Purification and detection of linamarin from cassava root cortex by high performance liquid chromatography

Sornyotha, Somphit; Kyu, Khin Lay

doi:10.1016/j.foodchem.2006.10.071

Cited by 35 publications

(20 citation statements)

References 17 publications

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“…The hydrolysis products were determined by thin-layer chromatography (TLC) on silica gel 60 F245 plates (catalog no. 1.05554, 20 by 20 cm; Merck) with a mixture of n-butanol, acetic acid, and water (2:1:1) as a solvent system (29). The sugar spots were detected by heating the plates to 100°C after spraying them with a reagent consisting of 4 g of ␣-diphenylamine, 4 ml of aniline, 200 ml of acetone, and 30 ml of 80% phosphoric acid.…”

Section: Methodsmentioning

confidence: 99%

Novel Trifunctional Xylanolytic Enzyme Axy43A from Paenibacillus curdlanolyticus Strain B-6 Exhibiting Endo-Xylanase, β- d -Xylosidase, and Arabinoxylan Arabinofuranohydrolase Activities

Teeravivattanakit

Baramee

Phitsuwan

et al. 2016

Appl Environ Microbiol

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The axy43A gene encoding the intracellular trifunctional xylanolytic enzyme from Paenibacillus curdlanolyticus B-6 was cloned and expressed in Escherichia coli. Recombinant PcAxy43A consisting of a glycoside hydrolase family 43 and a family 6 carbohydrate-binding module exhibited endo-xylanase, ␤-xylosidase, and arabinoxylan arabinofuranohydrolase activities. PcAxy43A hydrolyzed xylohexaose and birch wood xylan to release a series of xylooligosaccharides, indicating that PcAxy43A contained endo-xylanase activity. PcAxy43A exhibited ␤-xylosidase activity toward a chromogenic substrate, p-nitrophenyl-␤-D-xylopyranoside, and xylobiose, while it preferred to hydrolyze long-chain xylooligosaccharides rather than xylobiose. In addition, surprisingly, PcAxy43A showed arabinoxylan arabinofuranohydrolase activity; that is, it released arabinose from both singly and doubly arabinosylated xylose,Moreover, the combination of PcAxy43A and P. curdlanolyticus B-6 endo-xylanase Xyn10C greatly improved the efficiency of xylose and arabinose production from the highly substituted rye arabinoxylan, suggesting that these two enzymes function synergistically to depolymerize arabinoxylan. Therefore, PcAxy43A has the potential for the saccharification of arabinoxylan into simple sugars for many applications. IMPORTANCEIn this study, the glycoside hydrolase 43 (GH43) intracellular multifunctional endo-xylanase, ␤-xylosidase, and arabinoxylan arabinofuranohydrolase (AXH) from P. curdlanolyticus B-6 were characterized. Interestingly, PcAxy43A AXH showed a new property that acted on both the C(O)-2 and C(O)-3 positions of xylose residues doubly substituted with arabinosyl, which usually obstruct the action of xylanolytic enzymes. Furthermore, the studies here show interesting properties for the processing of xylans from cereal grains, particularly rye arabinoxylan, and show a novel relationship between PcAxy43A and endo-xylanase Xyn10C from strain B-6, providing novel metabolic potential for processing arabinoxylans into xylose and arabinose.

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Section: Methodsmentioning

confidence: 99%

Novel Trifunctional Xylanolytic Enzyme Axy43A from Paenibacillus curdlanolyticus Strain B-6 Exhibiting Endo-Xylanase, β- d -Xylosidase, and Arabinoxylan Arabinofuranohydrolase Activities

Teeravivattanakit

Baramee

Phitsuwan

et al. 2016

Appl Environ Microbiol

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“…Rye flour arabinoxylan (1%) in 50 mM SPB pH 7.0 was hydrolysed by 0.1 U of xylanase Xyn10C from P. curdlanolyticus strain B-6 (Imjongjairak et al in press) at 50 °C for 16 h. The hydrolysis products were separated by thin layer chromatography (TLC) as described by Sornyotha et al (2007). The A-X-A was cut out from the TLC plate at the same position as the standard A-X-A that had been prepared in the laboratory as described by Imjongjairak et al (in press); it was verified by electrospray ionization mass spectrometry and enzymatic analysis using Bacillus licheniformis α-L-arabinofuranosidase Axh43A (Sakka et al 2012), suspended in deionised water, and then sonicated.…”

Section: Preparation Of A-x-amentioning

confidence: 99%

Multifunctional Properties of Glycoside Hydrolase Family 43 from Paenibacillus curdlanolyticus Strain B-6 Including Exo-β-xylosidase, Endo-xylanase, and α-L-Arabinofuranosidase Activities

Wongratpanya¹,

Imjongjairak²,

Waeonukul³

et al. 2015

BioResources

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“…The bitter taste of fresh cassava roots is associated with high levels (>90%) of cyanogenic glycosides, mainly linamarin. 5,6 Cytotoxicity effects of pure linamarin as well as aqueous and methanol extract of cas- sava linamarin on Caov3, MCF-7, HT-29, and HL-60 cells had proved to have a bright future as an alternative anticancer. 7,8 This anticancer activity of linamarin is attributed to the release of hydrogen cyanide (CN) upon hydrolysis of linamarin.…”

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confidence: 99%

Optimizing the Process Parameters for Encapsulation of Linamarin into PLGA Nanoparticles Using Double Emulsion Solvent Evaporation Technique

2012

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Linamarin-loaded poly(lactide-co-glycolide) (PLGA) nanoparticles were prepared by using a double emulsion solvent evaporation method using polyvinyl alcohol as a surfactant. A two-factor full factorial design, Box-Behnken design and surface response methodology, were employed to improve the nanoparticle yield, particle size, and drug encapsulation efficiency OPTIMIZING ENCAPSULATION OF LINAMARIN PLGA NANOPARTICLESby determining the optimum levels of the process parameters, namely the polymer concentration, surfactant concentration, and homogenization speed. Both linear and quadratic empirical models were developed to express each response parameter as a function of the studied factors. A total of 12 and 17 experimental runs were necessary to obtain adequate empirical models ( p < 0.05) for both factorial and Box-Behnken designs, respectively. The final optimum values for the polymer concentration, surfactant concentration, and homogenization speed were determined at 9.8 mg/mL, 50 mg/mL, and 23,000 rpm, respectively. Formulations obtained at this optimum preparing condition resulted on average 96% yield, 61.2% drug encapsulation efficiency, and 144.6 nm particle size. However, all prepared nanoparticles showed some kind of controlled drug release; most likely the final optimized nanoparticles exhibited the most biphasic controlled drug release profile with a minimal burst release and overall drug release of <30% in 120 h of incubation. C

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Purification and detection of linamarin from cassava root cortex by high performance liquid chromatography

Cited by 35 publications

References 17 publications

Novel Trifunctional Xylanolytic Enzyme Axy43A from Paenibacillus curdlanolyticus Strain B-6 Exhibiting Endo-Xylanase, β- d -Xylosidase, and Arabinoxylan Arabinofuranohydrolase Activities

Novel Trifunctional Xylanolytic Enzyme Axy43A from Paenibacillus curdlanolyticus Strain B-6 Exhibiting Endo-Xylanase, β- d -Xylosidase, and Arabinoxylan Arabinofuranohydrolase Activities

Multifunctional Properties of Glycoside Hydrolase Family 43 from Paenibacillus curdlanolyticus Strain B-6 Including Exo-β-xylosidase, Endo-xylanase, and α-L-Arabinofuranosidase Activities

Optimizing the Process Parameters for Encapsulation of Linamarin into PLGA Nanoparticles Using Double Emulsion Solvent Evaporation Technique

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