Skip to Content
Merck
All Photos(1)

Documents

M9400

Sigma-Aldrich

β-Mannosidase from Helix pomatia

5-30 units/mL, ammonium sulfate suspension, crude extract

Synonym(s):

β-D-Mannoside mannohydrolase

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

form

ammonium sulfate suspension

quality

crude extract

mol wt

94 kDa

concentration

5-30 units/mL

foreign activity

β-N-acetylglucosaminidase and α-mannosidase <1.0%

storage temp.

2-8°C

Looking for similar products? Visit Product Comparison Guide

General description

β-Mannosidase is a lysosomal enzyme that belongs to the glycosyl hydrolase family 2.

Application

β-Mannosidase from Helix pomatia has been used:
  • in the digestion of glycans for enzymatic analysis
  • in the treatment of labeled monogalactosyl Manno-oligosaccharides
  • in non-mammalian glycosidase inhibition assays

Biochem/physiol Actions

β-Mannosidase participates in cleaving the β(1–4)-linked mannose located at the nonreducing end of N-glycosylated proteins. It is involved in the polysaccharide degradation pathway. In humans, mutations in the gene are associated with β-mannosidosis, a lysosomal storage disease. Low levels of β-Mannosidase due to mutations also lead to nystagmus, an eye disorder associated with involuntary eye movements.

Unit Definition

One unit will hydrolyze 1 μmole of p-nitrophenyl-β-D-mannopyranoside to p-nitrophenol and D-mannopyranoside per min at pH 4.0 at 25°C.

Physical form

Suspension in 3.0 M (NH4)2SO4 containing 10 mM sodium acetate, pH approx. 4.0

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

María del Carmen Rodríguez-Gacio et al.
Journal of experimental botany, 63(11), 3976-3988 (2012-05-04)
The softening and degradation of the cell wall (CW), often mannan enriched, is involved in several processes during development of higher plants, such as meristematic growth, fruit ripening, programmed cell death, and endosperm rupture upon germination. Mannans are also the
Yuya Kumagai et al.
Biochimie, 94(12), 2783-2790 (2012-09-27)
Mannanase is an important enzyme involved in the degradation of mannan, production of bioactive oligosaccharides, and biobleaching of kraft pulp. Mannanase must be thermostable for use in industrial applications. In a previous study, we found that the thermal stability of
Guojie Jin et al.
Bioresource technology, 111, 378-382 (2012-03-01)
Lipids produced by oleaginous microorganisms are a potential feedstock for biodiesel production and chemical synthesis. Yet, the costs of microbial lipids remain high, partially because the lipid recovery process is tedious and costly. In the present study, enzyme-assisted extraction of
Jia Zheng et al.
Bioresource technology, 118, 257-264 (2012-06-19)
An industrial medium, Corn Steep Liquor Powder Dextrose (CSD medium) was developed for constitutive expression of recombinant β-mananase by Pichia pastoris. The β-mananase activity (513 U/mL) with CSD medium was 1.64- and 2.5-fold higher than with YPD and BSM in
A P Félix et al.
Journal of animal science, 90(9), 3060-3067 (2012-05-16)
This experiment aimed at evaluating the effects of including the enzyme, β-mannanase, in dog (Canis lupus familiaris) diets based on either poultry (Gallus gallus domesticus) by-product meal (PBM) or soybean [Glycine max (L.) Merr.] Meal (SBM). The second objective was

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service