P2143
Protease from Aspergillus saitoi
Type XIII, ≥0.6 unit/mg solid
Synonym(s):
Molsin
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About This Item
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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).
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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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
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
Isolation and characterization of mutants of Aspergillus niger deficient in extracellular proteases.
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
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
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.
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