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P0107

Sigma-Aldrich

Protease from Rhizopus sp.

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CAS Number:
MDL number:
eCl@ss:
32160410
NACRES:
NA.54

description

acidic protease

form

powder

specific activity

≥0.2 unit/mg solid

storage temp.

2-8°C

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This Item
P0029P5380P0652
vibrant-m

P0107

Protease from Rhizopus sp.

vibrant-m

P0029

Protease from Bacillus sp.

vibrant-m

P0652

Protease from Streptomyces sp.

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

form

powder

form

granular

form

lyophilized powder

form

powder

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

description

acidic protease

description

-

description

-

description

-

General description

Exhibits both proteolytic and lipolytic activities.
Proteases are proteolytic enzymes that digests the proteins. It is classified into acidic, neutral and alkaline proteases based on their pH optimum. Proteases finds its applications in textile industries, laundry and healthcare. It is also being used in food processing industries such as baking and brewing. Rhizopus chinensis is the key species in the production of aspartate proteinase.
Stable in the acid range of pH 3-5. pH Optimum is 3.0.

application

Protease from Rhizopus sp. has been used in the enzyme treatment of planted and nonplanted scots pine seedlings.
Protease from Rhizopus spp. Has been used in a study to assess the amino acid sequences near the amino termini using automated Edman degradation. It has also been used in a study to investigate inactivation of the enzyme by reaction with diazoacetyl-DL-norleucine methyl ester in the presence of cupric acetate.

Biochem/physiol Actions

Protease from Rhizopus chinensis can be inhibited by pepstatin.

Unit Definition

One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 3.0 at 37 °C (color by Folin-Ciocalteu reagent), unless otherwise indicated.

Physical form

Supplied as a powder containing dextrin as a stabilizer

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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The structure and function of acid proteases. Specific inactivation of an acid protease from Rhizopus chinensis by diazoacetyl-DL-norleucine methyl ester.
F Mizobe et al.
Journal of biochemistry, 73(1), 61-68 (1973-01-01)
Characterization of proteases from Rhizopus species after growth on soybean protein
Heskamp ML and Barz W
Zeitschrift fur Naturforschung C, 52(9-10), 595-604 (1997)
The amino terminal sequences of acid proteases-human pepsin and gastricsin and the protease of Rhizopus chinensis.
P Sepulveda et al.
Biochemical and biophysical research communications, 63(4), 1106-1112 (1975-04-21)
J Marciniszyn et al.
The Journal of biological chemistry, 251(22), 7088-7094 (1976-11-25)
Four derivatives of pepstatin, each of which contains the unusual amino acid 4-amino-3-hydroxy-6-methylheptanoic acid (statine) have been prepared. All four are porcine pepsin inhibitors. Both N-acetylstatine and N-acetyl-alanyl-statine are competitive inhibitors for pepsin with Ki values of 1.2 X 10(-4)
Giovanni Caprioli et al.
Journal of chromatography. A, 1217(11), 1779-1785 (2010-02-09)
A new analytical method that uses high performance liquid chromatography-diode array detector (HPLC-DAD) was developed for the analysis of 14 benzimidazoles residues, including metabolites, in bovine liver. Samples were extracted using two different extraction procedures: with phosphate buffer after enzymatic

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