endo-1,4 β-Mannanase (Bacillus sp.) 

High purity endo-1,4 β-Mannanase (Bacillus sp.) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

EC 3.2.1.78
CAZy Family: GH26
CAS:  37288-54-3

mannan endo-1,4-beta-mannosidase; 4-beta-D-mannan mannanohydrolase

Highly purified. From Bacillus sp. Electrophoretically homogeneous.
In 3.2 M ammonium sulphate.
Supplied at ~ 1,200 U/mL. 

Specific activity:
> 50 U/mg (40oC, pH 8.8 on carob galactomannan).

Stability: > 4 years at 4oC.

Product Code
Content/size
Stock
Price
Qty
E-BMABS
2,000 Units
$182.00

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DESCRIPTION

endo-1,4 β-Mannanase (Bacillus sp.)

EC 3.2.1.78
CAZy Family: GH26
CAS:  37288-54-3

Synonyms:
mannan endo-1,4-beta-mannosidase; 4-beta-D-mannan mannanohydrolase

Form:
In 3.2 M ammonium sulphate.

Stability: 
> 4 years at 4oC.

Specific activity:
> 50 U/mg (40oC, pH 8.8 on carob galactomannan).

Unit definition:
One Unit of β-mannanase activity is the amount of enzyme which releases one µmole of mannose-reducing-sugar equivalents per minute from low viscosity carob galactomannan (10 mg/mL) in glycine buffer (100 mM), pH 8.8 at 40oC.

Specificity:
Random hydrolysis of (1,4)-β-D-mannosidic linkages in mannans, galactomannans and glucomannans.

Applications:
Applications established in diagnostics and research within the food and feed, carbohydrate, biofuels and paper production industries.

Galactomannan structure and β-mannanase and β-mannosidase activity in germinating legume seeds.

McCleary, B. V. & Matheson, N. K. (1975). Phytochemistry, 14(5-6), 1187-1194.

Galactomannans and a galactoglucomannan in legume seed endosperms: Structural requirements for β-mannanase hydrolysis.

McCleary, B. V., Matheson, N. K. & Small, D. B. (1976). Phytochemistry, 15(7), 1111-1117.

Modes of action of β-mannanase enzymes of diverse origin on legume seed galactomannans.

McCleary, B. V. (1979). Phytochemistry, 18(5), 757-763.

An enzymic technique for the quantitation of galactomannan in guar Seeds.

McCleary, B. V. (1981). Lebensmittel-Wissenschaft & Technologie, 14, 56-59.

Purification and properties of a β-D-mannoside mannohydrolase from guar.

McCleary, B. V. (1982), Carbohydrate Research, 101(1), 75-92.

Preparative–scale isolation and characterisation of 61-α-D-galactosyl-(1→4)-β-D-mannobiose and 62-α-D-galactosyl-(1→4)-β-D-mannobiose.

McCleary, B. V., Taravel, F. R. & Cheetham, N. W. H. (1982). Carbohydrate Research, 104(2), 285-297.

β-D-mannosidase from Helix pomatia.

McCleary, B. V. (1983). Carbohydrate Research, 111(2), 297-310.

Enzymic interactions in the hydrolysis of galactomannan in germinating guar: The role of exo-β-mannanase.

McCleary, B. V. (1983). Phytochemistry, 22(3), 649-658.

Characterisation of the oligosaccharides produced on hydrolysis of galactomannan with β-D-mannase.

McCleary, B. V., Nurthen, E., Taravel, F. R. & Joseleau, J. P. (1983). Carbohydrate Research, 118, 91-109.

Action patterns and substrate-binding requirements of β-D-mannanase with mannosaccharides and mannan-type polysaccharides.

McCleary, B. V. & Matheson, N. K. (1983). Carbohydrate Research, 119, 191-219.

The fine structures of carob and guar galactomannans.

McCleary, B. V., Clark, A. H., Dea, I. C. M. & Rees, D. A. (1985). Carbohydrate Research, 139, 237-260.

Effect of galactose-substitution-patterns on the interaction properties of galactomannas.

Dea, I. C. M., Clark, A. H. & McCleary, B. V. (1986). Carbohydrate Research, 147(2), 275-294.

Effect of the molecular fine structure of galactomannans on their interaction properties - the role of unsubstituted sides.

Dea, I. C. M., Clark, A. H. & McCleary, B. V. (1986). Food Hydrocolloids, 1(2), 129-140.

Galactomannan changes in developing Gleditsia Triacanthos Seeds.

McCleary, B. V., Mallett, I. & Matheson, N. K. (1987). Phytochemistry, 26(7), 1889-1894.

Measurement of cereal α-Amylase: A new assay procedure.

McCleary, B. V. & Sheehan, H. (1987). Journal of Cereal Science, 6(3), 237-251.

Measurement of α-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the ceralpha assay: Collaborative study.

McCleary, B. V., McNally, M., Monaghan, D. & Mugford, D. C. (2002). Journal of AOAC International, 85(5), 1096-1102.

Partially hydrolyzed guar gum characterization and sensitive quantification in food matrices by high performance anion exchange chromatography with pulsed amperometric detection—Validation using accuracy profile.

Mercier, G. & Campargue, C. (2012). Journal of Chromatography A, 1262, 180-187.

Functional genomic analysis supports conservation of function among cellulose synthase-like A gene family members and suggests diverse roles of mannans in plants.

Liepman, A. H., Nairn, C. J., Willats, W. G. T., Sørensen, I., Roberts, A. W. & Keegstra, K. (2007). Plant Physiology, 143(4), 1881-1893.

The water-soluble non-starch polysaccharides from bananas display immunomodulatory properties on cultured macrophages.

Sansone, M., Sansone, A. C. M. B., Shiga, T. M. & do Nascimento, J. R. O. (2016). Food Research International, 87, 125-133.