41493
Savinase® CLEA
≥8 U/g
Synonym(s):
Protease from Bacillus species, cross-linked enzyme aggregate
specific activity
≥8 U/g
Quality Level
General description
Savinase® a globular protein, is a serine protease that contains hydrophobic residues and metal-binding sites for Na+ and Ca+.
Application
Savinase® CLEA may be used as a serine protease for the proteolytic lysis of P. aeruginosa and S. aureus biofilms. It has also been used to treat S. cerevisiae cell wall samples for extraction of glycans.
Biochem/physiol Actions
Savinase® is a serine endopeptodase, which is responsible for stereoselective hydrolysis of amino esters and selective esters. It is mainly required for the hydrolysis of proteins and is used in transesterification and transpeptidation.
Savinase® stereoselective hydrolysis of selective as well as amino esters. It is bactericidal towards S. aureus strains. Savinase is stable in the pH range 7-10 and has potential industrial application for use in detergents.
Other Notes
1 U corresponds to the amount of enzyme which sets free 1 μmol folin-positive amino acids and peptides (as tyrosine) per minute at pH 8.0 and 37°C (casein as substrate)
Legal Information
Savinase is a registered trademark of Novozymes Corp.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Savinase is a bactericidal enzyme.
Edward M Smith et al.
Applied and environmental microbiology, 69(1), 719-720 (2003-01-07)
Elodie Lefebvre et al.
International journal of antimicrobial agents, 48(2), 181-188 (2016-07-19)
A multistep strategy was used to generate a combined antibiofilm treatment that could efficiently decrease the biomass of dense biofilms (≥6 × 10(7) CFU/cm(2)). Several compounds that exhibited activity against various targets were tested individually and in combination to search for possible synergistic
Abdul Razzaq et al.
Frontiers in bioengineering and biotechnology, 7, 110-110 (2019-07-03)
The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing
Adak Nasiripourdori et al.
International journal of biological macromolecules, 44(4), 311-315 (2008-10-29)
The industrial utilization of savinase is mainly constrained by its stability limitations. In the present study, the irreversible thermoinactivation of savinase has been evaluated at 70 degrees C, and various possible mechanisms for irreversible thermoinactivation of savinase were examined. The
Shanshan Wu et al.
PeerJ, 8, e9408-e9408 (2020-07-04)
Several examples have emerged of enzymes where slow conformational changes are of key importance for function and where low populated conformations in the resting enzyme resemble the conformations of intermediate states in the catalytic process. Previous work on the subtilisin
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