Production of structurally diverse wheat arabinoxylan hydrolyzates using combinations of xylanase and arabinofuranosidase

Mendis, Mihiri; Şimşek, Şenay

doi:10.1016/j.carbpol.2015.05.083

Cited by 46 publications

(30 citation statements)

References 18 publications

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“…Xylanase is a series of endogenous enzymes that is present in wheat malt, including endo-1,4-β-xylanase, arabinofuranosidase, β-D-xylosidase, feruloyl esterase, and so on; among these, endo-1,4-β-xylanase is the key enzyme for the degradation of AX, which breaks the β-(1,4)-glycosidic bond between xyloses (Xyls) [8], reduces the polymerization degree of AX, and changes the quantity and distribution of the arabinose (Ara) residues, which further alters the physical and chemical properties of AX dramatically.…”

Section: Introductionmentioning

confidence: 99%

Purification, Identification, and Characterization of an Endo-1,4-β-Xylanase from Wheat Malt

Peng

Jin

2020

Molecules

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In this study, an endo-1,4-β-xylanase was purified from wheat malt following the procedures of ammonium sulfate precipitation, cation-exchange chromatography, and two-step anion-exchange chromatography. The purified endo-1,4-β-xylanase had a specific activity of 3.94 u/mg, demonstrating a weight average molecular weight (Mw) of approximately 58,000 Da. After LC–MS/MS (Liquid chromatography-tandem mass spectrometry) identification, the purified enzyme had the highest matching degree with a GH10 (Glycoside Hydrolase 10) domain-containing protein from wheat, there were 23 match peptides with a score above the threshold and the prot-cover was 45.5%. The resulting purified enzyme was used to investigate its degradation ability on high viscosity wheat-derived water-extractable arabinoxylan (WEAX). Degradation experiments confirmed that the purified enzyme was a true endo-acting enzyme, which could degrade large WEAX into smaller WEAX. The average degree of polymerization (avDP) and the viscosity of WEAX decreased with the increasing reaction time. The enzyme could degrade a small amount of WEAX into arabinoxylan-oligosaccharides (AXOS) with a degree of polymerization of 2–6, but no monosaccharide was produced. The degradation occurred rapidly in the first 3.5 h and decreased with the further prolongation of reaction time.

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Section: Introductionmentioning

confidence: 99%

Purification, Identification, and Characterization of an Endo-1,4-β-Xylanase from Wheat Malt

Peng

Jin

2020

Molecules

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“…The enzyme production was carried out at different pH (4-6) when incubated at a different temp. (25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40) C) for 24-120 h at 50 ¡150 rpm based on the Central Composite Design (CCD) of RSM (Table 4 and Table 1). An aliquot of fermentation broth was withdrawn from the flask after a regular interval and centrifuged at 4 C at 7000 rpm for 15 min.…”

Section: Growth Conditions and Enzyme Production Set Upmentioning

confidence: 99%

“…The carboxymethyl cellulase and xylanase activities of crude enzyme were estimated by measuring the reducing sugars through DNS method 33,34 The laccase activity was determined spectrophotometrically with ABTS [2,2-azinobis (3-ethylbenzathiazoline-6-sulfonic acid) as a substrate. 35 One unit of CMCase activity was defined as an amount of enzyme that releases one micromole of glucose per minute under standard reaction conditions.…”

Section: Lignocellulolytic Enzyme Assaysmentioning

confidence: 99%

Bioprocessing of wheat bran for the production of lignocellulolytic enzyme cocktail byCotylidia pannosaunder submerged conditions

2016

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Characterization and production of efficient lignocellulytic enzyme cocktails for biomass conversion is the need for biofuel industry. The present investigation reports the modeling and optimization studies of lignocellulolytic enzyme cocktail production by Cotylidia pannosa under submerged conditions. The predominant enzyme activities of cellulase, xylanase and laccase were produced in the cocktail through submerged conditions using wheat bran as a substrate. A central composite design approach was utilized to model the production process using temperature, pH, incubation time and agitation as input variables with the goal of optimizing the output variables namely cellulase, xylanase and laccase activities. The effect of individual, square and interaction terms on cellulase, xylanase and laccase activities were depicted through the non-linear regression equations with significant R 2 and P-values. An optimized value of 20 U/ml, 17 U/ml and 13 U/ml of cellulase, xylanase and laccase activities, respectively, were obtained with a media pH of 5.0 in 77 h at 31C, 140 rpm using wheatbran as a substrate. Overall, the present study introduces a fungal strain, capable of producing lignocellulolytic enzyme cocktail for subsequent applications in biofuel industry.

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“…Galactose was previously detected in hemicellulose fractions from cereals as GAX side chain terminal units (Hromádková et al . ; Mendis & Simsek ; Coelho et al . ).…”

Section: Discussionmentioning

confidence: 99%

Changes in apoplastic peroxidase activity and cell wall composition are associated with cold‐induced morpho‐anatomical plasticity of wheat leaves

Lorenzo¹,

Pinedo

Equiza

et al. 2018

Plant Biol J

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Temperate grasses, such as wheat, become compact plants with small thick leaves after exposure to low temperature. These responses are associated with cold hardiness, but their underlying mechanisms remain largely unknown. Here we analyse the effects of low temperature on leaf morpho-anatomical structure, cell wall composition and activity of extracellular peroxidases, which play key roles in cell elongation and cell wall thickening, in two wheat cultivars with contrasting cold-hardening ability. A combined microscopy and biochemical approach was applied to study actively growing leaves of winter (ProINTA-Pincén) and spring (Buck-Patacón) wheat developed under constant warm (25 °C) or cool (5 °C) temperature. Cold-grown plants had shorter leaves but longer inter-stomatal epidermal cells than warm-grown plants. They had thicker walls in metaxylem vessels and mestome sheath cells, paralleled with accumulation of wall components, predominantly hemicellulose. These effects were more pronounced in the winter cultivar (Pincén). Cold also induced a sharp decrease in apoplastic peroxidase activity within the leaf elongating zone of Pincén, and a three-fold increase in the distal mature zone of the leaf. This was consistent with the enhanced cell length and thicker cell walls in this cultivar at 5 °C. The different response to low temperature of apoplastic peroxidase activity and hemicellulose between leaf zones and cultivar types suggests they might play a central role in the development of cold-induced compact morphology and cold hardening. New insights are presented on the potential temperature-driven role of peroxidases and hemicellulose in cell wall dynamics of grasses.

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Production of structurally diverse wheat arabinoxylan hydrolyzates using combinations of xylanase and arabinofuranosidase

Cited by 46 publications

References 18 publications

Purification, Identification, and Characterization of an Endo-1,4-β-Xylanase from Wheat Malt

Purification, Identification, and Characterization of an Endo-1,4-β-Xylanase from Wheat Malt

Bioprocessing of wheat bran for the production of lignocellulolytic enzyme cocktail byCotylidia pannosaunder submerged conditions

Changes in apoplastic peroxidase activity and cell wall composition are associated with cold‐induced morpho‐anatomical plasticity of wheat leaves

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