Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-796-2
NACRES:
NA.54
eCl@ss:
32160410
MDL number:
Product Name
Protease from Aspergillus saitoi, Type XIII, ≥0.6 unit/mg solid
biological source
Aspergillus sp. (Aspergillus saitoi)
type
Type XIII
form
solid
specific activity
≥0.6 unit/mg solid
foreign activity
alkaline protease, essentially free
storage temp.
−20°C
Quality Level
Related Categories
Application
Protease from Aspergillus saitoi has been used in a study to assess sequence coverage and resolution in hydrogen exchange of large proteins. It has also been used in a study to investigate the conversion of soybean curd isoflavone glycosides to their aglycones through β-glucosidase..
Biochem/physiol Actions
Protease from Aspergillus saitoi was shown to also function as a β-glucosidase.
Other Notes
One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 2.8 at 37 °C (color by Folin-Ciocalteu reagent).
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
E Ichishima
Bioscience, biotechnology, and biochemistry, 64(4), 675-688 (2000-06-01)
This review covers the unique catalytic and molecular properties of three proteolytic enzymes and a glycosidase from Aspergillus. An aspartic proteinase from A. saitoi, aspergillopepsin I (EC 3.4.23.18), favors hydrophobic amino acids at P1 and P'1 like gastric pepsin. However
Laetitia Cravello et al.
Rapid communications in mass spectrometry : RCM, 17(21), 2387-2393 (2003-10-31)
The combination of hydrogen exchange and mass spectrometry has been widely used in structural biology, providing views on protein structure and protein dynamics. One of the constraints is to use proteases working at low pH and low temperature to limit
E Ichishima et al.
The Biochemical journal, 339 ( Pt 3), 589-597 (1999-04-24)
For the construction of an overexpression system of the intracellular 1,2-alpha-mannosidase (EC 3.2.1.113) gene (msdS) from Aspergillus saitoi (now designated Aspergillus phoenicis), the N-terminal signal sequence of the gene was replaced with that of the aspergillopepsin I (EC 3.4.23.18) gene
Analysis of proteolytic degradation of a crude protein mixture using a surface acoustic wave sensor.
T M A Gronewold et al.
Biosensors & bioelectronics, 22(9-10), 2360-2365 (2006-11-03)
Degradation of a crude protein mixture by proteases with pH optima from acidic to basic was followed in real time using a surface acoustic wave biosensor in Love-wave geometry. Proteases EC 3.4.23.18 from Aspergillus saitoi, EC 3.4.21.62 from Bacillus licheniformis
Mizuho Nishinoaki et al.
Bioscience, biotechnology, and biochemistry, 72(2), 587-590 (2008-02-08)
An Aspergillus saitoi protease preparation, Molsin, was found to contain beta-glucosidase as well as protease activities. Application of Molsin to soybean curd improved its functionality by converting the contained isoflavone glycosides to their aglycones through beta-glucosidase, and also modified the
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
