P1236
Protease from Bacillus amyloliquefaciens
liquid, ≥0.8 U/g
Synonym(s):
Neutrase® 0.8L
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About This Item
Recommended Products
biological source
Bacillus sp. (Bacillus amyloliquefaciens)
Quality Level
form
liquid
specific activity
≥0.8 U/g
storage temp.
2-8°C
General description
Bacterial protease produced by submerged fermentation of a selected strain of Bacillus amyloliquefaciens
Application
Protease from Bacillus amyloliquefaciens has been used for the unhairing of hides and skins. It has also been used in a study to investigate peptide bond formation using the carbamoylmethyl ester as the acyl donor.
Biochem/physiol Actions
Secretion of protease by Bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin.
Legal Information
A product of Novozyme Corp.
Neutrase is a registered trademark of Novozymes Corp.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Keqin Ou et al.
Journal of agricultural and food chemistry, 58(8), 4894-4900 (2010-03-17)
Effects of enzymatic hydrolysates of whey protein concentrates (WPC) on iron absorption were studied using in vitro digestion combined with Caco-2 cell models for improved iron absorption. Neutrase- and papain-treated WPC could improve iron absorption; especially hydrolysates by Neutrase could
Production of protease by Bacillus amyloliquefaciens in solid-state fermentation and its application in the unhairing of hides and skins
George, S., et al.
Process. Biochem., 30, 457-462 (1995)
Cerulenin Inhibits Production of Extracellular Proteins but not Membrane Proteins in Bacillus amyloliquefaciens.
Paton, J.
Journal of General Microbiology, 118, 179-187 (1980)
Toshifumi Miyazawa et al.
Protein and peptide letters, 15(10), 1050-1054 (2008-12-17)
Bacillus amyloliquefaciens protease-catalyzed peptide bond formation was investigated using the carbamoylmethyl (Cam) ester as the acyl donor. A series of N-protected L-amino acid Cam esters were coupled with an L-amino acid amide in acetonitrile in good to excellent yields. The
R Kammoun et al.
Bioresource technology, 90(3), 249-254 (2003-10-25)
Neutrase, used for hydrolysis of wheat proteins, was inhibited by end-product in a competitive uncompetitive way. The inhibition ratio depends on the progress of protein hydrolysis (degree of hydrolysis) and it remains constant beyond a degree of hydrolysis of 7.5%.
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