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Key Documents

P4860

Sigma-Aldrich

Protease from Bacillus licheniformis

≥2.4 U/g

Synonym(s):

Alcalase® 2.4L, Proteinase from Bacillus licheniformis, Subtilisin A

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

form

aqueous solution

specific activity

≥2.4 U/g

storage temp.

2-8°C

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General description

Proteolytic enzymes are known to possess catalytic, non-catalytic and ancillary domains. Proteases are broadly classified as endopeptidases and exopeptidases. Functionally they are divided as aspartic, glutamic, cysteine, threonine, serine and metalloproteases.

Application

Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. Protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. Protease is used in nucleic acid isolation procedures in incubations.
The enzyme from Sigma has been used to prepare chicken (leg) bone protein hydrolysates while evaluating ACE inhibitory peptides. It has also been used for the hydrolysis of Chlorella pyrenoidosa protein extracts during a study of their antitumor activities.

Biochem/physiol Actions

Alcalase is an endo-protease of the serine type. It has a broad substrate specificity and can hydrolyze most peptide bonds within a protein molecule. It is active between pH 6.5 and 8.5 and has an optimum temperature of 60 °C. The enzyme is is used in detergent formulations to remove protein-based stains.
Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate .

Analysis Note

Activity expressed in Anson Units

Legal Information

A product of Novozyme Corp.
Alcalase is a registered trademark of Novozymes Corp.

Signal Word

Danger

Hazard Statements

Hazard Classifications

Aquatic Acute 1 - Aquatic Chronic 2 - Eye Dam. 1 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Andrew R Hirst et al.
Nature chemistry, 2(12), 1089-1094 (2010-11-26)
Supramolecular gels, which demonstrate tunable functionalities, have attracted much interest in a range of areas, including healthcare, environmental protection and energy-related technologies. Preparing these materials in a reliable manner is challenging, with an increased level of kinetic defects observed at
Srinidhi Jayaraman et al.
The Journal of pharmacology and experimental therapeutics, 379(2), 191-202 (2021-08-15)
Neurolysin (Nln) is a recently recognized endogenous mechanism functioning to preserve the brain from ischemic injury. To further understand the pathophysiological function of this peptidase in stroke and other neurologic disorders, the present study was designed to identify small molecule
Catherine Cesa-Luna et al.
PloS one, 15(10), e0240545-e0240545 (2020-10-16)
The bacterial strain, EMM-1, was isolated from the rhizosphere of red maize ("Rojo Criollo") and identified as Pseudomonas protegens EMM-1 based on phylogenetic analysis of 16S rDNA, rpoB, rpoD, and gyrB gene sequences. We uncovered genes involved in the production
Keiichi Yokoyama et al.
Applied microbiology and biotechnology, 87(6), 2087-2096 (2010-06-04)
Microbial transglutaminase (MTG) has been used extensively in academic research and the food industries through its cross-linking or posttranslational modification of proteins. Two enzyme engineering approaches were applied to improve MTG activity. One is a novel method of rational mutagenesis
Proteases: multifunctional enzymes in life and disease
Lopez-Otin C and Bond JS
Test, 283(45), 30433-30437 (2008)

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