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P2143

Sigma-Aldrich

Protease from Aspergillus saitoi

Type XIII, ≥0.6 unit/mg solid

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Synonym(s):
Molsin
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
32160410
NACRES:
NA.54

biological source

Aspergillus sp. (Aspergillus saitoi)

Quality Level

type

Type XIII

form

solid

specific activity

≥0.6 unit/mg solid

foreign activity

alkaline protease, essentially free

storage temp.

−20°C

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This Item
P403286247P3111
vibrant-m

P2143

Protease from Aspergillus saitoi

vibrant-m

P4032

Proteinase from Aspergillus melleus

vibrant-m

P3111

Protease from Bacillus sp.

biological source

Aspergillus sp. (Aspergillus saitoi)

biological source

Aspergillus sp. (A. melleus)

biological source

Aspergillus sp. (A. oryzae)

biological source

Bacillus sp.

form

solid

form

solid

form

powder

form

liquid

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

foreign activity

alkaline protease, essentially free

foreign activity

-

foreign activity

-

foreign activity

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

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.

Unit Definition

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).

pictograms

Exclamation markHealth hazard

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Customers Also Viewed

F J Moralejo et al.
Applied microbiology and biotechnology, 54(6), 772-777 (2001-01-11)
A gene encoding the sweet-tasting protein thaumatin (tha) with optimized codon usage was expressed in Aspergillus awamori. Mutants of A. awamori with reduced proteolytic activity were isolated. One of these mutants, named lpr66, contained an insertion of about 200 bp
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
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
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
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

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