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)
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.
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).
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_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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
Mizuho Nishinoaki et al.
Bioscience, biotechnology, and biochemistry, 72(2), 587-590 (2008-02-08)
An Aspergillus saitoi protease preparation, Molsin, was found to contain beta-glucosidase as well as protease activities. Application of Molsin to soybean curd improved its functionality by converting the contained isoflavone glycosides to their aglycones through beta-glucosidase, and also modified the
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
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.
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
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