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Key Documents

P2143

Sigma-Aldrich

Protease from Aspergillus saitoi

Type XIII, ≥0.6 unit/mg solid

Synonym(s):

Molsin

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

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

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

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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’.

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D W Burdon
Journal of medical microbiology, 29(2), 145-157 (1989-06-01)
A novel replicating agent (IFDO) was isolated from ileal fluid. Growth occurred in vitro under aerobic and anaerobic conditions, and was faster at 37 degrees C than at room temperature. The doubling time was 15.8 min. Colonies were dark brown
S W Cho et al.
Acta crystallographica. Section D, Biological crystallography, 57(Pt 7), 948-956 (2001-06-22)
The crystal structure of aspergillopepsin I (AP) from Aspergillus phoenicis has been determined at 2.18 A resolution and refined to R and R(free) factors of 21.5 and 26.0%, respectively. AP has the typical two beta-barrel domain structure of aspartic proteinases.
R E Cardoza et al.
Biotechnology and bioengineering, 83(3), 249-259 (2003-06-05)
A copy of the bovine chymosin gene (chy) with a codon usage optimized for its expression in Aspergillus awamori was constructed starting from synthetic oligonucleotides. To study the ability of this filamentous fungus to secrete bovine prochymosin, two plasmids were
E Skyttä et al.
The Journal of applied bacteriology, 74(2), 134-142 (1993-02-01)
The broad-spectrum antibacterial activity exhibited by three Pediococcus strains isolated from beer was preliminarily characterized. Factors affecting the production rate of bacterial inhibitors were screened and the effects of simultaneous cultivation of Lactococcus and Pediococcus on the production of inhibitory
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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