P2143
Protease from Aspergillus saitoi
Type XIII, ≥0.6 unit/mg solid
Synonym(s):
Molsin
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-796-2
NACRES:
NA.54
eCl@ss:
32160410
MDL number:
Specific activity:
≥0.6 unit/mg solid
Biological source:
Aspergillus sp. (Aspergillus saitoi)
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
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
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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
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
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