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Merck

S7776

Starch Azure

Insoluble corn starch covalently linked with Remazol Brilliant Blue R

Synonym(s):

Starch–Remazol brilliant blue R, RBB-Starch, Remazol brilliant blue R dyed starch, Starch Azure

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.28
MDL number:
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Product Name

Starch Azure, Insoluble corn starch covalently linked with Remazol Brilliant Blue R

form

powder

Quality Level

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Application

Starch Azure has been used as a substrate
  • in the screening of α-amylase activity in decontaminated malted flour at varying pH and temperature
  • for monitoring the inhibitory activity of Physalis peruviana extracts
  • for thermostable α-amylase extracted from deep sea and acidic soil

General description

Starch is an insoluble starch substrate specific for α-amylase and not for other exo enzymes. α-amylase catalysis of starch azure solubilization is measured at 595 nm.
Substrate for colorimetric determination of α-amylase.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Modeling cereal starch hydrolysis during simultaneous saccharification and lactic acid fermentation; case of a sorghum-based fermented beverage, gowe
Mestres C, et al.
Food Research International, 100, 102-111 (2017)
Inhibitory effects of an extract of fruits of Physalis peruviana on some intestinal carbohydrases
Rey D, et al.
Revista Colombiana de Ciencias Quimico-Farmaceuticas, 44(1), 72-89 (2015)
The use of starch azure for measurement of alpha-amylase activity
Lehoczki G, et al.
Carbohydrate Polymers, 183, 263-266 (2018)
Gábor Lehoczki et al.
Carbohydrate polymers, 183, 263-266 (2018-01-22)
Despite being widely used, there is no standard protocol for α-amylase activity measurement with starch azure substrate. Boiling pre-treatment of starch azure suspension increased the reaction rate of hydrolysis catalysed by human salivary α-amylase (HSA) or porcine pancreatic α-amylase (PPA)
A novel, high performance enzyme for starch liquefaction discovery and optimization of a low pH, thermostable alpha-amylase
Richardson TH, et al.
The Journal of Biological Chemistry, 277(29), 26501-26507 (2002)

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