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商品編號


E-BGLAEC



品牌


Megazyme



公司


Megazyme



公司分類(lèi)


Enzymes



Size

500,000 Units

商品信息

High purity recombinant β-Glucuronidase (
Escherichia coli
) for use in research, biochemical enzyme assays and
in vitro
diagnostic analysis.

EC 3.2.1.31
CAZy Family: GH2

Recombinant
. From
Escherichia coli
. Supplied in solution (Tris.HCl / NaCl / EDTA).
Hydrolysis of non-reducing terminal β-D-glucuronic acid residues from glycoproteins and oligosaccharides of glycoconjugates.
Supplied at ~ 250 kU/mL.?

Specific activity:

~ 35,000 U/mg (37
o
C, pH 6.8 on phenolphthalein-β-D-glucuronide);
~ 100 U/mg (37
o
C, pH 7.5 on
p
NP-β-D-glucuronide).

Store
at 4
o
C.
Do Not Freeze/Thaw
?

Custom quantities and formulations available up on request.?



Effect of heat-moisture treatment on multi-scale structures and physicochemical properties of breadfruit starch.

Tan, X., Li, X., Chen, L., Xie, F., Li, L. & Huang, J. (2017).
Carbohydrate Polymers
, 161, 286-294.


Link to Article

Read Abstract

Breadfruit starch was subjected to heat-moisture treatment (HMT) at different moisture content (MC). HMT did not apparently change the starch granule morphology but decreased the molecular weight and increased the amylose content. With increased MC, HMT transformed the crystalline structure (B → A + B → A) and decreased the relative crystallinity. With ≥25% MC, the scattering peak at ca. 0.6 nm
?1
disappeared, suggesting the lamellar structure was damaged. Compared with native starch, HMT-modified samples showed greater
Thermo
st
ABI
lity. Increased MC contributed to a higher pasting temperature, lower viscosity, and no breakdown. The pasting temperature of native and HMT samples ranged from 68.8 to 86.2&?deg;C. HMT increased the slowly-digest
IBL
e starch (SDS) and resistant starch (RS) contents. The SDS content was 13.24% with 35% MC, which was 10.25% higher than that of native starch. The increased enzyme resistance could be ascribed to the rearrangement of molecular chains and more compact granule structure.