How is subtilisin produced?
How is subtilisin produced?
Subtilisin (EC 3.4. 21.62) is a type of serine protease that is of high commercial importance. It is mainly produced by Bacillus species as an extra cellular enzyme. Subtilisin being stable over a wide range of pH and temperature is exploited as a detergent enzyme and also favoured by its non-specificity.
Where does subtilisin cleave?
Subtilisin is a serine protease. A 77 amino acid propeptide is cleaved from the N-terminus of pro-Sub to create the mature active enzym.
What is Maxatase?
Maxatase is trademark of a protease used in laundry detergent. It is very similar to Alcalase. It is a subtilisin produced by Bacillus licheniformis.
Is subtilisin toxic?
In conclusion it can be said, that use of Subtilisin in laundry and cleaning products represents no safety concerns for consumers.
How is subtilisin used?
Protein-engineered subtilisins are widely used in commercial products (the native enzyme is easily inactivated by detergents and high temperatures) and is also called a stain cutter, for example, in laundry and dishwashing detergents, cosmetics, food processing, skin care ointments, contact lens cleaners, and for …
Why are chymotrypsin and subtilisin considered examples of convergent evolution?
Why are chymotrypsin and subtilisin considered examples of convergent evolution? -Because their polypeptide chains have different folds, and their active sites have different residues.
What is the purpose of serine?
Serine is a polar amino acid that plays a fundamental role in plant metabolism, plant development, and cell signalling. In addition to being a building block for proteins, Serine participates in the biosynthesis of biomolecules such as amino acids, nucleotides, phospholipids, and sphingolipids.
What is Anson unit?
Anson used denatured hemoglobin as a substrate for proteolytic enzymes in a Lowry assay. Thus, the term Anson units was popularized and mAnson Unit was defined as the amount of enzyme that liberates 1 μmol of TCA-soluble, Folin-positive amino acids within 1 minute at pH 7.5 and 37°C, using hemoglobin as a substrate.
What does the catalytic triad do?
The catalytic triad provides a paradigm for the structural and chemical features of enzymes that allow them to facilitate a difficult reaction. The reaction in this case is hydrolysis of a peptide bond, which – although thermodynamically favorable – is kinetically inaccessible under normal physiological conditions.
What is the structure of subtilisin?
The structure of subtilisin has been determined by X-ray crystallography. It is a 275-residue globular protein with several alpha-helices, and a large beta-sheet. It is structurally unrelated to the chymotrypsin-clan of serine proteases, but uses the same type of catalytic triad in the active site.
How many Cys residues are present in a subtilisin protein?
No Cys residues are present in the protein. Several crystal structures are available for subtilisins including subtilisin BPN′ [8,69–71], subtilisin Carlsberg [69,72], subtilisin 309 [21,73], and Bacillus alcalophilus subtilisin PB92 [74]. The subtilisin structures are highly superimposable, with an r.m.s. deviation of 0.4–0.7 Å [63,75].
Is subtilisin serine endopeptidase?
It is the type serine endopeptidase of MEROPS family S8. The structure of subtilisin has been determined by X-ray crystallography. The mature form is a 275-residue globular protein with several alpha-helices, and a large beta-sheet.
What is the origin of the name subtilisin?
The name subtilisin derives from the name of the bacterial species, Bacillus subtilis, from which the enzyme was first isolated [1,2]. Subtilisins are extracellular serine endopeptidases, and the term now encompasses the enzymes isolated from related Bacillus species as well.
