Oligosaccharide distribution in Brazilian soya bean cultivars

Trugo, L.C.; Farah, Adriana; Cabral, Lair C.

doi:10.1016/0308-8146(95)93286-z

Cited by 36 publications

(25 citation statements)

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“…Concluding Remarks-In conclusion, sucrose and raffinose are the most abundant soluble carbohydrates found in plants (9), and they are probably part of the human carbohydrate energy intake. Although sucrose from diet is the substrate of the human intestinal sucrase-isomaltase, raffinose is degraded into galactose and sucrose only by intestinal microbial enzymes.…”

Section: Volume 286 • Number 47 • November 25 2011mentioning

confidence: 89%

“…For example, they represent from 39 to 53 g/kg in soybean meals (9). They consist of galactose units ␣- (1,6) linked to a mannopyranose backbone (galactomannans) or ␣-(1,6) linked to glucose (melibiose) or sucrose (raffinose) or raffinose (stachyose), with sucrose and raffinose being the most abundant soluble carbohydrates found in plant cell walls (9). However, there exists no ␣-(1,6)-galactosidase activity in the human intestine mucosa, and ␣-galactosides are exclusively fermented by microbial ␣-(1,6)-galactosidases (EC 3.2.1.22).…”

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confidence: 99%

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α-Galactosidase/Sucrose Kinase (AgaSK), a Novel Bifunctional Enzyme from the Human Microbiome Coupling Galactosidase and Kinase Activities

Bruel

Sulzenbacher

Tison³

et al. 2011

Journal of Biological Chemistry

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Background:Raffinose, an abundant carbohydrate in plants, is degraded into galactose and sucrose by intestinal microbial enzymes. Results: AgaSK is a protein coupling galactosidase and sucrose kinase activity. The structure of the galactosidase domain sheds light onto substrate recognition. Conclusion: AgaSK produces sucrose-6-phosphate directly from raffinose. Significance: Production of sucrose-6-phosphate directly from raffinose points toward a novel glycolytic pathway in bacteria.

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Section: Volume 286 • Number 47 • November 25 2011mentioning

confidence: 89%

mentioning

confidence: 99%

α-Galactosidase/Sucrose Kinase (AgaSK), a Novel Bifunctional Enzyme from the Human Microbiome Coupling Galactosidase and Kinase Activities

Bruel

Sulzenbacher

Tison³

et al. 2011

Journal of Biological Chemistry

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“…Soybean meal contains up to 22.7% non starch polysaccharides (NSPs) on a dry matter basis (Chesson, 1987). This includes about 6% oligosaccharides, including 1.0% raffinose and 4.6% stachyose (Trugo et al, 1995). These oligosaccharides cannot be digested in the small intestine of poultry because of the absence of endogenous -(1,6)-galactosidase enzyme (Gitzelman and Auricchio, 1965).…”

Section: The Use Of Exogenous Enzymes To Increase the Nutritional Valmentioning

confidence: 99%

Using Exogenous Enzymes to Increase the Nutritional Value of Soybean Meal in Poultry Diet

Ao¹

2011

Soybean and Nutrition

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“…The mechanism of sugar escape remains unknown but may involve downhill leakage via permease which transports precursor saccharides or novel sugar export proteins. If sugar escape occurs in nature with wild organisms, it could facilitate the development of complex bacterial communities which are based on the sequence of saccharide catabolism and the hierarchy of sugar utilization.is second only to sucrose as a soluble component in plant tissues (10,18,31) and beet molasses (19). Many members of the family Enterobacteriaceae can degrade this sugar (6).…”

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confidence: 99%

Extracellular melibiose and fructose are intermediates in raffinose catabolism during fermentation to ethanol by engineered enteric bacteria

et al. 1997

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Contrary to general concepts of bacterial saccharide metabolism, melibiose (25 to 32 g/liter) and fructose (5 to 14 g/liter) accumulated as extracellular intermediates during the catabolism of raffinose (O-␣-D-galactopyranosyl-1,6-␣-D-glucopyranosyl-␤-D-fructofuranoside) (90 g/liter) by ethanologenic recombinants of Escherichia coli B, Klebsiella oxytoca M5A1, and Erwinia chrysanthemi EC16. Both hydrolysis products (melibiose and fructose) were subsequently transported and further metabolized by all three organisms. Raffinose catabolism was initiated by ␤-fructosidase; melibiose was subsequently hydrolyzed to galactose and glucose by ␣-galactosidase. Glucose and fructose were completely metabolized by all three organisms, but galactose accumulated in the fermentation broth with EC16(pLOI555) and P2. MM2 (a raffinose-positive E. coli mutant) was the most effective biocatalyst for ethanol production (38 g/liter) from raffinose. All organisms rapidly fermented sucrose (90 g/liter) to ethanol (48 g/liter) at more than 90% of the theoretical yield. During sucrose catabolism, both hydrolysis products (glucose and fructose) were metabolized concurrently by EC16(pLOI555) and P2 without sugar leakage. However, fructose accumulated extracellularly (27 to 28 g/liter) at early stages of fermentation with KO11 and MM2. Sequential utilization of glucose and fructose correlated with a diauxie in base utilization (pH maintenance). The mechanism of sugar escape remains unknown but may involve downhill leakage via permease which transports precursor saccharides or novel sugar export proteins. If sugar escape occurs in nature with wild organisms, it could facilitate the development of complex bacterial communities which are based on the sequence of saccharide catabolism and the hierarchy of sugar utilization.is second only to sucrose as a soluble component in plant tissues (10,18,31) and beet molasses (19). Many members of the family Enterobacteriaceae can degrade this sugar (6). In a comparison of more than 300 Escherichia coli isolates from humans and farm animals (25, 30), half were able to metabolize raffinose and 15% were able to transfer this trait by conjugation. Subsequent studies established the presence of conjugal plasmids containing genes for raffinose utilization (7). One of these plasmids, pRSD2, has been investigated in considerable detail (2,3,28,29) and forms the basis for current models of raffinose utilization (21). Raffinose genes are organized into an operon (2, 3); rafR (regulatory protein), rafA (␣-galactosidase), rafB (raffinose permease), and rafD (sucrose hydrolase). According to the current model (2, 3, 28), intracellular raffinose is initially hydrolyzed by ␣-galactosidase into galactose and sucrose. Intracellular sucrose is subsequently cleaved into glucose and fructose by sucrose hydrolase.The rafA-encoded ␣-galactosidase is quite different from the native E. coli enzyme and has been used as a serological marker to compare 39 independently isolated raf plasmids (28). The cross-reactivity of ␣-galactos...

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Oligosaccharide distribution in Brazilian soya bean cultivars

Cited by 36 publications

References 5 publications

α-Galactosidase/Sucrose Kinase (AgaSK), a Novel Bifunctional Enzyme from the Human Microbiome Coupling Galactosidase and Kinase Activities

α-Galactosidase/Sucrose Kinase (AgaSK), a Novel Bifunctional Enzyme from the Human Microbiome Coupling Galactosidase and Kinase Activities

Using Exogenous Enzymes to Increase the Nutritional Value of Soybean Meal in Poultry Diet

Extracellular melibiose and fructose are intermediates in raffinose catabolism during fermentation to ethanol by engineered enteric bacteria

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