P0107
Protease from Rhizopus sp.
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About This Item
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description
acidic protease
form
powder
specific activity
≥0.2 unit/mg solid
storage temp.
2-8°C
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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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Brazilian Archives of Biology and Technology, 49(5), 843-851 (2006)
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.
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J Marciniszyn et al.
The Journal of biological chemistry, 251(22), 7088-7094 (1976-11-25)
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