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P2143

Sigma-Aldrich

Protease aus Aspergillus saitoi

Type XIII, ≥0.6 unit/mg solid

Synonym(e):

Molsin

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About This Item

CAS-Nummer:
9025-49-4
EC-Nummer:
3.4.23.18 (BRENDA, IUBMB)
EG-Nummer:
232-796-2
MDL-Nummer:
MFCD00132092
UNSPSC-Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

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Biologische Quelle

Aspergillus sp. (Aspergillus saitoi)

Typ

Type XIII

Form

solid

Spezifische Aktivität

≥0.6 unit/mg solid

Fremdaktivität

alkaline protease, essentially free

Lagertemp.

−20°C

Verwandte Kategorien

Anwendung

Protease from Aspergillus saitoi has been used in a study to assess sequence coverage and resolution in hydrogen exchange of large proteins. [1] It has also been used in a study to investigate the conversion of soybean curd isoflavone glycosides to their aglycones through β-glucosidase.. [2]

Biochem./physiol. Wirkung

Protease from Aspergillus saitoi was shown to also function as a β-glucosidase. [2]

Einheitendefinition

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).

Piktogramme

Health hazardExclamation mark
GHS08,GHS07

Signalwort

Danger

Gefahreneinstufungen

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

Zielorgane

Respiratory system

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

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Analysenzertifikate (COA)

Lot/Batch Number
0000323390
0000323389
0000323389
0000323390
0000273115

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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
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
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
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
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