• Food Science and Biotechnology
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• v.14 no.6
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• pp.818-822
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• 2005

Beta-1,4-mannotriose was prepared by the enzymatic hydrolysis of poonac and the subsequent elimination with yeast of monosaccharides and disaccharide from the resultant hydrolysate. The enzyme system hydrolyzed poonac and produced monosaccharides, disaccharide and ${\beta}$-1,4-mannotriose without other oligomers at the final reaction stage. Poonac (50 g) was hydrolyzed at $50^{\circ}C$ and pH 6 for 48 hr with the crude enzyme solution (500 mL) from Trichoderma harzianum. The elimination of monosaccharides and disaccharide from the hydrolysis products with a yeast (Candida guilliermondii) produced 10.5 g of crystalline [${\beta}$-1,4-mannotriose without the use of chromatographic techniques. After 48 hr of yeast cultivation, the total sugar content fell from 4.8% to 3.4%, and the average degree of polymerization (D.P) rose from 2.5 to 3.2. The preparation method presented was confirmed to be suitable for the preparation of mannotriose from poonac.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.6
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• pp.1020-1025
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• 1995

A new method was developed to prepare ${\beta}-1$, 4-mannotriose by the enzymatic hydrolysis of white copra meal and the subsequent elimination of monosaccharides and mannobiose from the resulted hydrolysate with a yeast. The optimum pH and temperature for the mannanase were 6 and $50^{\circ}C$, respectively. The mannanase was stable between pH 5.5 and 7 after 2hr treatment at $30^{\circ}C$. White copra meal(70g) was hgydrolyzed with the mannanase(3,450units/500ml) at pH 6 and $50^{\circ}C$ for 24hr. The hydolysis products were monosaccharides, mannobiose and mannotriose. By the elimination of monosaccharides and mannobiose from the hydrolysis products with Candida guilliermondii IFO 0556, 12.1g of mannotriose was obtained without the use of chromatographic techiniques.

• Preventive Nutrition and Food Science
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• v.5 no.4
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• pp.179-183
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• 2000

$\beta$-1,4-Mannotriose was prepared b he enzymatic hydrolysis of white copra meal (WCM) and the subsequent elimination of monosaccharides from the resultant hydrolysate with a yeast. The enzyme system from sunflower seed hydrolyzed WCM and produced monosaccharides and $\beta$-1,4-mannotriose without other oligomers at the final stage of the reaction. WCM(50g) was hydrolyzed at 5$0^{\circ}C$ and pH 4.5 for 24 hr with crude enzyme solution (500 mL) from sunflower seed. By the elimination of monosaccharides from the hydrolysis products with a yeast (Candida glaebosa), 8.1 g of crystalline mannotriose was obtained without the use of chromatographic techniques. After 48hr of yeast cultivation, the total sugar content decreased from 4.6% to 3.5%, whereas the average degree of polymerization increased from 2.3 to 3.1.

• Journal of Applied Biological Chemistry
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• v.51 no.6
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• pp.292-295
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• 2008

Three kinds of oligosaccharides were obtained from the hydrolysate of brown copra meal galactomannan by a purified extracellular ${\beta}$-mannanase from Trichoderma sp. These oligosaccharides were identified as Man-Man, ${Gal^2}{Man_3}(6^2 mono-O-{\alpha}-D-galactopyranosyl-4-O-{\beta}-D-mannotriose)$, and ${Gal^2}{Man_6}(6^2-mono-O-{\alpha}-D-galactopyranosyl-4-O-{\beta}-D-mannohexaose)$, where Gal- and Man-represent ${\alpha}$-1,6-D-galactosidic and ${\beta}$-1,4-mannosidic linkages, respectively. The mode of action of ${\beta}$-mannanase on brown copra meal galactomannan is described on the basis of the structure of these oligosaccharides.

• Korean Journal of Microbiology
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• v.46 no.4
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• pp.397-400
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• 2010

The activities of mannanase, ${\beta}$-mannosidase, and ${\alpha}$-galactosidase were detected in culture filtrate of Paenibacillus woosongensis showing mannanolytic activity for locust bean gum. Optimal conditions occurred at pH 5.5 and $60^{\circ}C$ for mannanase toward locust bean gum, pH 6.5 and $50^{\circ}C$ for ${\beta}$-mannosidase toward para-nitrophenyl-${\beta}$-D-mannopyranoside, and pH 6.0-6.5 and $50^{\circ}C$ for ${\alpha}$-galactosidase toward para-nitrophenyl-${\alpha}$-D-galactopyranoside in the culture filtrate, respectively. The mannanolytic enzyme of culture filtrate hydrolyzed mannobiose as well as manno-oligosaccharides including mannotriose, mannotetraose, mannopentaose and mannohexaose. It could also hydrolyze ${\alpha}$-1,6 linked galacto-oligosaccharides such as melibiose, raffinose and stachyose to liberate galactose residue. From these results, it is assumed that P. woosongensis produces three enzymes required for the complete decomposition of galactomannan.

• Journal of Applied Biological Chemistry
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• v.51 no.6
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• pp.272-276
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• 2008

Purification and some properties of Xylogone sphaerospora ${\beta}$-mannanase were reprevious previous paper. Locust bean gum galactomannan was hydrolyzed by the purified ${\beta}$-mannanase, and then the hydrolysates was separated by activated carbon column chromatography. The main hydrolysates were composed of D.P. (Degree of Polymerization) 4 and 6 galactosyl mannooligosaccharides. For elucidate the structure of D.P 4 and 6 galactosyl mannooligosaccharides, sequential enzymatic action was performed. D.P 4 and 6 were identified as ${Gal^2}{Man_3}\;(6^2-mono-O-{\alpha}-D-galactopyranosyl-4-O-{\beta}-D-mannotriose)$ and ${Gal^2}{Man_5}\;(6^2-mono-O-{\alpha}-D-galacto- pyranosyl-4-O-{\beta}-D-mannopentaose)$. To investigate the effects of locust bean gum galactosyl mannooligosaccharides on in vitro growth of Bifidobacterium longum, B. bifidum, B. infantis, B. adolescentis, B. animalis, B. auglutum and B. breve. Bifidobacterium spp. were cultivated individually on the modified-MRS medium containing carbon source such as D.P. 4 and D.P. 6 galactosyl mannooligosaccharides, respectively. B. longum and B. bifidum grew up to-fold and 6.6-fold more effectively by the treatment of D.P. 6 galactosyl mannooligosaccharides, compared to those of standard MRS medium. Especially, D.P. 6 was more effective than D.P. 4 galactosyl mannooligosaccharide on the growth of Bifidobacterium spp.

• Microbiology and Biotechnology Letters
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• v.32 no.4
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• pp.347-351
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• 2004

Hydrolysis of manno-oligosaccharides and galactomannan was studied with the purified Bacillus subtilis WL-7 mannanase from recombinant Eschericoli. The predominant products of hydrolysis were mannose, mannobiose and mannotriose. The enzyme could hydrolyze $\beta$-1 A-linked manno-oligosaccharides larger than mannobiose, but was not active on mannobiose. When the mannanase hydrolyzed manno-oligo saccharides of degree of polymerization(DP) 4-6, it was more active on the substrate of higher DP. Based on analysis of transient reaction products by TLC, the enzyme was found to have a preference for internal $\beta$-IA-mannosidic linkages, which are the central mannosidic bond of mannotetraose and the two middle mannosidic bonds of mannopentaose. The $\beta$-l A-mannosidic bonds situated at the second and fourth positions from the nonreducing end of mannohexaose were preferenhydrolyzed by the mannanase. Locust bean gum(LBG) was enzymatically hydrolyzed with higher efficiency than guar gum, resulting that amount of reducing sugars was liberated more efficiently from LBG than guar gum with same activity of mannanase.