes de-esterases: a review

Kameshwar

Qin

2018

Bioresour. Bioprocess.

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Biological conversion of plant biomass into commercially valuable products is one of the highly studied subjects in the last two decades. Studies were continuously being conducted to understand and develop efficient enzymes for the breakdown and conversion of plant cell-wall components into valuable commercial products. Naturally, plant cell-wall components are differentially esterified to protect from the invading microorganisms. However, during the process of evolution, microorganisms have developed special set of enzymes to de-esterify the plant cell-wall components. Among the carbohydrate-active enzymes (CAZy), carbohydrate esterases stand first during the process of enzymatic conversion of plant biomass, as these enzymes de-esterify the plant biomass and make it accessible for the hydrolytic enzymes such as cellulases, hemicellulases, ligninolytic and pectinases. In this article, we have extensively discussed about the structural and functional properties of pectin methyl esterases, feruloyl, cinnamoyl and glucuronoyl esterases which are required for the de-esterification of pectin and lignin-carbohydrate complexes. Pectin esterases are classified among CE8, CE12, CE13 and CE15 carbohydrate esterase class of CAZy database. Whereas, lignin-carbohydrate complex de-esterifying enzymes are classified among CE1 (feruloyl esterase) and CE15 (glucuronoyl esterase) classes. Understanding the structural and functional abilities of pectin and lignin-carbohydrate esterases will significantly aid in developing efficient class of de-esterases for reducing the recalcitrant nature of plant biomass. These efficient de-esterases will have various applications including pretreatment of plant biomass, food, beverage, pulp and paper, textile, pharmaceutical and biofuel industries. which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Section: Commercial Significance Of Pectin and Lignin De-esterasesmentioning

confidence: 99%

Structural and functional properties of pectin and lignin–carbohydrate complexes de-esterases: a review

Kameshwar

Qin

2018

Bioresour. Bioprocess.

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“…xylanases-to reach their targets within the plant biomass. To date, all characterized GEs are either singledomain proteins, or are coupled with an N-terminal carbohydrate-binding module 1 (CBM1) domain [36]. This module is thought to allow the enzyme to bind easier to insoluble substrates, and thus increase the overall activity [37].…”

Section: Introductionmentioning

confidence: 99%

Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme from Caldicellulosiruptor kristjanssonii incorporating multiple carbohydrate-binding modules

Krska

Larsbrink

2020

Biotechnol Biofuels

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Background: Efficient degradation of lignocellulosic biomass has become a major bottleneck in industrial processes which attempt to use biomass as a carbon source for the production of biofuels and materials. To make the most effective use of the source material, both the hemicellulosic as well as cellulosic parts of the biomass should be targeted, and as such both hemicellulases and cellulases are important enzymes in biorefinery processes. Using thermostable versions of these enzymes can also prove beneficial in biomass degradation, as they can be expected to act faster than mesophilic enzymes and the process can also be improved by lower viscosities at higher temperatures, as well as prevent the introduction of microbial contamination. Results: This study presents the investigation of the thermostable, dual-function xylanase-glucuronoyl esterase enzyme CkXyn10C-GE15A from the hyperthermophilic bacterium Caldicellulosiruptor kristjanssonii. Biochemical characterization of the enzyme was performed, including assays for establishing the melting points for the different protein domains, activity assays for the two catalytic domains, as well as binding assays for the multiple carbohydratebinding domains present in CkXyn10C-GE15A. Although the enzyme domains are naturally linked together, when added separately to biomass, the expected boosting of the xylanase action was not seen. This lack of intramolecular synergy might suggest, together with previous data, that increased xylose release is not the main beneficial trait given by glucuronoyl esterases. Conclusions: Due to its thermostability, CkXyn10C-GE15A is a promising candidate for industrial processes, with both catalytic domains exhibiting melting temperatures over 70 °C. Of particular interest is the glucuronoyl esterase domain, as it represents the first studied thermostable enzyme displaying this activity.

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“…Glucuronoyl esterase (GE) is a recently defined carbohydrate esterase that has been isolated from several microorganisms [1][2][3][4][5][6]. GE has potential for production of biofuels and biomaterials in lignocellulose biorefineries [7][8][9][10][11][12]. GE cleaves alkali-labile bonds from the lignincarbohydrate complexes at acidic pH [12].…”

Section: Introductionmentioning

confidence: 99%

“…GE has potential for production of biofuels and biomaterials in lignocellulose biorefineries [7][8][9][10][11][12]. GE cleaves alkali-labile bonds from the lignincarbohydrate complexes at acidic pH [12]. Recent reports have proven that the removal of glucuronic acid branches from the hemicellulose significantly improved release of fermentable sugars for biofuels production [7,8,13].…”

Section: Introductionmentioning

confidence: 99%

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Scalable methanol-free production of recombinant glucuronoyl esterase in Pichia pastoris

Conacher

García-Aparicio

Coetzee

et al. 2019

Preprint

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Objective: Glucuronoyl esterase (GE) is an emerging enzyme that improves fractionation of lignin-carbohydrate complexes. However, the commercial availability of GE is limited, which hinders the research of GE-based bioprocesses for its industrial application in lignocellulose biorefineries. This study evaluated a workable, cost-effective, and commercially scalable production strategy to improve the ease of GE-based research. This strategy consisted of a constitutive and methanol-free enzyme production step coupled with a two-step filtration process. The aim was to determine if this strategy can yield copious amounts of GE, by secretion into the extracellular medium with an acceptable purity that could allow its direct application. This approach was further validated for cellobiose dehydrogenase, another emerging lignocellulose degrading enzyme which is scarcely available at high cost. Results: The secreted recombinant enzymes were functionally produced in excess of levels previously reported for constitutive production (1489-2780 mg.L -1 ), and were secreted at moderate to high percentages of the total extracellular protein (51-94 %). The constant glycerol feed, implemented during fed-batch fermentation, lead to a decline in growth rate and plateaued productivity. Tangential flow ultrafiltration was used to concentrate cell-free enzyme extracts 5-6-fold, reaching enzyme activity levels (1020-202 U.L -1 ) that could allow their direct application.

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Characterisation of three fungal glucuronoyl esterases on glucuronic acid ester model compounds

Cited by 29 publications

References 45 publications

Structural and functional properties of pectin and lignin–carbohydrate complexes de-esterases: a review

Structural and functional properties of pectin and lignin–carbohydrate complexes de-esterases: a review

Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme from Caldicellulosiruptor kristjanssonii incorporating multiple carbohydrate-binding modules

Scalable methanol-free production of recombinant glucuronoyl esterase in Pichia pastoris

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