Purification and structural characterisation of (1→3;1→6)-β--glucans (botryosphaerans) from grown on sucrose and fructose as carbon sources: a comparative study

Silva, Maria de Lourdes Corradi da; Izeli, Nataly Lino; Martinez, Paula Felippe; Silva, Iara R.; Constantino, Carlos J. L.; Cardoso, Marilsa S.; Barbosa, Aneli M.; Dekker, Robert F. H.; Silva, Gil Valdo José da

doi:10.1016/j.carbpol.2005.01.002

Cited by 42 publications

(15 citation statements)

References 43 publications

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“…The column was regenerated after 20 min with 100% eluent 2, followed by 15 min of 16 mM NaOH before addition of a new sample. Purified β‐glucosidase F 42 samples containing 2% carbohydrates were previously subjected to acid hydrolysis in a heater (Digi‐Block, Laboratory Devices Inc., Placerville, CA) at 120C for 2 h using trifluoroacetic acid (Merck KGaA, Darmstadt, Germany) and 4 M HCl to release the neutral and acidic monosaccharides (Corradi da Silva et al . 2005).…”

Section: Methodsmentioning

confidence: 99%

PURIFICATION AND CHARACTERIZATION OF SOY COTYLEDON Β-Glucosidase

Santos

Oliveira

Varéa

et al. 2012

Journal of Food Biochemistry

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β‐Glucosidase F42 of soy cotyledons was purified by ammonium sulfate fractionation, ion‐exchange chromatography (CM‐Sephadex‐C‐50, Sigma, St. Louis, MO) and gel filtration (Sephadex G‐100, Sigma). The enzyme was purified 111.8‐fold relative to its concentration in the crude extract. It had an apparent molecular mass of 53 kDa in gel filtration experiments and produced a 33‐kDa band in sodium dodecyl sulfate–polyacrylamide gel electrophoresis, suggesting that it is dimeric. The purified β‐glucosidase F42 was characterized as a glycoprotein after the identification of fucose, galactosamine and glucosamine by high‐pressure anion‐exchange chromatography–pulsed amperometric detector. Its highest activity was observed at pH 5.0 and 45C, and it was stable for up to 4 days at 25C. The Km of the enzyme was 0.12 mM p‐nitrophenyl‐β‐d‐glucopyranoside. β‐Glucosidase F42 showed specificity for different substrates, and its activity was inhibited by 1 mM HgCl2, 10 mM glucono‐δ‐lactone or 150 mM glucose and increased by 10 mM MnCl2. PRACTICAL APPLICATIONS β‐Glucosidase is an enzyme that hydrolyzes β‐glucosidic bonds to liberate glucose and hydrolyzes isoflavones to release aglycones. Soy aglycones have been broadly investigated because of their biological activity in the prevention and treatment of some chronic diseases. Soy β‐glucosidase can be used in the food industry to alter soy isoflavones for the production of functional foods that are rich in aglycone isoflavones. Therefore, it was an established method of purification of the enzyme that has great biotechnological potential.

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Section: Methodsmentioning

confidence: 99%

PURIFICATION AND CHARACTERIZATION OF SOY COTYLEDON Β-Glucosidase

Santos

Oliveira

Varéa

et al. 2012

Journal of Food Biochemistry

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“…Botryosphaeran was produced by B. rhodina MAMB-05 grown on nutrient medium containing fructose (EPS FRU ) as previously described [14,15].…”

Section: Production and Preparation Of Botryosphaeranmentioning

confidence: 99%

“…Studies on the biological activity of botryosphaeran (EPS GLU ) showed that it was not mutagenic, and exhibited strong anticlastogenic activity in mice at low doses [16]. The EPS produced by B. rhodina MAMB-05 on fructose (EPS FRU ) was reported to have a higher degree of branching (31%), and formed less viscous solutions in water compared to botryosphaeran produced on glucose and sucrose [15]. It is therefore of interest to examine the effect of derivatization of EPS FRU by sulfonation and its effect on anticoagulant activity.…”

Section: Introductionmentioning

confidence: 97%

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Sulfonation and anticoagulant activity of botryosphaeran from Botryosphaeria rhodina MAMB-05 grown on fructose

Mendes¹,

Santos²,

Barbosa³

et al. 2009

International Journal of Biological Macromolecules

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“…Botryosphaeria rhodina MAMB-05 grown on fructose presented a higher degree of branching (31 %) compared to that when grown on sucrose and glucose (21-22 %) as carbon sources. In each case, the degree of branching affected the physical properties (viz., rheology) of the botryosphaerans produced (Corradi da Silva et al, 2005). Botryosphaeran exists in solution in a triple helical conformation (Giese et al, 2008); an important property manifesting biological response modifying activity.…”

Section: Soybean Oil Emulsification To Enhance the Production Of The mentioning

confidence: 99%

Soybean Oil and Meal as Substrates for Lipase Production by Botryosphaeria ribis, and Soybean Oil to Enhance the Production of Botryosphaeran by Botryosphaeria rhodina

Barbosa¹,

Messias²,

Andrade³

et al. 2011

Soybean - Biochemistry, Chemistry and Physiology

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Purification and structural characterisation of (1→3;1→6)-β--glucans (botryosphaerans) from grown on sucrose and fructose as carbon sources: a comparative study

Cited by 42 publications

References 43 publications

PURIFICATION AND CHARACTERIZATION OF SOY COTYLEDON Β-Glucosidase

PURIFICATION AND CHARACTERIZATION OF SOY COTYLEDON Β-Glucosidase

Sulfonation and anticoagulant activity of botryosphaeran from Botryosphaeria rhodina MAMB-05 grown on fructose

Soybean Oil and Meal as Substrates for Lipase Production by Botryosphaeria ribis, and Soybean Oil to Enhance the Production of Botryosphaeran by Botryosphaeria rhodina

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