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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)

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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
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
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
I E Mattern et al.
Molecular & general genetics : MGG, 234(2), 332-336 (1992-08-01)
In the present study, the extracellular protease activity in a strain of the filamentous fungus Aspergillus niger was investigated and mutant strains deficient in the production of extracellular proteases were isolated. The major protease, which is responsible for 80-85% of

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